US20170266306A1 - Targeted antimicrobial moieties - Google Patents

Abstract

This invention provides novel targeted antimicrobial compositions. In various embodiments chimeric moieties are provided comprising an antimicrobial peptide attached to a peptide targeting moiety that binds a bacterial strain or species.

Description

CROSS-REFERENCE TO RELATED APPLICATIONS
• This application is a Divisional of U.S. Ser. No. 14/255,858, filed Apr. 17, 2014, which is a Divisional of U.S. Ser. No. 12/683,160, filed Jan. 6, 2010 issued as U.S. Pat. No. 8,754,039 on Jun. 17, 2014, which claims benefit of and priority to U.S. Ser. No. 61/142,830, filed Jan. 6, 2009, U.S. Ser. No. 61/151,445, filed Feb. 10, 2009, U.S. Ser. No. 61/243,905, filed Sep. 18, 2009, and U.S. Ser. No. 61/243,930, filed Sep. 18, 2009, all of which are incorporated herein by reference in their entirety for all purposes.
STATEMENT OF GOVERNMENTAL SUPPORT
• [Not Applicable]
FIELD OF THE INVENTION
• The present invention relates to novel targeting peptides, novel antimicrobial peptides, chimeric moieties comprising novel targeting and/or novel antimicrobial peptides and uses thereof.
BACKGROUND OF THE INVENTION
• Antibiotic research at the industrial level was originally focused on the identification of refined variants of already existing drugs. This resulted example, in the development of antibiotics such as newer penicillins, cephalosporins, macrolides, and fluoroquinolones.
• However, resistance to old and newer antibiotics among bacterial pathogens is evolving rapidly, as exemplified by extended beta-lactamase (ESBL) and quinolone resistant gram-negatives, multi-resistant gonococci, methicillin resistant Staphylococcus aureus (MRSA), vancomycin resistant enterococci (VRE), penicillin non-susceptible pneumococci (PNSP) and macrolide resistant pneumococci and streptococci (see, e.g., Panlilo et al. (1992) Infect Control Hosp Epidemio., 13: 582-586; Morris et al. (1995) Ann Intern Me., d 123: 250-259, and the like). An overuse, or improper use, of antibiotics is believed to be of great importance for triggering and spread of drug resistant bacteria. Microbes have, in many cases, adapted and are resistant to antibiotics due to constant exposure and improper use of the drugs.
• Drug resistant pathogens represent a major economic burden for health-care systems. For example, postoperative and other nosocomial infections will prolong the need for hospital care and increase antibiotic drug expenses. It is estimated that the annual cost of treating drug resistant infections in the United States is approximately $5 billion.
SUMMARY OF THE INVENTION
• In certain embodiments, novel targeting moieties (e.g., peptides) that specifically/preferentially bind to microorganisms (e.g., certain bacteria, yeasts, fungi, molds, viruses, algae, protozoa, and the like) are provided. The targeting moieties can be attached to effectors (e.g., detectable labels, drugs, antimicrobial peptides, etc.) to form chimeric constructs for specifically/preferentially delivering the effector to and/or into the target organism. In certain embodiments novel antimicrobial peptides that can be used to inhibit (e.g., kill and/or inhibit growth and/or proliferation) of certain microorganisms (e.g., certain bacteria, yeasts, fungi, molds, viruses, algae, protozoa, and the like) are provided.
• Accordingly, in certain embodiments, a chimeric construct (chimeric moiety) is provided comprising: an effector attached to a peptide targeting moiety comprising an amino acid sequence found in Table 3 and/or Table 12; and/or an antimicrobial peptide comprising an amino acid sequence found in Table 4 and/or Table 5 attached to a targeting moiety. In certain embodiments the targeting moiety is a peptide comprising an amino acid sequence of a peptide found one or more of Table 3 and Table 12. In certain embodiments the targeting moiety is a peptide comprising two or more amino acid sequences of a peptide found one or more of Table 3 and Table 12. In certain embodiments the targeting moiety is a peptide whose amino acid sequence consists of the amino acid sequence of a peptide found in Table 3.
• In various embodiments the effector comprises a moiety selected from the group consisting of an antimicrobial peptide, an antibiotic, a ligand, a lipid or liposome, a agent that physically disrupts the extracellular matrix within a community of microorganisms, and a polymeric particle. In certain embodiments the effector comprises an antimicrobial peptide comprising an amino acid sequence found in one or more of Tables 4, 5, 14, and Table 15. In certain embodiments the effector comprises an antimicrobial peptide comprising an amino acid sequence found in one or more of Tables 4, and 5. In certain embodiments the effector comprises an antimicrobial peptide comprising an amino acid sequence characterized by a motif selected from the group consisting of KIF, FIK, KIH, HIK, and KIV (e.g., as identified in Table 7). In certain embodiments the construct comprises a targeting peptide comprising an amino acid sequence found in Table 3 attached to an antimicrobial peptide comprising an amino acid sequence found in Table 4 and/or Table 5. In certain embodiments the construct comprises an antimicrobial peptide comprising an amino acid sequence found in Table 4 attached to a targeting moiety comprising an amino acid sequence found in Table 3 and/or Table 10, and/or Table 12. In certain embodiments the construct comprises a targeting peptide comprising an amino acid sequence found in Table 3 attached to an antimicrobial peptide comprising an amino acid sequence found in Table 4.
• In various embodiments the targeting moiety is chemically conjugated to the effector (directly or via a linker). In certain embodiments the liker comprises a polyethylene glycol (PEG). In certain embodiments the targeting moiety is chemically conjugated to the effector via a non-peptide linker found in Table 16. In certain embodiments the targeting moiety is linked to the effector via a peptide linkage. In certain embodiments the effector comprises an antimicrobial peptide and the construct is a fusion protein. In certain embodiments the targeting moiety is attached to the effector by a peptide linker comprising or consisting of an amino acid sequence found in Table 16. In certain embodiments any of the constructs and/or peptides described herein bears one or more protecting groups. In certain embodiments the one or more protecting groups are independently selected from the group consisting of acetyl, amide, 3 to 20 carbon alkyl groups, fmoc, tboc, 9-fluoreneacetyl group, 1-fluorenecarboxylic group, 9-florenecarboxylic group, 9-fluorenone-1-carboxylic group, benzyloxycarbonyl, xanthyl (Xan), trityl (Trt), 4-methyltrityl (Mtt), 4-methoxytrityl (Mmt), 4-methoxy-2,3,6-trimethyl-benzenesulphonyl (Mtr), mesitylene-2-sulphonyl (Mts), 4,4-dimethoxybenzhydryl (Mbh), tosyl (Tos), 2,2,5,7,8-pentamethyl chroman-6-sulphonyl (Pmc), 4-methylbenzyl (MeBzl), 4-methoxybenzyl (MeOBzl), benzyloxy (BzlO), benzyl (Bzl), benzoyl (Bz), 3-nitro-2-pyridinesulphenyl (Npys), 1-(4,4-dimentyl-2,6-diaxocyclohexylidene)ethyl (Dde), 2,6-dichlorobenzyl (2,6-DiCl-Bzl), 2-chlorobenzyloxycarbonyl (2-Cl—Z), 2-bromobenzyloxycarbonyl (2-Br—Z), benzyloxymethyl (Bom), t-butoxycarbonyl (Boc), cyclohexyloxy (cHxO), t-butoxymethyl (Bum), t-butoxy (tBuO), t-Butyl (tBu), and trifluoroacetyl (TFA). In certain embodiments the peptide and/or construct comprises a protecting group at a carboxyl and/or amino terminus. In certain embodiments the carboxyl terminus is amidated and/or the amino terminus is acetylated. In various embodiments the chimeric construct and/or peptide is functionalized with a polymer (e.g., comprises polyethylene glycol, cellulose, modified cellulose, dextrin, etc.) to increase serum halflife.
• In certain embodiments pharmaceutical compositions are provided. In various embodiments the pharmaceutical compositions comprise a chimeric construct as described herein (e.g., a chimeric construct according to any of claims 1-26) and/or an antimicrobial peptide as described herein, in a pharmaceutically acceptable carrier. In certain embodiments the composition is formulated as a unit dosage formulation. In certain embodiments the composition is formulated for administration by a modality selected from the group consisting of intraperitoneal administration, topical administration, oral administration, inhalation administration, transdermal administration, subdermal depot administration, systemic IV application, ocular administration, and rectal administration.
• In certain embodiments isolated antimicrobial peptides are provided. In various embodiments the peptides comprise one or more sequences selected from the amino acid sequences listed in Table 4 and/or Table 5 (and/or the retro, inverso, retroinverso, or beta forms). In various embodiments the antimicrobial peptide bears one or more protecting groups e.g., as described herein.
• In certain embodiments a composition effective to kill or to inhibit the growth and/or of a microorganism and/or the formation and/or maintenance of a biofilm is provided. The composition typically comprises one or more isolated antimicrobial peptides, the amino acid sequences of the peptides comprising one or more sequences selected from the amino acid sequences listed in Table 4 and/or Table 5 (and/or their retro, inverso, or retroinverso forms). In certain embodiments the composition is effective to kill or inhibit the growth and/or proliferation of a yeast or fungus, and the composition comprises one or more peptides, the amino acid sequences of the peptides comprising one or more sequences selected from the group of amino acid sequences listed in Table 4 and/or Table 5 identified (e.g., in those tables) as effective to effective to kill or inhibit the growth and/or proliferation of a yeast or fungus. In certain embodiments the composition is effective to kill or inhibit the growth and/or proliferation of Aspergillus niger and the composition comprises one or more peptides, the amino acid sequences of the peptides comprising one or more sequences selected from the group of amino acid sequences listed in Table 4 and/or Table 5 identified as effective to effective to kill or inhibit the growth and/or proliferation of Aspergillus niger. In certain embodiments the composition is effective to kill or inhibit the growth and/or proliferation of C. albicans and the composition comprises one or more peptides, the amino acid sequences of the peptides comprising one or more sequences selected from the group of amino acid sequences listed in Table 4 and/or Table 5 identified as effective to effective to kill or inhibit the growth and/or proliferation of C. albicans. In certain embodiments the composition is effective to kill or inhibit the growth and/or proliferation of T. rubrum and the composition comprises one or more peptides, the amino acid sequences of the peptides comprising one or more sequences selected from the group of amino acid sequences listed in Table 4 and/or Table 5 identified as effective to effective to kill or inhibit the growth and/or proliferation of T. rubrum. In certain embodiments the composition is effective to kill or inhibit the growth and/or proliferation of a bacterium, and the composition comprises one or more peptides, the amino acid sequences of the peptides comprising one or more sequences selected from the group of amino acid sequences listed in Table 4 and/or Table 5 identified as effective to effective to kill or inhibit the growth and/or proliferation of a bacterium. In certain embodiments the composition is effective to kill or inhibit the growth and/or proliferation of a gram positive bacterium, and the composition comprises one or more peptides, the amino acid sequences of the peptides comprising one or more sequences selected from the group of amino acid sequences listed in Table 4 and/or Table 5 identified as effective to effective to kill or inhibit the growth and/or proliferation of a gram positive bacterium. In certain embodiments the composition is effective to kill or inhibit the growth and/or proliferation of A. naeslundii, and the composition comprises one or more peptides, the amino acid sequences of the peptides comprising one or more sequences selected from the group of amino acid sequences listed in Table 4 and/or Table 5 identified as effective to effective to kill or inhibit the growth and/or proliferation of A. naeslundii. In certain embodiments the composition is effective to kill or inhibit the growth and/or proliferation of B. subtilis, and the composition comprises one or more peptides, the amino acid sequences of the peptides comprising one or more sequences selected from the group of amino acid sequences listed in Table 4 and/or Table 5 identified as effective to effective to kill or inhibit the growth and/or proliferation of B. subtilis. In certain embodiments the composition is effective to kill or inhibit the growth and/or proliferation of C. difficile, and the composition comprises one or more peptides, the amino acid sequences of the peptides comprising one or more sequences selected from the group of amino acid sequences listed in Table 4 and/or Table 5 identified as effective to effective to kill or inhibit the growth and/or proliferation of C. difficile. In certain embodiments the composition is effective to kill or inhibit the growth and/or proliferation of C. jeikeium, and the composition comprises one or more peptides, the amino acid sequences of the peptides comprising one or more sequences selected from the group of amino acid sequences listed in Table 4 and/or Table 5 identified as effective to effective to kill or inhibit the growth and/or proliferation of C. jeikeium. In certain embodiments the composition is effective to kill or inhibit the growth and/or proliferation of E. faecalis, and the composition comprises one or more peptides, the amino acid sequences of the peptides comprising one or more sequences selected from the group of amino acid sequences listed in Table 4 and/or Table 5 identified as effective to effective to kill or inhibit the growth and/or proliferation of E. faecalis. In certain embodiments the composition is effective to kill or inhibit the growth and/or proliferation of M. luteus, and the composition comprises one or more peptides, the amino acid sequences of the peptides comprising one or more sequences selected from the group of amino acid sequences listed in Table 4 and/or Table 5 identified as effective to effective to kill or inhibit the growth and/or proliferation of M. luteus. In certain embodiments the composition is effective to kill or inhibit the growth and/or proliferation of MRSA, and the composition comprises one or more peptides, the amino acid sequences of the peptides comprising one or more sequences selected from the group of amino acid sequences listed in Table 4 and/or Table 5 identified as effective to effective to kill or inhibit the growth and/or proliferation of MRSA. In certain embodiments composition is effective to kill or inhibit the growth and/or proliferation of S. epidermidis, and the composition comprises one or more peptides, the amino acid sequences of the peptides comprising one or more sequences selected from the group of amino acid sequences listed in Table 4 and/or Table 5 identified as effective to effective to kill or inhibit the growth and/or proliferation of S. epidermidis. In certain embodiments the composition is effective to kill or inhibit the growth and/or proliferation of S. mutans, and the composition comprises one or more peptides, the amino acid sequences of the peptides comprising one or more sequences selected from the group of amino acid sequences listed in Table 4 and/or Table 5 identified as effective to effective to kill or inhibit the growth and/or proliferation of S. mutans. In certain embodiments the composition is effective to kill or inhibit the growth and/or proliferation of S. pneumoniae, and the composition comprises one or more peptides, the amino acid sequences of the peptides comprising one or more sequences selected from the group of amino acid sequences listed in Table 4 and/or Table 5 identified as effective to effective to kill or inhibit the growth and/or proliferation of S. pneumoniae. In certain embodiments the composition is effective to kill or inhibit the growth and/or proliferation of a gram negative bacterium, and the composition comprises one or more peptides, the amino acid sequences of the peptides comprising one or more sequences selected from the group of amino acid sequences listed in Table 4 and/or Table 5 identified as effective to effective to kill or inhibit the growth and/or proliferation of a gram negative bacterium. In certain embodiments the composition is effective to kill or inhibit the growth and/or proliferation of A. baumannii, and the composition comprises one or more peptides, the amino acid sequences of the peptides comprising one or more sequences selected from the group of amino acid sequences listed in Table 4 and/or Table 5 identified as effective to effective to kill or inhibit the growth and/or proliferation of A. baumannii. In certain embodiments the composition is effective to kill or inhibit the growth and/or proliferation of C. jejuni, and the composition comprises one or more peptides, the amino acid sequences of the peptides comprising one or more sequences selected from the group of amino acid sequences listed in Table 4 and/or Table 5 identified as effective to effective to kill or inhibit the growth and/or proliferation of C. jejuni. In certain embodiments the composition is effective to kill or inhibit the growth and/or proliferation of E. coli, and the composition comprises one or more peptides, the amino acid sequences of the peptides comprising one or more sequences selected from the group of amino acid sequences listed in Table 4 and/or Table 5 identified as effective to effective to kill or inhibit the growth and/or proliferation of E. coli. In certain embodiments the composition is effective to kill or inhibit the growth and/or proliferation of F. nucleatum, and the composition comprises one or more peptides, the amino acid sequences of the peptides comprising one or more sequences selected from the group of amino acid sequences listed in Table 4 and/or Table 5 identified as effective to effective to kill or inhibit the growth and/or proliferation of F. nucleatum. In certain embodiments the composition is effective to kill or inhibit the growth and/or proliferation of E. coli, and the composition comprises one or more peptides, the amino acid sequences of the peptides comprising one or more sequences selected from the group of amino acid sequences listed in Table 4 and/or Table 5 identified as effective to effective to kill or inhibit the growth and/or proliferation of M. xanthus. In certain embodiments the composition is effective to kill or inhibit the growth and/or proliferation of P. aeruginosa, and the composition comprises one or more peptides, the amino acid sequences of the peptides comprising one or more sequences selected from the group of amino acid sequences listed in Table 4 and/or Table 5 identified as effective to effective to kill or inhibit the growth and/or proliferation of P. aeruginosa. In certain embodiments the composition is effective to kill or inhibit the growth and/or proliferation of P. gingivalis, and the composition comprises one or more peptides, the amino acid sequences of the peptides comprising one or more sequences selected from the group of amino acid sequences listed in Table 4 and/or Table 5 identified as effective to effective to kill or inhibit the growth and/or proliferation of P. gingivalis. In certain embodiments the composition is effective to kill or inhibit the growth and/or proliferation of P. mirabilis, and the composition comprises one or more peptides, the amino acid sequences of the peptides comprising one or more sequences selected from the group of amino acid sequences listed in Table 4 and/or Table 5 identified as effective to effective to kill or inhibit the growth and/or proliferation of P. mirabilis.
• In various embodiments one or more of the peptides comprising the composition comprise all “L” amino acids or all “D” amino acids, or a mixture of “L” and “D” amino acids. In various embodiments one or more of the peptides comprising the composition are β peptides. In various embodiments one or more of the peptides comprising the composition comprise one or more protecting groups (e.g. protected carboxyl and/or amino termini). In various embodiments one or more of the peptides comprising the composition comprise an amide on the carboxyl terminus and/or an acetyl on the amino terminus. In various embodiments the peptides comprising the composition are in a pharmaceutically acceptable carrier. In certain embodiments the carrier is suitable for administration via a route selected from the group consisting of topical administration, aerosol administration, administration via inhalation, oral administration, and/or rectal administration.
• In various embodiments methods are provided for killing and/or inhibiting the growth and/or proliferation of a microorganism and or for disrupting and/or inhibiting the growth and/or maintenance of a biofilm, the method comprising contacting the microorganism (or a biofilm comprising the microorganism) with a chimeric construct as described herein (e.g., see description above, and/or a chimeric construct according to any one of claims 1-29), or with an antimicrobial peptide as described herein, and/or with a composition as described herein (e.g., a composition according to any one of claims 30-65). In certain embodiments the microorganism is a yeast or fungus and the chimeric construct or composition is a chimeric construct comprising an effector identified as killing a yeast or fungus, or a composition comprising an antimicrobial peptide described herein as killing a yeast or fungus. In certain embodiments the microorganism is a bacterium (e.g., gram negative and/or gram positive bacterium) and the chimeric construct or composition is a chimeric construct comprising an effector identified as killing a bacterium (e.g., gram negative and/or gram positive bacterium), or a composition comprising an antimicrobial peptide described herein as killing a gram negative and/or gram positive bacterium. In certain embodiments the effector is an antimicrobial peptide. In certain embodiments he microorganism is S. mutans, and the chimeric construct or composition is applied to the oral cavity of an animal or human, e.g., to reduces the incidence or severity of dental caries and/or periodontal disease). In certain embodiments the chimeric construct or composition preferentially targets Corynebacterium spp. and the chimeric construct or composition is applied to the skin surface of an animal or human (e.g., to reduce body odor).
• Methods are also provided for disinfecting a surface. The methods typically involve contacting the surface with one or more chimeric constructs described herein (e.g. a construct according to any one of claims 1-29), or a composition as described herein (e.g., a composition according to any one of claims 30-65). In certain embodiments, the surface comprises a surface of a prosthesis or medical implant. In certain embodiments the surface comprises a surface of a medical device. In certain embodiments the surface comprises a surface of a plant or foodstuff. In certain embodiments the chimeric construct and/or the antimicrobial peptide(s) are combined with a second disinfectant selected from the group consisting of other antimicrobial agent is a disinfectant selected from the group consisting of acetic acid, phosphoric acid, citric acid, lactic, formic, propionic acid, hydrochloric acid, sulfuric acid, nitric acid, sodium hydroxide, potassium hydroxide, sodium carbonate, ammonium hydroxide, ethyl alcohol, isopropyl alcohol, phenol, formaldehyde, glutaraldehyde, hypochlorites, chlorine dioxide, sodium dichloroisocyanurate, chloramine-T, iodine, povidone-iodine, chlorhexidine, hydrogen peroxide, peracetic acid, and benzalkonium chloride.
• In various embodiments the use of a chimeric construct described herein and/or an antimicrobial composition as described herein (e.g., a chimeric construct according to any one of claims 1-29, or a composition according to any one of claims 30-65) in the manufacture of a medicament for killing and/or inhibiting the growth and/or proliferation of a microorganism and/or inhibiting the growth and/or maintenance of a biofilm comprising the microorganism is provided. In certain embodiments the microorganism is a yeast or fungus and the chimeric construct or composition is a chimeric construct comprising an effector identified as killing a yeast or fungus, or a composition comprising an antimicrobial peptide described herein as killing a yeast or fungus. In certain embodiments the microorganism is a bacterium (e.g., gram negative and/or gram positive bacterium) and the chimeric construct or composition is a chimeric construct comprising an effector identified as killing a bacterium (e.g., gram negative and/or gram positive bacterium), or a composition comprising an antimicrobial peptide described herein as killing a gram negative and/or gram positive bacterium. In certain embodiments the effector is an antimicrobial peptide.
• In various embodiments methods are also provided for of detecting a bacterium and/or a bacterial film (e.g., a biofilm comprising the bacteria). The methods typically involve contacting the bacterium or bacterial film with a composition comprising a detectable label attached to a targeting peptide comprising one or more amino acid sequences found Table 3 and/or Table 12; and detecting the detectable label where the quantity and/or location of the detectable label is an indicator of the presence of the bacterium and/or bacterial film. In certain embodiments the targeting peptide comprises or consists of an amino acid sequence of a peptide found in Table 3 (and/or the retro, inverso, retroinverso form of the sequence). In certain embodiments the detectable label is a label selected from the group consisting of a radioactive label, a radio-opaque label, a fluorescent dye, a fluorescent protein, an enzymatic label, a colorimetric label, and a quantum dot.
• Certain compositions are also provided comprising a photosensitizing or photoactivatable agent attached to a targeting peptide (e.g., a peptide comprising an amino acid sequence of a peptide found in Table 3 and/or Table 12). In certain embodiments the targeting peptide comprises or consists of an amino acid sequence of a peptide found in Table 3. In certain embodiments the photosensitizing agent is an agent selected from the group consisting of a porphyrinic macrocycle, a porphyrin, a chlorine, a crown ether, an acridine, an azine, a phthalocyanine, a cyanine, a psoralen, a cucumin, and a perylenequinonoid. In certain embodiments the photosensitizing agent comprises one or more agents agent shown in any of FIGS. 1-12. In certain embodiments the photosensitizing agent is attached to the targeting peptide by a non-peptide linker (e.g., a polyethylene glycol (PEG)). In certain embodiments the photosensitizing agent is attached to the targeting peptide by a non-peptide linker found in Table 16.
• In various embodiments methods are provided for killing and/or for inhibiting the growth and/or proliferation of a microorganism or a biofilm comprising a microorganism, where the methods involve contacting the microorganism or biofilm with a composition comprising a photosensitizing or photoactivatable agent attached to a targeting peptide (e.g., a peptide comprising an amino acid sequence of a peptide found in Table 3 and/or Table 12). In certain embodiments the targeting peptide comprises or consists of an amino acid sequence of a peptide found in Table 3. In certain embodiments the photosensitizing agent is an agent selected from the group consisting of a porphyrinic macrocycle, a porphyrin, a chlorine, a crown ether, an acridine, an azine, a phthalocyanine, a cyanine, a psoralen, a cucumin, and a perylenequinonoid. In certain embodiments the photosensitizing agent comprises one or more agents agent shown in any of FIGS. 1-12. In certain embodiments the photosensitizing agent is attached to the targeting peptide by a non-peptide linker (e.g., a polyethylene glycol (PEG)). In certain embodiments the photosensitizing agent is attached to the targeting peptide by a non-peptide linker found in Table 16. In certain embodiments the method further comprises exposing the microorganism or biofilm to a light source. In certain embodiments the microorganism is a microorganism selected from the group consisting of a bacterium (e.g., a gram positive and/or a gram negative bacterium), a yeast, a fungus, a protozoan, and a virus. In certain embodiments the biofilm comprises a bacterial film. In certain embodiments the biofilm is a biofilm on an implanted or implantable medical device. In certain embodiments the microorganism or biofilm is an organism or biofilm in an oral cavity.
• In various embodiments certain formulations are provided. Typical formulations include, but are not limited to a targeting peptide, an antimicrobial peptide, and/or a STAMP; and a salt at a concentration comparable to that found in phosphate buffered saline (PBS) ranging from about 0.5×PBS to about 2.5×PBS. In certain embodiments the formulation comprises a targeting peptide found in Tables 3 or 10. In certain embodiments the formulation comprises an anti-S. mutans peptide targeting peptide (e.g., as identified in Tables 3 or 12). In certain embodiments the anti-S. mutans targeting peptide has the amino acid sequence TFFRLFNRSFTQALGK (SEQ ID NO:1). In certain embodiments the anti-S. mutans targeting peptide is attached to an antimicrobial peptide. In certain embodiments the antimicrobial peptide is a peptide found in Tables 4, 5, or 14. In certain embodiments the antimicrobial peptide has the amino acid sequence KNLRIIRKGIHIIKKY (SEQ ID NO:3080). In certain embodiments the formulation comprises the amino acid sequence of the C16G2 STAMP (TFFRLFNRSFTQALGKGGGKNLRIIRKGIHIIKKY, (SEQ ID NO:2). In various embodiments the targeting peptide, antimicrobial peptide, and/or a STAMP bears one or more protecting groups. In certain embodiments the protecting group(s) are independently selected from the group consisting of acetyl, amide, 3 to 20 carbon alkyl groups, Fmoc, Tboc, 9-fluoreneacetyl group, 1-fluorenecarboxylic group, 9-florenecarboxylic group, 9-fluorenone-1-carboxylic group, benzyloxycarbonyl, Xanthyl (Xan), Trityl (Trt), 4-methyltrityl (Mtt), 4-methoxytrityl (Mmt), 4-methoxy-2,3,6-trimethyl-benzenesulphonyl (Mtr), Mesitylene-2-sulphonyl (Mts), 4,4-dimethoxybenzhydryl (Mbh), Tosyl (Tos), 2,2,5,7,8-pentamethyl chroman-6-sulphonyl (Pmc), 4-methylbenzyl (MeBzl), 4-methoxybenzyl (MeOBzl), Benzyloxy (BzlO), Benzyl (Bzl), Benzoyl (Bz), 3-nitro-2-pyridinesulphenyl (Npys), 1-(4,4-dimentyl-2,6-diaxocyclohexylidene)ethyl (Dde), 2,6-dichlorobenzyl (2,6-DiCl-Bzl), 2-chlorobenzyloxycarbonyl (2-Cl—Z), 2-bromobenzyloxycarbonyl (2-Br—Z), Benzyloxymethyl (Born), t-butoxycarbonyl (Boc), cyclohexyloxy (cHxO), t-butoxymethyl (Bum), t-butoxy (tBuO), t-Butyl (tBu), and Trifluoroacetyl (TFA). In certain embodiments the targeting peptide, antimicrobial peptide, and/or a STAMP is amidated at the carboxyl terminus and/or bears an acetyl group at the amino terminus. In certain embodiments the pH of the formulation ranges from about pH 5.0 to about pH 8.5. In certain embodiments the pH is about pH 7.4. In various embodiments the salt is at a concentration comparable to that found in 1×PBS. In certain embodiments the formulation comprises PBS. In certain embodiments the formulation of further comprising ethanol, and/or glycerin, and/or polyethylene glycol, and/or fluoride.
Definitions
• The term “peptide” as used herein refers to a polymer of amino acid residues typically ranging in length from 2 to about 50 or about 60 residues. In certain embodiments the peptide ranges in length from about 2, 3, 4, 5, 7, 9, 10, or 11 residues to about 60, 50, 45, 40, 45, 30, 25, 20, or 15 residues. In certain embodiments the peptide ranges in length from about 8, 9, 10, 11, or 12 residues to about 15, 20 or 25 residues. In certain embodiments the amino acid residues comprising the peptide are “L-form” amino acid residues, however, it is recognized that in various embodiments, “D” amino acids can be incorporated into the peptide. Peptides also include amino acid polymers in which one or more amino acid residues is an artificial chemical analogue of a corresponding naturally occurring amino acid, as well as to naturally occurring amino acid polymers. In addition, the term applies to amino acids joined by a peptide linkage or by other, “modified linkages” (e.g., where the peptide bond is replaced by an α-ester, a β-ester, a thioamide, phosphonamide, carbonate, hydroxylate, and the like (see, e.g., Spatola, (1983) Chem. Biochem. Amino Acids and Proteins 7: 267-357), where the amide is replaced with a saturated amine (see, e.g., Skiles et al., U.S. Pat. No. 4,496,542, which is incorporated herein by reference, and Kaltenbronn et al., (1990) Pp. 969-970 in Proc. 11th American Peptide Symposium, ESCOM Science Publishers, The Netherlands, and the like)).
• The term “residue″” as used herein refers to natural, synthetic, or modified amino acids. Various amino acid analogues include, but are not limited to 2-aminoadipic acid, 3-aminoadipic acid, beta-alanine (beta-aminopropionic acid), 2-aminobutyric acid, 4-aminobutyric acid, piperidinic acid, 6-aminocaproic acid, 2-aminoheptanoic acid, 2-aminoisobutyric acid, 3-aminoisobutyric acid, 2-aminopimelic acid, 2,4 diaminobutyric acid, desmosine, 2,2′-diaminopimelic acid, 2,3-diaminopropionic acid, n-ethylglycine, n-ethylasparagine, hydroxylysine, allo-hydroxylysine, 3-hydroxyproline, 4-hydroxyproline, isodesmosine, allo-isoleucine, n-methylglycine, sarcosine, n-methylisoleucine, 6-n-methyllysine, n-methylvaline, norvaline, norleucine, ornithine, and the like. These modified amino acids are illustrative and not intended to be limiting.
• “β-peptides” comprise of “β amino acids”, which have their amino group bonded to the β carbon rather than the α-carbon as in the 20 standard biological amino acids. The only commonly naturally occurring β amino acid is β-alanine.
• Peptoids, or N-substituted glycines, are a specific subclass of peptidomimetics. They are closely related to their natural peptide counterparts, but differ chemically in that their side chains are appended to nitrogen atoms along the molecule's backbone, rather than to the α-carbons (as they are in natural amino acids).
• The terms “conventional” and “natural” as applied to peptides herein refer to peptides, constructed only from the naturally-occurring amino acids: Ala, Cys, Asp, Glu, Glu, Phe, Gly, His, Ile, Lys, Leu, Met, Asn, Pro, Gln, Arg, Ser, Thr, Val, Trp, and Tyr. A compound of the invention “corresponds” to a natural peptide if it elicits a biological activity (e.g., antimicrobial activity) related to the biological activity and/or specificity of the naturally occurring peptide. The elicited activity may be the same as, greater than or less than that of the natural peptide. In general, such a peptoid will have an essentially corresponding monomer sequence, where a natural amino acid is replaced by an N-substituted glycine derivative, if the N-substituted glycine derivative resembles the original amino acid in hydrophilicity, hydrophobicity, polarity, etc. The following are illustrative, but non-limiting N-substituted glycine replacements: N-(1-methylprop-1-yl)glycine substituted for isoleucine (Ile), N-(prop-2-yl)glycine for valine (Val), N-benzylglycine for phenylanlaine (Phe), N-(2-hydroxyethyl)glycine for serine (Ser), and the like. In certain embodiments substitutions need not be “exact”. Thus for example, in certain embodiments N-(2-hydroxyethyl)glycine may substitute for Ser, Thr, Cys, and/or Met; N-(2-methylprop-1-yl)glycine may substitute for Val, Leu, and/or Ile. In certain embodiments N-(2-hydroxyethyl)glycine can be used to substitute for Thr and Ser, despite the structural differences: the side chain in N-(2-hydroxyethyl)glycine is one methylene group longer than that of Ser, and differs from Thr in the site of hydroxy-substitution. In general, one may use an N-hydroxyalkyl-substituted glycine to substitute for any polar amino acid, an N-benzyl- or N-aralkyl-substituted glycine to replace any aromatic amino acid (e.g., Phe, Trp, etc.), an N-alkyl-substituted glycine such as N-butylglycine to replace any nonpolar amino acid (e.g., Leu, Val, Ile, etc.), and an N-(aminoalkyl)glycine derivative to replace any basic polar amino acid (e.g., Lys and Arg).
• Where an amino acid sequence is provided herein, L-, D-, or beta amino acid versions of the sequence are also contemplated as well as retro, inversion, and retro-inversion isoforms. In addition, conservative substitutions (e.g., in the binding peptide, and/or antimicrobial peptide, and/or linker peptide) are contemplated. Non-protein backbones, such as PEG, alkane, ethylene bridged, ester backbones, and other backbones are also contemplated. Also fragments ranging in length from about 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, or 25 amino acids up to the full length minus one amino acid of the peptide are contemplated where the fragment retains at least 50%, preferably at least 60% 70% or 80%, more preferably at least 90%, 95%, 98%, 99%, or at least 100% of the activity (e.g., binding specificity and/or avidity, antimicrobial activity, etc.) of the full length peptide are contemplated.
• A “compound antimicrobial peptide” or “compound AMP” refers to a construct comprising two or more AMPs joined together. The AMPs can be joined directly or through a linker. They can be chemically conjugated or, where joined directly together or through a peptide linker can comprise a fusion protein.
• In certain embodiments, conservative substitutions of the amino acids comprising any of the sequences described herein are contemplated. In various embodiments one, two, three, four, or five different residues are substituted. The term “conservative substitution” is used to reflect amino acid substitutions that do not substantially alter the activity (e.g., antimicrobial activity and/or specificity) of the molecule. Typically conservative amino acid substitutions involve substitution one amino acid for another amino acid with similar chemical properties (e.g. charge or hydrophobicity). Certain conservative substitutions include “analog substitutions” where a standard amino acid is replaced by a non-standard (e.g., rare, synthetic, etc) amino acid differing minimally from the parental residue. Amino acid analogs are considered to be derived synthetically from the standard amino acids without sufficient change to the structure of the parent, are isomers, or are metabolite precursors. Examples of such “analog substitutions” include, but are not limited to, 1) Lys-Orn, 2) Leu-Norleucine, 3) Lys-Lys[TFA], 4) Phe-Phe[Gly], and 5) δ-amino butylglycine-ξ-amino hexylglycine, where Phe[gly] refers to phenylglycine (a Phe derivative with a H rather than CH₃ component in the R group), and Lys[TFA] refers to a Lys where a negatively charged ion (e.g., TFA) is attached to the amine R group. Other conservative substitutions include “functional substitutions” where the general chemistries of the two residues are similar, and can be sufficient to mimic or partially recover the function of the native peptide. Strong functional substitutions include, but are not limited to 1) Gly/Ala, 2) Arg/Lys, 3) Ser/Tyr/Thr, 4) Leu/Ile/Val, 5) Asp/Glu, 6) Gln/Asn, and 7) Phe/Trp/Tyr, while other functional substitutions include, but are not limited to 8) Gly/Ala/Pro, 9) Tyr/His, 10) Arg/Lys/His, 11) Ser/Thr/Cys, 12) Leu/Ile/Val/Met, and 13) Met/Lys (special case under hydrophobic conditions). Various “broad conservative substations” include substitutions where amino acids replace other amino acids from the same biochemical or biophysical grouping. This is similarity at a basic level and stems from efforts to classify the original 20 natural amino acids. Such substitutions include 1) nonpolar side chains: Gly/Ala/Val/Leu/Ile/Met/Pro/Phe/Trp, and/or 2) uncharged polar side chains Ser/Thr/Asn/Gln/Tyr/Cys. In certain embodiments broad-level substitutions can also occur as paired substitutions. For example, Any hydrophilic neutral pair [Ser, Thr, Gln, Asn, Tyr, Cys]+[Ser, Thr, Gln, Asn, Tyr, Cys] can may be replaced by a charge-neutral charged pair [Arg, Lys, His]+[Asp, Glu]. The following six groups each contain amino acids that, in certain embodiments, are typical conservative substitutions for one another: 1) Alanine (A), Serine (S), Threonine (T); 2) Aspartic acid (D), Glutamic acid (E); 3) Asparagine (N), Glutamine (Q); 4) Arginine (R), Lysine (K), Histidine (H); 5) Isoleucine (I), Leucine (L), Methionine (M), Valine (V); and 6) Phenylalanine (F), Tyrosine (Y), Tryptophan (W). Where amino acid sequences are disclosed herein, amino acid sequences comprising, one or more of the above-identified conservative substitutions are also contemplated.
• In certain embodiments, targeting peptides, antimicrobial peptides, and/or STAMPs compromising at least 80%, preferably at least 85% or 90%, and more preferably at least 95% or 98% sequence identity with any of the sequences described herein are also contemplated. The terms “identical” or percent “identity,” refer to two or more sequences that are the same or have a specified percentage of amino acid residues that are the same, when compared and aligned for maximum correspondence, as measured using one of the following sequence comparison algorithms or by visual inspection. With respect to the peptides of this invention sequence identity is determined over the full length of the peptide. For sequence comparison, typically one sequence acts as a reference sequence, to which test sequences are compared. When using a sequence comparison algorithm, test and reference sequences are input into a computer, subsequence coordinates are designated, if necessary, and sequence algorithm program parameters are designated. The sequence comparison algorithm then calculates the percent sequence identity for the test sequence(s) relative to the reference sequence, based on the designated program parameters. Optimal alignment of sequences for comparison can be conducted, e.g., by the local homology algorithm of Smith & Waterman (1981) Adv. Appl. Math. 2: 482, by the homology alignment algorithm of Needleman & Wunsch (1970) J Mol. Biol. 48: 443, by the search for similarity method of Pearson & Lipman (1988) Proc. Natl. Acad. Sci., USA, 85: 2444, by computerized implementations of these algorithms (GAP, BESTFIT, FASTA, and TFASTA in the Wisconsin Genetics Software Package, Genetics Computer Group, 575 Science Dr., Madison, Wis.), or by visual inspection.
• The term “specificity” when used with respect to the antimicrobial activity of a peptide indicates that the peptide preferentially inhibits growth and/or proliferation and/or kills a particular microbial species as compared to other related and/or unrelated microbes. In certain embodiments the preferential inhibition or killing is at least 10% greater (e.g., LD₅₀ is 10% lower), preferably at least 20%, 30%, 40%, or 50%, more preferably at least 2-fold, at least 5-fold, or at least 10-fold greater for the target species.
• “Treating” or “treatment” of a condition as used herein may refer to preventing the condition, slowing the onset or rate of development of the condition, reducing the risk of developing the condition, preventing or delaying the development of symptoms associated with the condition, reducing or ending symptoms associated with the condition, generating a complete or partial regression of the condition, or some combination thereof.
• The term “consisting essentially of” when used with respect to an antimicrobial peptide (AMP) or AMP motif as described herein, indicates that the peptide or peptides encompassed by the library or variants, analogues, or derivatives thereof possess substantially the same or greater antimicrobial activity and/or specificity as the referenced peptide. In certain embodiments substantially the same or greater antimicrobial activity indicates at least 80%, preferably at least 90%, and more preferably at least 95% of the anti microbial activity of the referenced peptide(s) against a particular bacterial species (e.g., S. mutans).
• The term “porphyrinic macrocycle” refers to a porphyrin or porphyrin derivative. Such derivatives include porphyrins with extra rings ortho-fused, or orthoperifused, to the porphyrin nucleus, porphyrins having a replacement of one or more carbon atoms of the porphyrin ring by an atom of another element (skeletal replacement), derivatives having a replacement of a nitrogen atom of the porphyrin ring by an atom of another element (skeletal replacement of nitrogen), derivatives having substituents other than hydrogen located at the peripheral (meso-, .beta.-) or core atoms of the porphyrin, derivatives with saturation of one or more bonds of the porphyrin (hydroporphyrins, e.g., chlorins, bacteriochlorins, isobacteriochlorins, decahydroporphyrins, corphins, pyrrocorphins, etc.), derivatives obtained by coordination of one or more metals to one or more porphyrin atoms (metalloporphyrins), derivatives having one or more atoms, including pyrrolic and pyrromethenyl units, inserted in the porphyrin ring (expanded porphyrins), derivatives having one or more groups removed from the porphyrin ring (contracted porphyrins, e.g., corrin, corrole) and combinations of the foregoing derivatives (e.g. phthalocyanines, porphyrazines, naphthalocyanines, subphthalocyanines, and porphyrin isomers). Certain porphyrinic macrocycles comprise at least one 5-membered ring.
• As used herein, an “antibody” refers to a protein consisting of one or more polypeptides substantially encoded by immunoglobulin genes or fragments of immunoglobulin genes. The recognized immunoglobulin genes include the kappa, lambda, alpha, gamma, delta, epsilon and mu constant region genes, as well as myriad immunoglobulin variable region genes. Light chains are classified as either kappa or lambda. Heavy chains are classified as gamma, mu, alpha, delta, or epsilon, which in turn define the immunoglobulin classes, IgG, IgM, IgA, IgD and IgE, respectively.
• A typical immunoglobulin (antibody) structural unit is known to comprise a tetramer. Each tetramer is composed of two identical pairs of polypeptide chains, each pair having one “light” (about 25 kD) and one “heavy” chain (about 50-70 kD). The N-terminus of each chain defines a variable region of about 100 to 110 or more amino acids primarily responsible for antigen recognition. The terms variable light chain (V_L) and variable heavy chain (V_H) refer to these light and heavy chains respectively.
• Antibodies exist as intact immunoglobulins or as a number of well characterized fragments produced by digestion with various peptidases. Thus, for example, pepsin digests an antibody below the disulfide linkages in the hinge region to produce F(ab)′₂, a dimer of Fab which itself is a light chain joined to V_H-C _H1 by a disulfide bond. The F(ab)′₂ may be reduced under mild conditions to break the disulfide linkage in the hinge region thereby converting the (Fab′)₂ dimer into an Fab′ monomer. The Fab′ monomer is essentially an Fab with part of the hinge region (see, Fundamental Immunology, W.E. Paul, ed., Raven Press, N.Y. (1993), for a more detailed description of other antibody fragments). While various antibody fragments are defined in terms of the digestion of an intact antibody, one of skill will appreciate that such Fab′ fragments may be synthesized de novo either chemically or by utilizing recombinant DNA methodology. Thus, the term antibody, as used herein also includes antibody fragments either produced by the modification of whole antibodies or synthesized de novo using recombinant DNA methodologies, including, but are not limited to, Fab′₂, IgG, IgM, IgA, scFv, dAb, nanobodies, unibodies, and diabodies.
• In certain embodiments antibodies and fragments of the present invention can be bispecific. Bispecific antibodies or fragments can be of several configurations. For example, bispecific antibodies may resemble single antibodies (or antibody fragments) but have two different antigen binding sites (variable regions). In various embodiments bispecific antibodies can be produced by chemical techniques (Kranz et al. (1981) Proc. Natl. Acad. Sci., USA, 78: 5807), by “polydoma” techniques (see, e.g., U.S. Pat. No. 4,474,893), or by recombinant DNA techniques. In certain embodiments bispecific antibodies of the present invention can have binding specificities for at least two different epitopes, at least one of which is an epitope of a microbial organism. The microbial binding antibodies and fragments can also be heteroantibodies. Heteroantibodies are two or more antibodies, or antibody binding fragments (e.g., Fab) linked together, each antibody or fragment having a different specificity.
• The term “STAMP” refers to Specifically Targeted Anti-Microbial Peptides. In various embodiments, a STAMP comprises one or more peptide targeting moieties attached to one or more antimicrobial moieties (e.g.., antimicrobial peptides (AMPs)). An MH-STAMP is a STAMP bearing two or more targeting domains (i.e., a multi-headed STAMP).
• The terms “isolated” “purified” or “biologically pure” refer to material which is substantially or essentially free from components that normally accompany it as found in its native state. In the case of a peptide, an isolated (naturally occurring) peptide is typically substantially free of components with which it is associated in the cell, tissue, or organism. The term isolated also indicates that the peptide is not present in a phage display, yeast display, or other peptide library.
• In various embodiments the amino acid abbreviations shown in Table 1 are used herein.

• TABLE 1
  Amino acid abbreviations.

  Abbreviation

  Name

  	3 Letter	1 Letter
  	Alanine	Ala	A
  	βAlanine	βAla
  	(NH2—CH2—CH2—COOH)
  	Arginine	Arg	R
  	Asparagine	Asn	N
  	Aspartic Acid	Asp	D
  	Cysteine	Cys	C
  	Glutamic Acid	Glu	E
  	Glutamine	Gln	Q
  	Glycine	Gly	G
  	Histidine	His	H
  	Homoserine	Hse	—
  	Isoleucine	Ile	I
  	Leucine	Leu	L
  	Lysine	Lys	K
  	Methionine	Met	M
  	Methionine sulfoxide	Met (O)	—
  	Methionine methylsulfonium	Met (S-Me)	—
  	Norleucine	Nle	—
  	Phenylalanine	Phe	F
  	Proline	Pro	P
  	Serine	Ser	S
  	Threonine	Thr	T
  	Tryptophan	Trp	W
  	Tyrosine	Tyr	Y
  	Valine	Val	V
  	episilon-aminocaproic acid	Ahx	J
  	(NH2—(CH2)5—COOH)
  	4-aminobutanoic acid	gAbu
  	(NH2—(CH2)3—COOH)
  	tetrahydroisoquinoline-3-		O
  	carboxylic acid
  	Lys(N(epsilon)-trifluoroacetyl)		K[TFA]
  	α-aminoisobutyric acid	Aib	B

BRIEF DESCRIPTION OF THE DRAWINGS
• FIG. 1 shows some illustrative porphyrins (compounds 92-99) suitable for use as targeting moieties and/or antimicrobial effectors.
• FIG. 2 shows some illustrative porphyrins (compounds 100-118) suitable for use as targeting moieties and/or antimicrobial effectors.
• FIG. 3 shows some illustrative porphyrins (in particular phthalocyanines) (compounds 119-128) suitable for use as targeting moieties and/or antimicrobial effectors.
• FIG. 4 illustrates the structures of two phthalocyanines, Monoastral Fast Blue B and Monoastral Fast Blue G suitable for use as targeting moieties and/or antimicrobial effectors.
• FIG. 5 illustrates certain azine photosensitizers suitable for use as targeting moieties and/or antimicrobial effectors in the compositions and methods described herein.
• FIG. 6 shows illustrative cyanine suitable for use as targeting moieties and/or antimicrobial effectors in the compositions and methods described herein.
• FIG. 7 shows illustrative psoralen (angelicin) photosensitizers suitable for use as targeting moieties and/or antimicrobial effectors in the compositions and methods described herein.
• FIG. 8 shows illustrative hypericin and the perylenequinonoid pigments suitable for use as targeting moieties and/or antimicrobial effectors in the compositions and methods described herein.
• FIG. 9 shows illustrative acridines suitable for use as targeting moieties and/or antimicrobial effectors in the compositions and methods described herein.
• FIG. 10 illustrates the structure of the acridine Rose Bengal.
• FIG. 11 illustrates various crown ethers suitable for use as targeting moieties and/or antimicrobial effectors in the compositions and methods described herein.
• FIG. 12 illustrates the structure of cumin.
• FIG. 13 illustrates an example of a targeted light-activated porphyrin we have constructed: C16-P18 comprising a porphyrin coupled to a C16 (SEQ ID NO:3) targeting sequence.
• FIG. 14 schematically shows some illustrative configurations for chimeric constructs described herein. A: Shows a single targeting moiety T1 attached to a single effector E1 by a linker/spacer L. B: Shows multiple targeting moieties T1, T2, T3 attached directly to each other and attached by a linker L to a single effector E1. In various embodiments T1, T2, and T3, can be domains in a fusion protein. C: Shows multiple targeting moieties T1, T2, T3 attached to each other by linkers L and attached by a linker L to a single effector E1. In various embodiments T1, T2, and T3, can be domains in a fusion protein. D: Shows a single targeting moiety T1 attached by a linker L to multiple effectors E1, E2, and E3 joined directly to each other. E: Shows a single targeting moiety T1 attached by a linker L to multiple effectors E1, E2, and E3 joined to each other by linkers L. F: Shows multiple targeting moieties joined directly to each other and by a linker L to multiple effectors joined to each other by linkers L. G: Shows multiple targeting moieties joined to each other by linkers L and by a linker L to multiple effectors joined to each other by linkers L. In various embodiments T1, T2, and T3, and/or E1, E2, and E3 can be domains in a fusion protein. H: Illustrates a branched configuration where multiple targeting moieties are linked to a single effector. I: Illustrates a dual branched configuration where multiple targeting moieties are linked to multiple effectors. J: Illustrates a branched configuration where multiple targeting moieties are linked to multiple effectors where the effectors are joined to each other in a linear configuration.
• FIG. 15 illustrates various MH-STAMPs used in Example 1. The design, sequence, and observed mass (m/z) for M8(KH)-20 (SEQ ID NOs:4, 5, and 6), BL(KH)-20 ( SEQ ID 7, 8, and 9), and M8(BL)-20 ( SEQ ID 10, 11, and 12).
• FIGS. 16A and 16B show HPLC and MS spectra of M8(KH)-20. The quality of the completed MH-STAMP was analyzed by HPLC (FIG. 16A) and MALDI mass spectroscopy (FIG. 16B). At UV absorbance 215 nm (260 and 280 nm are also plotted), a single major product was detected by HPLC (* retention volume 11.04 mL). After fraction collection, the correct mass (m/z) for single-charged M8(KH)-20, 4884.91 (marked by *), was observed for this peak. Y-axis: 16A, mAU miliabsorbance units; 16B, percent intensity.
• FIG. 17A-17E show growth inhibitory activity of MH-STAMPs. Monocultures of S. mutans (FIG. 17A); P. aeruginosa (FIG. 17B); S. epidermidis (FIG. 17C); S. aureus (FIG. 17D); or E. coli (FIG. 17E); were treated with peptides (as indicated in the figure) for 10 min. Agent was then removed and fresh media returned. Culture recovery was measured over time (OD600). Plots represent the average of at least 3 independent experiments with standard deviations.
• FIG. 18 illustrates the selective activity of dual-targeted and single-targeted MH-STAMPs in mixed culture. A mixture of P. aeruginosa (Pa), S. mutans (Sm), E. coli (Ec), and S. epidermidis (Se) planktonic cells were mixed with MH-STAMPs (as indicated in the figure) and treated 24 h. After incubation, cfu/mL of remaining constituent species were quantitated after plating to selective media. * indicates under 200 surviving cfu/mL recovered.
• FIGS. 19A and 19B illustrate Rose Bengal (FIG. 19A) and synthesis scheme for C16-RB, halides and side-chains omitted for clarity (FIG. 19B).
• FIG. 20 shows LC/MS profile C16-RB. Purity and molecular mass of C16-RB was confirmed by LC/MS. A single product was observed at 11.92 min with mass species at 1040.8 and 1560.25 daltons. Expected C16-RB mas: m/z=3118, m²⁺/z=1559, m³⁺/z=1039.
• FIG. 21 illustrates activity of RB and C16-RB against single-species S. mutans biofilms. * indicates fewer than 100 cfu/mL recovered
• FIG. 22 shows S. mutans-specific C16-RB activity. C16-RB, and not RB alone, preferentially eliminated S. mutans, and not other oral streptococci, after blue light illumination.
DETAILED DESCRIPTION
• In various embodiments, novel “targeting” peptides are identified that specifically or preferentially bind particular microorganisms (e.g., bacteria, yeasts, fungi, etc.). These peptides can be used alone to bind/capture and thereby identify and/or isolate particular target microorganisms, or they can be attached to one or more effectors (e.g., drugs, labels, etc.) and used as targeting moieties thereby providing a chimeric moiety that preferentially or specifically delivers the effector to a target microorganism, a population of target microorganisms, a microbial film, a biofilm, and the like.
• In various embodiments novel peptides having antimicrobial activity against certain bacteria, fungi, yeasts, and/or viruses and/or having activity that inhibits the growth or maintenance of biofilms comprising such microorganisms are provided. The AMPs can be used to inhibit the growth and/or proliferation of a microbial species and/or the growth and/formation and/or maintenance of a biofilm comprising the microbial species.
• In certain embodiments, the targeting moieties can be attached to antimicrobial peptides to form Specifically Targeted Anti-Microbial Peptides (STAMPs). In certain embodiments attachment of one or more targeting moieties/peptides to one or more antimicrobial peptides can narrow the spectrum of activity of the AMP(s) to provide efficacy against one or a few target microorganisms without substantially disrupting the remaining microbial ecology and thereby provide increased efficacy with fewer side effects.
• In certain embodiments STAMPs or effector peptides can be delivered against pathogenic bacteria by being cloned and expressed in probiotic organisms for therapeutic delivery in vivo. Recombinant expression (and overexpression) and export of antimicrobial peptides and other peptides are well documented in bacteria, including species that are also utilized as probiotics.
• In various embodiments the targeting peptides, antimicrobial peptides, and/or STAMPs can be formulated individually, in combination with each other, in combination with other antimicrobial peptides, and/or in combination with various antibacterial agents to provide antimicrobial reagents and/or pharmaceuticals.
• Accordingly, in certain embodiments this invention provides peptides having antimicrobial activity, compositions comprising the peptides, methods of using the peptides (or compositions thereof) to inhibit the growth of or kill a wide variety of microbial targets and methods of using the peptides (or compositions thereof) to treat or prevent microbial infections and diseases related thereto in both plants and animals.
• The various peptides (targeting peptides, AMPs, STAMPs, etc.) described herein exhibit antimicrobial activity, being biostatic or biocidal against a certain microbial targets, including but not limited to, Gram-negative bacteria such as Acinetobacter baumannii, Escherichia coli, Fusobacterium nucleatum, Pseudomonas aeruginosa, Porphyromonas gingivalis; Gram-positive bacteria such as Actinomyces naeslundii, Bacillus subtilis, Clostridium difficile, Enterococcus faecalis, Staphylococcus aureus (and MRSA), S. epidermidis, Streptococcus mutans, Streptococcus pneumoniae; and yeast or fungi such as Aspergillus niger, Candida albicans, Malassezia furfur, and Trichophyton rubrum (see, e.g., Table 2). Significantly, various peptides described herein are biostatic or biocidal against clinically relevant pathogens exhibiting multi-drug resistance such as, for example, methicillin-resistant Staphylococcus aureus (“MRSA”).

• TABLE 2
  Illustrative target microorganisms and associated pathology.

  Acinetobacter baumannii	Pathogenic gram-negative bacillus that is naturally sensitive
  (A. baumannii)	to relatively few antibiotics.
  Actinomyces naeslundii	Gram positive rod shaped bacteria that occupy the oral
  (A. naeslundii)	cavity and are implicated in periodontal disease and root
  	caries.
  Aspergillus niger	A fungal infection that often causes a black mould to appear
  (A. niger)	on some fruit and vegetables but may also infect humans
  	through inhalation of fungal spores.
  Bacteroides fragilis	Gram positive bacilli that are opportunistic human
  (B. fragilis)	pathogens, causing infections of the peritoneal cavity,
  	gastrointestinal surgery, and appendicitis via abscess
  	formation, inhibiting phagocytosis. Resistant to a wide
  	variety of antibiotics -- β-lactams, aminoglycosides, and
  	recently many species have acquired resistance to
  	erythromycin and tetracycline.
  Bacillus subtilis	Gram-positive, catalase-positive bacterium.
  (B. subtilis)
  Candida albicans	Causal agent of opportunistic oral and genital fungal
  (C. albicans)	infections in humans.
  Clostridium difficile	A gram-positive, anaerobic, spore-forming bacillus that is
  (C. difficile)	responsible for the development of antibiotic-associated
  	diarrhea and colitis.
  Corynebacterium jeikeium	Gram positive, opportunistic pathogen primarily of
  (C. jeikeium)	immunocompromised (neutropenic) patients. Highly
  	resistant to antibiotics
  Campylobacter jejuni	Gram negative cause of human gastroenteritis/food
  (C. jejuni)	poisoning.
  Escherichia coli	Gram negative rod-shaped bacterium commonly found in the
  (E. coli)	lower intestine of warm-blooded organisms. Certain strains
  	cause serious food poisoning in humans.
  Enterococcus faecalis	Gram-positive commensal bacterium
  (E. faecalis)
  Fusobacterium nucleatum	Gram negative schizomycetes bacterium often seen in
  (F. nucleatum)	necrotic tissue and implicated, but not conclusively, with
  	other organisms in the causation and perpetuation of
  	periodontal disease.
  Lactobacillus acidophilus	Gram-positive commensal bacterium.
  (L. acidophilus)
  Legionella pneumophila	Gram negative bacterium that is the causative agent of
  (L. pneumophila)	legionellosis or Legionnaires' disease.
  (Micrococcus luteus)	Gram positive, spherical, saprotrophic bacterium found in
  M. luteus	soil, dust, water and air, and as part of the normal flora of the
  	mammalian skin. The bacterium also colonizes the human
  	mouth, mucosae, oropharynx and upper respiratory tract.
  	Considered an emerging nosocomial pathogen in
  	immunocompromised patients.
  Mycobacterium smegmatis	Gram-variable (acid-fast) soil-dwelling organism utilized as
  (M. smegmatis)	a proxy for Mycobacterium tuberculosis during research and
  	development.
  Malassezia furfur	Yeast - cutaneous pathogen.
  (M. furfur)
  Methicillin-resistant	Any strain of Staphylococcus aureus bacteria (gram positive)
  Staphylococcus aureus	that is resistant to a one or more members of a large group of
  (MRSA)	antibiotics called the beta-lactams. Responsible for skin and
  	systemic infections.
  Myxococcus xanthus	Gram negative cells that form biofilms and display primitive
  (M. xanthus)	social motility and fruiting body organization.
  Pseudomonas aeruginosa	Gram-negative rod. Frequent opportunistic pathogen and
  P. aeruginosa	infects burn wounds. Causes ear infections in children.
  	Infects the lungs of cystic fibrosis patients.
  Porphyromonas gingivalis	Non-motile, gram-negative, rod-shaped, anaerobic
  (P. gingivalis)	pathogenic bacterium (periodontal disease)
  Progeussmirabilis	Gram-negative, facultatively anaerobic bacterium. Causes
  (P. mirabilis)	90% of all ‘Proteus’ infections in humans.
  S. epidermidis	Gram-positive, coagulase-negative cocci. Nosocomial
  (S. epidermidis)	pathogen associated with infection (biofilm) of implanted
  	medical device.
  Streptococcus mutans	Gram-positive, facultatively anaerobic bacterium commonly
  (S. mutans)	found in the human oral cavity and is a significant
  	contributor to tooth decay
  Streptococcus pneumoniae	Gram-positive, alpha-hemolytic, bile soluble aerotolerant
  (S. pneumoniae)	anaerobe. Causal agent for streptococcal pneumonia.
  Treponema denticola	Gram-negative oral spirochete associated with the incidence
  (T. denticola)	and severity of human periodontal disease.
  Trichophyton rubrum	Most common cause of athlete's foot, jock itch and
  (T. rubrum)	ringworm.

• The various agents described herein (targeting peptides, compound targeting peptides, antimicrobial peptides (AMPs) and/or compound AMPs, STAMPs and/or other chimeric moieties). or compositions thereof, are useful as biocidal or biostatic or fungicidal or fungistatic agents and/or virucidal agents in a wide variety of applications. For example, the agents can be used to disinfect or preserve a variety of materials including medical instruments, foodstuffs, medicaments, cosmetics and other nutrient-containing materials. Various peptides described herein are particularly useful as bacteriostatic or bactericidal agents against multi-drug-resistant pathogens such as MRSA in a variety of clinical settings.
• The agents described herein, or compositions thereof, are also useful for the prophylaxis or treatment of microbial infections and diseases related thereto in both plants and animals. Such diseases include, but are not limited to, Gram-negative and Gram-positive bacterial infections, endocarditis, pneumonia and other respiratory infections, urinary tract infections, systemic candidiasis, oral mucositis, fungal infections, biofilm formation or maintenance (e.g., on medical implants), and the like.
• In various embodiments, the agents described herein can be formulated individually, in combination with each other, in combination with other antimicrobial peptides, and/or in combination with various antibiotic (e.g., antibacterial) agents in “home healthcare” formulations. Such formulations include, but are not limited to toothpaste, mouthwash, tooth whitening strips or solutions, contact lens storage, wetting, or cleaning solutions, dental floss, toothpicks, toothbrush bristles, oral sprays, oral lozenges, nasal sprays, aerosolizers for oral and/or nasal application, wound dressings (e.g., bandages), and the like.
• Such applications are illustrative and not limiting. Using the teachings provided herein other uses of the AMPs and compositions described herein will be recognized by one of
I. Targeting Peptides.
• A) Uses of Targeting Peptides.
• The novel microorganism-binding peptides (targeting peptides) described herein can be used to preferentially or specifically deliver an effector to a microorganism (e.g., a bacterium, a fungus, a protozoan, an algae, etc.), to a bacterial film, to a biofilm, and the like. The targeting peptides described herein can be used to bind to and thereby label particular targets, and/or as capture reagents to bind target microorganisms and thereby provide an indicator of the presence and/or quantity of the target microorganism(s). In certain embodiments the targeting peptide can be attached to an effector such as an epitope tag and/or a detectable label and thereby facilitate the identification of the presence and/or location, and/or quantity of the target (e.g., target organism). Thus targeting moieties are thus readily adapted for use in in vivo diagnostics, and/or ex vivo assays. Moreover, because of small size and good stability, microorganism binding peptides are well suited for microassay systems (e.g., microfluidic assays (Lab on a Chip), microarray assays, and the like).
• In certain embodiments the microorganism binding peptides (targeting peptides) can be attached to an effector that has antimicrobial activity (e.g., an antimicrobial peptide, an antibacterial and/or antifungal, a vehicle that contains an antibacterial or antifungal, etc. In various embodiments these chimeric moieties can be used in vivo, or ex vivo to preferentially inhibit or kill the target organism(s).
• In certain embodiments the targeting peptides can be recombinantly expressed as part of a yeast or phage tail fiber or coat protein to enhance binding of the yeast or phage to a specific bacterial Gram-designation, genus, species, or strain. Phage with expressed peptides will then display altered infection selectivity towards a designed target bacteria for use in phage therapy. Cloning the DNA encoding a peptide of interest into the major or minor coat proteins of a bacteriophage, for example in Proteins I through VIII of phages SAP-2, M13, or T7, will result in a targeted phage expressing 1-200 copies of the targeting peptide on the phage surface.
• In certain embodiments the targeting peptides can be used in various pre-targeting protocols. In pre-targeting protocols, a chimeric molecule is utilized comprising a primary targeting species (e.g. a microorganism-binding peptide) that specifically binds the desired target (e.g. a bacterium) and an effector that provides a binding site that is available for binding by a subsequently administered second targeting species. Once sufficient accretion of the primary targeting species (the chimeric molecule) is achieved, a second targeting species comprising (i) a diagnostic or therapeutic agent and (ii) a second targeting moiety, that recognizes the available binding site of the primary targeting species, is administered.
• An illustrative example of a pre-targeting protocol is the biotin-avidin system for administering a cytotoxic radionuclide to a tumor. In a typical procedure, a monoclonal antibody targeted against a tumor-associated antigen is conjugated to avidin and administered to a patient who has a tumor recognized by the antibody. Then the therapeutic agent, e.g., a chelated radionuclide covalently bound to biotin, is administered. The radionuclide, via its attached biotin is taken up by the antibody-avidin conjugate pretargeted at the tumor. Examples of pre-targeting biotin/avidin protocols are described, for example, in Goodwin et al., U.S. Pat. No. 4,863,713; Goodwin et al. (1988) J. Nucl. Med. 29: 226; Hnatowich et al. (1987) J. Nucl. Med. 28: 1294; Oehr et al. (1988) J. Nucl. Med. 29: 728; Klibanov et al. (1988) J. Nucl. Med. 29: 1951; Sinitsyn et al. (1989) J. Nucl. Med. 30: 66; Kalofonos et al. (1990) J. Nucl. Med. 31: 1791; Schechter et al. (1991) Int. J. Cancer 48:167; Paganelli et al. (1991) Cancer Res. 51: 5960; Paganelli et al. (1991) Nucl. Med. Commun. 12: 211; Stickney et al. (1991) Cancer Res. 51: 6650; and Yuan et al. (1991) Cancer Res. 51:3119.
• It will be recognized that the tumor-specific antibody used for cancer treatments can be replaced with a microorganism binding peptide of the present invention and similar pre-targeting strategies can be used to direct labels, antibiotics, and the like to the target organism(s).
• Three-step pre-targeting protocols in which a clearing agent is administered after the first targeting composition has localized at the target site also have been described. The clearing agent binds and removes circulating primary conjugate which is not bound at the target site, and prevents circulating primary targeting species (antibody-avidin or conjugate, for example) from interfering with the targeting of active agent species (biotin-active agent conjugate) at the target site by competing for the binding sites on the active agent-conjugate. When antibody-avidin is used as the primary targeting moiety, excess circulating conjugate can be cleared by injecting a biotinylated polymer such as biotinylated human serum albumin. This type of agent forms a high molecular weight species with the circulating avidin-antibody conjugate which is quickly recognized by the hepatobiliary system and deposited primarily in the liver.
• Examples of these protocols are disclosed, e.g., in PCT Application No. WO 93/25240; Paganelli et al. (1991) Nucl. Med. Comm., 12: 211-234; Oehr et al. (1988) J. Nucl. Med., 29: 728-729; Kalofonos et al. (1990) J. Nucl. Med., 31: 1791-1796; Goodwin et al. (1988) J. Nucl. Med., 29: 226-234; and the like).
• These applications of microorganism binding peptides of this invention are intended to be illustrative and not limiting. Using the teaching provided herein, other uses will be recognized by one of skill in the art.
• B) Illustrative Novel Targeting Peptides.
• In certain embodiments, the targeting moiety comprises one or more targeting peptides that bind particular bacteria, fungi, and/or yeasts, and/or algae, and/or viruses and/or that bind particular groups of bacteria, and/or groups of fungi, and/or groups of yeasts, and/or groups of algae.
• In certain embodiments the targeting peptides include peptides comprising or consisting of one or more of the amino acid sequences shown in Table 3 (SEQ ID NOs:13-1566). In various embodiments the peptides include peptides comprising or consisting of the retro, inverso, retro-inverso, and/or beta form of one or more of the amino acid sequences shown in Table 3. Also contemplated are circular permutations of these sequences as well as peptides comprising or consisting of the retro, inverso, retro-inverso, and/or beta form of such circular permutations.
• It will also be recognized, that in certain embodiments, any peptide or compound AMP described herein can be circularized.
• In various embodiments the peptides can optionally bear one or more protecting groups, e.g., and the amino and/or carboxyl termini, and/or on side chains.
• Also contemplated are peptides comprising one, two, three four, or five conservative substitutions of these amino acid sequences.

• TABLE 3
  Illustrative list of novel targeting peptides.

  			SEQ ID
  ID	Target(s)	Targeting Peptide Sequence	NO

  1T-3	S. mutans	VLGIAGGLDAYGELVGGN	13
  	S. gordonii
  1T-4	S. mutans	LDAYGELVGGN	14
  	S. gordonii
  	S. sanguinis
  	S. oralis
  	V. atypica
  	L. casei
  1T-6	S. mutans	KFINGVLSQFVLERK	15
  1T-7	M. xanthus	SQRIIEPVKSPQPYPGFSVS	16
  1T-8	M. xanthus	FSVAACGEQRAVTFVLLIEDLI	17
  1T-9	M. xanthus	WAWAESPRCVSTRSNIHALAFRVEVAA	18
  		LT
  1T-10	M. xanthus	SPAGLPGDGDEA	19
  1T-11	S. mutans	RISE	20
  	S. epidermidis
  	P. aeruginosa
  1T-12	C. xerosis	FGNIFKGLKDVIETIVKWTAAK	21
  	C. striatum
  	S. epidermidis
  	S. mutans
  1T-13	S. aureus	FRSPCINNNSLQPPGVYPAR	22
  	S. epidermidis
  	P. aeruginosa
  1T-14	S. mutans	ALAGLAGLISGK	23
  	S. aureus
  	S. epidermidis
  	C. xerosis
  1T-15	S. mutans	DVILRVEAQ	24
  1T-16	P. aeruginosa	IDMR	25
  1T-17	S. mutans	NNAIVYIS	26
  1T-18	S. aureus	YSKTLHFAD	27
  	S. epidermidis
  	C. striatum
  	P. aeruginosa
  1T-19	S. aureus	PGAFRNPQMPRG	28
  	S. epidermidis
  	P. aeruginosa
  1T-20	S. mutans	PALVDLSNKEAVWAVLDDHS	29
  	P. aeruginosa
  1T-21	S. mutans	YVEEAVRAALKKEARISTEDTPVNLPSF	30
  	P. aeruginosa	DC
  1T-22	S. epidermidis	VPLDDGTRRPEVARNRDKDRED	31
  	P. aeruginosa
  1T-23	S. mutans	PALVDLSNKEAVWAVLDDHS	32
  	P. aeruginosa
  1T-24	P. aeruginosa	EEAEEKLAEVSQAVKRLVR	33
  1T-25	S. aureus	VGLDVSVLVLFFGLQLLSVLLGAMIR	34
  	S. epidermidis
  	C. xerosis
  	C. striatum
  	P. aeruginosa
  1T-26	S. mutans	LTILPTTFFAIIVPILAVAFIAYSGFKIKGI	35
  	S. aureus	VEHKDQW
  	S. epidermidis
  	C. jeikeium
  	C. xerosis
  	C. striatum
  	P. aeruginosa
  1T-27	S. mutans	ALFVSLEQFLVVVAKSVFALCHSGTLS	36
  	S. aureus
  	S. epidermidis
  	C. jeikeium
  	C. xerosis
  	C. striatum
  	P. aeruginosa
  1T-28	P. aeruginosa	VSRDEAMEFIDREWTTLQPAGKSHA	37
  1T-29	S. mutans	GSVIKKRRKRMSKKKHRKMLRRTRVQ	38
  	S. aureus	RRKLGK
  	S. epidermidis
  	C. jeikeium
  	C. xerosis
  	C. striatum
  	P. aeruginosa
  1T-30	S. aureus	GKAKPYQVRQVLRAVDKLETRRKKGG	39
  	S. epidermidis	R
  	C. xerosis
  	C. striatum
  	P. aeruginosa
  1T-31	S. mutans	NATGTDIGEVTLTLGRFS	40
  	P. aeruginosa
  1T-32	S. mutans	VSFLAGWLCLGLAAWRLGNA	41
  1T-33	S. aureus	VRTLTILVIFIFNYLKSISYKLKQPFENNL	42
  	S. epidermidis	AQSMISI
  	C. jeikeium
  	C. xerosis
  	C. striatum
  	P. aeruginosa
  1T-34	S. aureus	AFWLNILLTLLGYIPGIVHAVYIIAKR	43
  	S. epidermidis
  	C. jeikeium
  	C. xerosis
  	C. striatum
  	P. aeruginosa
  1T-35	P. aeruginosa	EICLTLVFPIRGSYSEAAKFPVPIHIVEDG	44
  		TVELPK
  1T-36	S. aureus	VYRHLRFIDGKLVEIRLERK	45
  	S. epidermidis
  	C. jeikeium
  	C. xerosis
  	C. striatum
  	P. aeruginosa
  1T-37	S. mutans	YIVGALVILAVAGLIYSMLRKA	46
  	S. aereus
  	S. epidermidis
  	C. jeikeium
  	C. xerosis
  	C. striatum
  	P. aeruginosa
  1T-38	S. mutans	VMFVLTRGRSPRPMIPAY	47
  	S. aereus
  	S. epidermidis
  	C. jeikeium
  	C. xerosis
  	C. striatum
  	P. aeruginosa
  1T-39	S. mutans	FGFCVWMYQLLAGPPGPPA	48
  	P. aeruginosa
  1T-40	S. mutans	QRVSLWSEVEHEFR	49
  	P. aeruginosa
  1T-41	S. mutans	KRGSKIVIAIAVVLIVLAGVWVW	50
  	S. aureus
  	S. epidermidis
  	C. jeikeium
  	C. striatum
  	P. aeruginosa
  1T-42	S. aureus	TVLDWLSLALATGLFVYLLVALLRADR	51
  	S. epidermidis	A
  	C. xerosis
  	C. striatum
  	P. aeruginosa
  1T-43	C. jeikium	DRCLSVLSWSPPKVSPLI	52
  	P. aeruginosa
  1T-44	S. mutans	DPALADFAAGMRAQVRT	53
  	S. aureus
  	S. epidermidis
  	C. jeikeium
  	C. striatum
  	P. aeruginosa
  1T-45	S. aureus	WTKPSFTDLRLGFEVTLYFANR	54
  	S. epidermidis
  	C. striatum
  	P. aeruginosa
  1T-46	S. aureus	FSFKQRVMFRKEVERLR	55
  	S. epidermidis
  	C. jeikeium
  	C. xerosis
  	C. striatum
  	P. aeruginosa
  1T-47	S. mutans	VIKISVPGQVQMLIP	56
  	S. epidermidis
  	P. aeruginosa
  1T-48	S. aureus	KLQVHHGRATHTLLLQPPLCAPGTIR	57
  	S. epidermidis
  	C. jeikeium
  	C. xerosis
  	C. striatum
  	P. aeruginosa
  1T-49	S. aureus	SLVRIHDQQPWVTRGAFIDAARTCS	58
  	S. epidermidis
  	C. jeikeium
  	P. aeruginosa
  1T-50	P. aeruginosa	HSDEPIPNILFKSDSVH	59
  1T-51	S. aureus	GKPKRMPAEFIDGYGQALLAGA	60
  	P. aeruginosa
  1T-52	S. aureus	DEYPAKLPLSDKGATEPRRH	61
  	C. xerosis
  	P. aeruginosa
  1T-53	P. aeruginosa	SDILAEMFEKGELQTLVKDAAAKANA	62
  1T-54	S. epidermidis	RWVSCNPSWRIQ	63
  	C. xerosis
  	C. striatum
  	P. aeruginosa
  1T-55	C. xerosis	NHKTLKEWKAKWGPEAVESWATLLG	64
  	P. aeruginosa
  1T-56	C. xerosis	LALIGAGIWMIRKG	65
  	P. aeruginosa
  1T-57	P. aeruginosa	RLEYRRLETQVEENPESGRRPMRG	66
  1T-58	P. aeruginosa	CDDLHALERAGKLDALLSA	67
  1T-59	S. aureus	AVGNNLGKDNDSGHRGKKHRKHKHR	68
  	S. epidermidis
  	P. aeruginosa
  1T-60	S. aureus	YLTSLGLDAAEQAQGLLTILKG	69
  	S. epidermidis
  	C. jeikeium
  	C. striatum
  	P. aeruginosa
  1T-61	P. aeruginosa	HATLLPAVREAISRQLLPALVPRG	70
  1T-62	S. epidermidis	GCKGCAQRDPCAEPEPYFRLR	71
  	P. aeruginosa
  1T-63	S. aureus	EPLILKELVRNLFLFCYARALR	72
  	S. epidermidis
  	C. jeikeium
  	C. xerosis
  	C. striatum
  	P. aeruginosa
  1T-64	S. aureus	QTVHHIHMHVLGQRQMHWPPG	73
  	S. epidermidis
  	C. jeikeium
  	C. xerosis
  	C. striatum
  	P. aeruginosa
  1T-65	S. mutans	HARAAVGVAELPRGAAVEVELIAAVRP	74
  	S. aureus
  	S. epidermidis
  	C. jeikeium
  	C. xerosis
  	C. striatum
  	P. aeruginosa
  1T-66	S. mutans	DTDCLSRAYAQRIDELDKQYAGIDKPL	75
  	S. aureus
  	S. epidermidis
  	C. jeikeium
  	C. xerosis
  	C. striatum
  	P. aeruginosa
  1T-67	S. aureus	GQRQRLTCGRVSGCSEGPSREAAR	76
  	S. epidermidis
  	C. jeikeium
  	C. xerosis
  	C. striatum
  	P. aeruginosa
  1T-68	S. mutans	GGTKEIVYQRG	77
  	S. aureus
  	C. jeikeium
  	C. xerosis
  	C. striatum
  	P. aeruginosa
  1T-69	S. mutans	ILSQEADRKKLF	78
  	P. aeruginosa
  1T-70	S. aureus	NRQAQGERAHGEQQG	79
  	C. jeikeium
  	P. aeruginosa
  1T-71	P. aeruginosa	KIDTNQWPPNKEG	80
  1T-72	P. aeruginosa	EPTDGVACKER	81
  1T-73	S. pneumoniae	GWWEELLHETILSKFKITKALELPIQL	82
  1T-74	S. pneumoniae	DIDWGRKISCAAGVAYGAIDGCATTV	83
  1T-75	S. pneumoniae	GVARGLQLGIKTRTQWGAATGAA	84
  1T-76	S. pneumoniae	EMRLSKFFRDFILWRKK	85
  1T-77	S. pneumoniae	EMRISRIILDFLFLRKK	86
  1T-78	S. pneumoniae	FFKTIFVLILGALGVAAGLYIEKNYIDK	87
  1T-79	S. pneumoniae	FGTPWSITNFWKKNFNDRPDFDSDRRR	88
  		Y
  1T-80	S. pneumoniae	GGNLGPGFGVIIP	89
  1T-81	S. pneumoniae	AIATGLDIVDGKFDGYLWA	90
  1T-82	S. pneumoniae	FGVGVGIALFMAGYAIGKDLRKKFGKS	91
  		C
  1T-83	S. pneumoniae	QKPRKNETFIGYIQRYDIDGNGYQSLPC	92
  		PQN
  1T-84	S. pneumoniae	FRKKRYGLSILLWLNAFTNLVNSIHAFY	93
  		MTLF
  1T-85	A. naeslundii	VMASLTWRMRAASASLPTHSRTDA	94
  	F. nucleatum
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-86	S. mitis	HRKNPVLGVGRRHRAHNVA	95
  	S. oralis
  	S. salivarious
  1T-87	S. mitis	EAVGQDLVDAHHP	96
  	S. mutans
  	S. oralis
  1T-89	S. mitis	HEDDKRRGMSVEVLGFEVVQHEE	97
  	S. mutans
  1T-90	S. gordonii	RNVIGQVL	98
  	S. mitis
  	S. mutans
  	S. oralis
  	S. sanguinis
  1T-91	S. mitis	TSVRPGAAGAAVPAGAAGAAGAGWR	99
  	S. mutans	WP
  	S. oralis
  	S. sanguinis
  1T-92	S. mitis	GQDEGQRRAGVGEGQGVDG	100
  	S. mutans
  1T-93	S. epidermidis	AMRSVNQA	101
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. sanguinis
  1T-94	S. mitis	DQVAHSGDMLVQARRRDS	102
  	S. mutans
  	S. oralis
  1T-95	S. gordonii	GHLLRVGGRVGGVGGVAGACAQPFGG	103
  	S. mitis	Q
  	S. mutans
  	S. oralis
  	S. sanguinis
  1T-96	S. gordonii	VAGACAQPFGGQ	104
  	S. mitis
  	S. mutans
  	S. oralis
  	S. sanguinis
  1T-97	A. naeslundii	GVAERNLDRITVAVAIIWTITIVGLGLV	105
  	F. nucleatum	AKLG
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-98	A. naeslundii	VRSAKAVKALTAAGYTGELVNVSGGM	106
  	F. nucleatum	KAWLGQ
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-99	S. gordonii	MKAWLGQ	107
  	S. mitis
  	S. mutans
  	S. oralis
  	S. sanguinis
  1T-100	S. gordonii	LDPLEPRIAPPGDRSHQGAPACHRDPLR	108
  	S. mitis	GRSARDAER
  	S. mutans
  1T-101	A. naeslundii	RLRVGRATDLPLTSFAVGVVRNLPDAP	109
  	P. gingivalis	AH
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. sanguinis
  1T-102	A. naeslundii	WKRLWPARILAGHSRRRMRWMVVWR	110
  	F. nucleatum	YFAAT
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-103	A. naeslundii	AQFYEAIITGYALGAGQRIGQL	111
  	F. nucleatum
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. sanguinis
  1T-104	S. mitts	RAVAAHLQGRHEIGHQVRRQRHGQR	112
  1T-105	S. epidermidis	GEGLPPPVLHLPPPRMSGR	113
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  1T-106	S. gordonii	DALRRSRSQGRRHR	114
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  1T-107	A. naeslundii	SPVPRFTAVGGVSRGSP	115
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-108	S. gordonii	WGPLGPERPLW	116
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-109	A. naeslundii	VTTNVRQGAGS	117
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-110	A. naeslundii	LAAKTAVCVGRAFM	118
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. sanguinis
  1T-111	A. naeslundii	GRLSRREEDPATSIILLRGAYRMAVF	119
  	F. nucleatum
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-112	S. gordonii	SDNDGKLILGTSQ	120
  1T-113	S. mitis	HGAHQRTGQRLHEIHRGRTVSGCRQNP	121
  		VAGVDPDEHR
  1T-114	A. naeslundii	RQAPGPGLVTITAACSAPGSRSR	122
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. sanguinis
  1T-115	A. naeslundii	LLIERFSNHH	123
  	F. nucleatum
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-116	A. naeslundii	MILHRRRDR	124
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-117	S. mutans	GPGVVGPAPFSRLPAHALNL	125
  1T-118	A. naeslundii	TASPPAPSDQGLRTAFPATLLIALAALA	126
  	F. nucleatum	RISR
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-119	S. gordonii	SPATQKAPTRAQPSRAPVQDCGDGRPT	127
  	S. mitis	AAPDDVERLSPR
  	S. mutans
  	S. oralis
  1T-120	A. naeslundii	DVRDRVDLAGADLCAAHATR	128
  	F. nucleatum
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-121	S. gordonii	FAKETGFGIGGAQEGWWIIADIYGPNPF	129
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-122	S. mitts	GAIPDPVTHRVDWEEDHQTRPSR	130
  1T-123	S. gordonii	LVRRNAVAGRSDGLAGAEQLDLVRLQ	131
  		GVL
  1T-124	S. mitts	LFDERNKIA	132
  	S. mutans
  	S. oralis
  1T-125	S. epidermidis	DAITGGNPPLSDTDGLRP	133
  	S. gordonii
  	S. mutans
  	S. oralis
  1T-126	S. gordonii	QGLARPVLRRIPL	134
  	S. mitis
  	S. mutans
  1T-127	A. naeslundii	YDPVPKRKNKNSEGKREE	135
  	F. nucleatum
  	P. gingivalis
  	T. denticola
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-128	A. naeslundii	SGSAIRMLEIATKMLKR	136
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-129	A. naeslundii	YDKYIKYLSIQPPFIVYFI	137
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-130	A. naeslundii	QKIIDMSKFLFSLILFIMIVVIYIGKSIGG	138
  	F. nucleatum	YSAIVSSIMLELDTVLYNKKIFFIYK
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-131	A. naeslundii	DEVWKMLGI	139
  	F. nucleatum
  	P. gingivalis
  	T. denticola
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-132	A. naeslundii	YSKKLFEYFYFIIFILIRYLIFYKIIQNKNY	140
  	F. nucleatum	YINNIAYN
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-133	A. naeslundii	YFIKDDNEALSKDWEVIGNDLKGTIDK	141
  	P. gingivalis	YGKEFKVR
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-134	A. naeslundii	SRLVREIKKKCRKS	142
  	F. nucleatum
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-135	A. naeslundii	FESLLPQATKKIVNNKGSKINKIF	143
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-136	A. naeslundii	ELLTQIRLALLYSVNEW	144
  	F. nucleatum
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-137	A. naeslundii	PLNFYRAVKENRLPLSEKNINDFTNIKL	145
  	F. nucleatum	KVSPKLINLLQESSIFYNFSPKKRNTN
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-138	A. naeslundii	YPNEYCIFLENLSLEELKEIKAINGETLN	146
  	F. nucleatum	LEEIINERKNLKD
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-139	A. naeslundii	AVAGAAVGALLGNDARSTAVGAAIGG	147
  	S. gordonii	ALGAGAGELTKNK
  	S. mitis
  	S. mutans
  	S. oralis
  1T-140	A. naeslundii	IKGTIAFVGEDYVEIRVDKGVKLTFRKS	148
  	F. nucleatum	AIANVINNNQQ
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-141	F. nucleatum	KKFIILLFILVQGLIFSATKTLSDIIAL	149
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. sanguinis
  1T-142	A. naeslundii	FTQGIKRIVLKRLKED	150
  	F. nucleatum
  	P. gingivalis
  	T. denticola
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-143	A. naeslundii	MPKRHYYKLEAKALQFGLPFAYSPIQL	151
  	F. nucleatum	LK
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-144	A. naeslundii	IIELHPKSWTQDWRCSFL	152
  	F. nucleatum
  	P. gingivalis
  	T. denticola
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-145	S. mitts	VEAGKRNISLENIEKISKGLGISISELFKY	153
  	S. mutans	IEEGEDKIG
  	S. oralis
  1T-146	A. naeslundii	RNSADNQTKIDKIRIDISLWDEHLNIVK	154
  	F. nucleatum	QGK
  	P. gingivalis
  	T. denticola
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-147	A. naeslundii	GVENRRFYERDVSKVSMNITSEAVAPR	155
  	F. nucleatum	GGSK
  	P. gingivalis
  	T. denticola
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-148	A. naeslundii	IVELDDTTILERALSMLGEANA	156
  	F. nucleatum
  	P. gingivalis
  	T. denticola
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-149	A. naeslundii	SVRAVKPIDETVARHFPGDFIVN	157
  	F. nucleatum
  	P. gingivalis
  	T. denticola
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-150	A. naeslundii	YINRRLKKAFSDADIKEAPAEFYEELRR	158
  	F. nucleatum	VQYV
  	P. gingivalis
  	T. denticola
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-151	A. naeslundii	SVRAVKPIDEIVAWHFPGDFIVN	159
  	F. nucleatum
  	P. gingivalis
  	T. denticola
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-152	A. naeslundii	YVSADESAYNHIVTDDIPLADRRIEAVQ	160
  	F. nucleatum	Q
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-153	A. naeslundii	YIACPGYFY	161
  	F. nucleatum
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-154	P. gingivalis	YFSFLEIVGMARR	162
  1T-155	A. naeslundii	LKLAFGVYPFQANISQSDTAVSERNVL	163
  	F. nucleatum	WR
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-156	A. naeslundii	GRFQISIRGEEKSKVKVQGKGTFTDRNT	164
  	F. nucleatum	T
  	P. gingivalis
  	T. denticola
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-157	A. naeslundii	RRFRKTTENREKSKNKKAVLGLSTTST	165
  	F. nucleatum	ASY
  	P. gingivalis
  	T. denticola
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-158	A. naeslundii	WENKPSPLGSIKKLQGLVYRLIGYRHF	166
  	F. nucleatum	WV
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-159	P. gingivalis	IFSLHHFALICSEMGTFAVSKRAKYKWE	167
  		VL
  1T-160	A. naeslundii	AQYKYINKLLN	168
  	F. nucleatum
  	P. gingivalis
  	T. denticola
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-161	A. naeslundii	NKVLQVEVMWDGSVVGRPAGVISIKSS	169
  	F. nucleatum	KKG
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-162	A. naeslundii	QKAKEESDRKAAVSYNGFHRVNVVSIP	170
  	F. nucleatum	K
  	P. gingivalis
  	T. denticola
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-163	A. naeslundii	MENILIYIPMVLSPFGSGILLFLGKDRRY	171
  	F. nucleatum	ML
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-164	A. naeslundii	KKSHSQGKRKLKDLNSAYKIDNQLHYA	172
  	F. nucleatum	LR
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-165	A. naeslundii	CYDSFDFSIFVTFANRMKLSVGS	173
  	F. nucleatum
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. Mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-166	A. naeslundii	AQSAGQIKRKSKVRIHV	174
  	F. nucleatum
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-167	A. naeslundii	SRMSEHSPAGLVFEVGPMDKGSFIILDS	175
  	F. nucleatum	YHPTVKK
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-168	A. naeslundii	ELHRIMSTEKIGAVTKMNFDTAPIMSILP	176
  	F. nucleatum	IDIYPKEVGIGS
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-169	A. naeslundii	FARVRRLHQNRILTQPLTNLKYCLRQPI	177
  	F. nucleatum	YSD
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-170	P. gingivalis	AYGKVFSMDIMLSENDKLIVLRISHESA	178
  		WH
  1T-171	A. naeslundii	SVRAVKPIDKTVARHFPGDFIVN	179
  	F. nucleatum
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-172	A. naeslundii	FEGLKNLLGDDII	180
  	F. nucleatum
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-173	A. naeslundii	LFRKEDQEHVLL	181
  	F. nucleatum
  	P. gingivalis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-174	A. naeslundii	SGGSDTDGSSSGEPGSHSGDL	182
  	F. nucleatum
  	P. gingivalis
  	T. denticola
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-175	A. naeslundii	GEPGSHSGDL	183
  	F. nucleatum
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-176	A. naeslundii	PVGDIMSGFLRGANQPRFLLDHISFGS	184
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-177	P. gingivalis	GTNVPTQILGYSREERFDYEPAPEQR	185
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-178	A. naeslundii	LLASHPERLSLGVFFVYRVLHLLLENT	186
  	F. nucleatum
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-179	A. naeslundii	TCYPLIQRKTDRAYEA	187
  	F. nucleatum
  	P. gingivalis
  	T. denticola
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-180	A. naeslundii	VVFGGGDRLV	188
  	F. nucleatum
  	P. gingivalis
  	T. denticola
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-181	A. naeslundii	YGKESDP	189
  	F. nucleatum
  	P. gingivalis
  	T. denticola
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-182	A. naeslundii	LTASICRQWNDNSTPYQR	190
  	F. nucleatum
  	P. gingivalis
  	T. denticola
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-183	A. naeslundii	PLRSFVAEKAEHAFRVVRIADFDFGHS	191
  	F. nucleatum
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-184	A. naeslundii	ALLVLNLLLMQFFFGKNIVI	192
  	F. nucleatum
  	P. gingivalis
  	T. denticola
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-185	A. naeslundii	HYHFLLEFGFHKGDYLE	193
  	F. nucleatum
  	P. gingivalis
  	T. denticola
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-188	S. sanguinis	HRKDVYKK	194
  1T-190	A. naeslundii	IQIIVNAFVEKDKTGAVIEVLYASNNHE	195
  	F. nucleatum	KVKAKYEELVAIS
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-192	S. sanguinis	ILVLLALQVELDSKFQY	196
  1T-193	S. sanguinis	LMIFDKHANLKYKYGNRSFGVEAIM	197
  1T-195	S. mutans	AASGFTYCASNGVWHPY	198
  1T-196	F. nucleatum	KPEKEKLDTNTLMKVVNKALSLFDRLL	199
  	S. sanguinis	IKFGA
  1T-197	A. naeslundii	TEILNFLITVCADRENWKIKHGLSDSVL	200
  	F. nucleatum	LIFFARFTGAEYW
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-198	P. gingivalis	MPVSKKRYMLSSAYATALGICYGQVAT	201
  	S. epidermidis	DEKESEITAIPDLLDYLSVEEYLL
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. sanguinis
  1T-199	S. sanguinis	RAGRIKKLSQKEAEPFEN	202
  1T-200	A. naeslundii	MRFKRFDRDYALSGDNVFEVLTASCDV	203
  	F. nucleatum	IERNLSYREMCGLMQ
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-201	S. sanguinis	KRKHENVIVAEEMRVIKN	204
  1T-202	A. naeslundii	LCRLEKLCKQFLRQDKVVTYYLMLPYK	205
  	F. nucleatum	RAIEAFYQELKERS
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-203	A. naeslundii	YPFCLATVDHLPEGLSVTDYERVQRLV	206
  	F. nucleatum	SQFLLNKEER
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. Mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-207	F. nucleatum	SPLEKYGTGSMTALTFLLGCCLLVLSKK	207
  	S. sanguinis	SR
  1T-208	Unanalyzed	KRKRWAILTLFLAGLGAVGIVLATF	208
  1T-215	S. sanguinis	VCFKDISVFLSPFRGQEVLFCGKAKHSL	209
  		IYVIGT
  1T-216	S. sanguinis	FFLNVIAIRIPHF	210
  1T-217	F. nucleatum	MLSNVLSRSVVSPNVDIPNSMVILSPLLI	211
  	S. sanguinis	SISNYH
  1T-218	F. nucleatum	KLIFAALGLVFLLIGLRDSRSK	212
  	S. sanguinis
  1T-219	S. sanguinis	RNINVSATFITEKSLV	213
  1T-221	A. naeslundii	DIGRIIGKKGRTITAIRSIVYSVPTQGKK	214
  	F. nucleatum	VRLVIDEK
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-222	F. nucleatum	RIEASLISAIMFSMFNAIVKFLQK	215
  	S. sanguinis
  1T-223	A. naeslundii	NQKMEINSMTSEKEKMLAGHFHNEAN	216
  	F. nucleatum	FAVIFKYSLFYNFF
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-225	A. naeslundii	RRSLGNSASFAEWIEYIRYLHYIIRVQFI	217
  	F. nucleatum	HFFSKNKKI
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. Mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-226	A. naeslundii	KLQEKQIDRNFERVSGYSTYRAVQAAK	218
  	F. nucleatum	AKEKGFISLEN
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-228	A. naeslundii	IFKLFEEHLLYLLDAFYYSKIFRRLKQGL	219
  	F. nucleatum	YRRKEQPYTQDLFRIVI
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-230	A. naeslundii	EFLEKFKVLKQPRKANNISKNRVAMIFL	220
  	F. nucleatum	TIHKSRGFLSSPY
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-233	A. naeslundii	TDQELEHLIVTELESKRLDFTYSKDITEF	221
  	P. gingivalis	FDEAFPEYDQNY
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-234	A. naeslundii	DNFYLILKMEERGKSKKTSQTRGFRAFF	222
  	F. nucleatum	DIIRKKIKKEDGK
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-237	S. sanguinis	EDPVPNHFTLRRNKKEKPSKS	223
  1T-238	A. naeslundii	IFNRRKFFQYFGLSKEAMVEHIQPFILDI	224
  	F. nucleatum	WQIHLF
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-239	A. naeslundii	ADDLLNKRLTDLIMENAETVKTIDLDN	225
  	S. gordonii	SD
  	S. mitis
  	S. mutans
  	S. oralis
  	S. sanguinis
  1T-240	A. naeslundii	VILGNGISNIAQTLGQLPNIAWVWIYMV	226
  	F. nucleatum	LIAALLEESNVC
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-242	F. nucleatum	KQVQNTTLIICGTVLLGILFKSYLKSQKS	227
  	S. sanguinis	V
  1T-243	A. naeslundii	SENIARFAAAFENEQVVSYARWFRRSW	228
  	P. gingivalis	RGSGSSSRF
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-248	S. sanguinis	IGGALNSCG	229
  1T-249	F. nucleatum	VFSVLKHTTWPTRKQSWHDFISILEYSA	230
  	S. sanguinis	FFALVIFIFDKLLTLGLAELLKRF
  1T-250	S. mitis	LVQGDTILIENHVGTPVKDDGKDCLIIR	231
  	S. mutans	EADVLAVVND
  	S. oralis
  1T-252	F. nucleatum	MKKNLKRFYALVLGFIIGCLFVSILIFIG	232
  	S. sanguinis	Y
  1T-253	A. naeslundii	KTKESLTQQEKKFLKDYDRKSLHHFRD	233
  	F. nucleatum	ILTYCFILDKLTNK
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-256	S. sanguinis	KGKSLMPLLKQINQWGKLYL	234
  1T-257	A. naeslundii	IILAKAADLAEIERIISEDPFKINEIANYDI	235
  	F. nucleatum	IEFCPTKSSKAFEKVLK
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-258	A. naeslundii	TINIDDKVLDYLKKINSKAITIDLIGCAS	236
  	F. nucleatum
  	P. gingivalis
  	T. denticola
  	S. mitis
  	S. mutans
  	S. oralis
  1T-259	F. nucleatum	EKLKKILLKLAVCGKAWYTL	237
  	P. gingivalis
  	T. denticola
  	S. mitis
  	S. mutans
  	S. oralis
  	S. sanguinis
  1T-260	A. naeslundii	NILYFIHDENQWEPQKAEIFRGSIKHCA	238
  	P. gingivalis	WLSS
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. sanguinis
  1T-261	F. nucleatum	SFEKNKIENNLKIAQAYIYIKPKPRICQA	239
  	S. mutans
  	S. oralis
  	S. sanguinis
  1T-262	A. naeslundii	LSLPLIVLTKSI	240
  	F. nucleatum
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-263	A. naeslundii	FIAVSFTGNPATFKLVIGCKADN	241
  	F. nucleatum
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-264	S. sanguinis	LEGKFYMAEDFDKTPECFKDYV	242
  1T-265	A. naeslundii	GMFENLLMINFQIMNDLKIEIVVKDRIC	243
  	F. nucleatum	AV
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-266	S. sanguinis	RAGTWLVVDEIR	244
  1T-267	A. naeslundii	RIKEERKNRSYKFFIWRLFDEKTGFI	245
  	F. nucleatum
  	P. gingivalis
  	T. denticola
  	S. mitis
  	S. mutans
  	S. oralis
  	S. sanguinis
  1T-268	F. nucleatum	PITPKKEKCGLGTYAPKNPVFSKSRV	246
  	S. mutans
  	S. oralis
  	S. sanguinis
  1T-269	F. nucleatum	PLYVAAVEKINTAKKH	247
  	S. mutans
  	S. oralis
  	S. sanguinis
  1T-270	F. nucleatum	VHEFDIQKILQNR	248
  	S. mutans
  	S. oralis
  	S. sanguinis
  1T-271	A. naeslundii	FLIQKFLLIKTFPPYRKKYVVIVSQTGTA	249
  	F. nucleatum
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-272	F. nucleatum	QLAPIDKQLKAVKKIAFYESESTAAKAV	250
  	S. mutans	TVA
  	S. oralis
  	S. sanguinis
  1T-273	F. nucleatum	YNEPNYKWLESYKIYKQRCEDRTGMY	251
  	P. gingivalis	YTEET
  	T. denticola
  	S. mitis
  	S. mutans
  	S. oralis
  1T-274	F. nucleatum	ETTTEINAIKLHRIKQRSPQGTRRVN	252
  	S. mutans
  	S. oralis
  	S. sanguinis
  1T-275	A. naeslundii	QVLKNFSISRRYKINNPFFKILLFIQLRTL	253
  	F. nucleatum
  	P. gingivalis
  	T. denticola
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-276	A. naeslundii	ILTLLILGSIGFFILKIKLKLGRF	254
  	F. nucleatum
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. sanguinis
  1T-277	A. naeslundii	IYYMRFVNKPLEKTFFKI	255
  	F. nucleatum
  	P. gingivalis
  	T. denticola
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-278	A. naeslundii	SINSSAGIQPHCLSSSFVLRTKHCFY	256
  	F. nucleatum
  	P. gingivalis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-279	A. naeslundii	FVLRTKHCFY	257
  	F. nucleatum
  	P. gingivalis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-280	A. naeslundii	TNNKNKVIIKAIKFKNKDFINLDLFIYRR	258
  	F. nucleatum
  	P. gingivalis
  	T. denticola
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-281	A. naeslundii	KYEKLTKENLFIRNSGNMCVFIYFLFFG	259
  	F. nucleatum
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-282	F. nucleatum	ISLVFPAYT	260
  	P. gingivalis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-283	A. naeslundii	LCTKLEDKQRGRIPAELFIISPIKILERND	261
  	F. nucleatum	AL
  	P. gingivalis
  	T. denticola
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-284	A. naeslundii	FQYYFSLKRV	262
  	F. nucleatum
  	P. gingivalis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-285	A. naeslundii	FFPYYLADFYKQLKFLNEYQTKNKDKV	263
  	F. nucleatum	VEFK
  	P. gingivalis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-286	S. sanguinis	LGFFNNKADLVKADTERDNRIVISSLKIK	264
  		DL
  1T-287	P. gingivalis	KGYPLPFQYRLNNH	265
  	T. denticola
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-288	F. nucleatum	RWVGGEPSADIYLSAKDTKT	266
  	S. gordonii
  	S. salivarius
  	S. sanguinis
  1T-289	F. nucleatum	EPSADIYLSAKDTKT	267
  	P. gingivalis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. sanguinis
  1T-290	A. naeslundii	IINQLNLILLRLMEILIL	268
  	F. nucleatum
  	P. gingivalis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-291	A. naeslundii	DMKIIKLYIKILSFLFIKYCNKKLNSVKL	269
  	F. nucleatum	KA
  	P. gingivalis
  	T. denticola
  	S. mitis
  	S. mutans
  	S. oralis
  1T-292	A. naeslundii	IINQLNLILLRLMEILIL	270
  	F. nucleatum
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-293	A. naeslundii	HVEDCFLLSNARTTAIHGRANPARGEPR	271
  	F. nucleatum	TRSE
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarious
  	S. sanguinis
  1T-294	T. denticola	YDKIADGVFKIGKRGVL	272
  1T-295	S. mitis	KYKLKKIIL	273
  	S. salivarious
  	S. sanguinis
  1T-296	A. naeslundii	EYSQQSFKAKPCSERGVLSP	274
  	F. nucleatum
  	P. gingivalis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-297	A. naeslundii	RSLRLNNALTKLPKLWYNRIKEAFYAY	275
  	F. nucleatum	NDYDK
  	T. denticola
  	S. mitis
  	S. mutans
  	S. oralis
  1T-298	A. naeslundii	ILNKKPKLPLWKLGKNYFRRFYVLPTFL	276
  	F. nucleatum	A
  	P. gingivalis
  	T. denticola
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-299	A. naeslundii	SMLTSFLRSKNTRSLKMYKDVHF	277
  	F. nucleatum
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-300	A. naeslundii	PLIISKAQIKMSGDILGSCFKLFYLRPFF	278
  	F. nucleatum
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-301	F. nucleatum	SKLPRVLDASLKL	279
  	S. gordonii
  	S. sanguinis
  1T-302	A. naeslundii	IIIILPKIYLVCKTV	280
  	P. gingivalis
  	S. epidermidis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-303	A. naeslundii	LDYENMDCKKRIRI	281
  	F. nucleatum
  	P. gingivalis
  	S. gordonii
  	S. mitis
  	S. mutans
  	S. oralis
  	S. salivarius
  	S. sanguinis
  1T-304	P. gingivalis	STAGEASRRTASEASRRTAAKLRG	282
  TT-305	F. nucleatum	ARNALNMRDVPVDAAIIGIIDGMDEE	283
  TT-306	F. nucleatum	KILNEAEGKLLKVIEKNGEIDIEEI	284
  TT-307	F. nucleatum	NGDKKAKEELDKWDEVIKELNIQF	285
  TT-308	F. nucleatum	GLVIIPNLIALIILFSQVRQQTKDYFSNPK	286
  		LSSR
  TT-309	F. nucleatum	EPLPLTKYDKKDTEMKKVFKEILAGKV	287
  		GYEKEEE
  TT-310	F. nucleatum	TKLKKNNKLLSAKKENTLHTKDK	288
  TT-311	S. mutans	AIFDAMHNL	289
  	S. sobrinus
  PVCFBP	P. fluorescens	DLys-Dorn-Gly-DThr-Thr-Gln-Gly-DSer-	290
  2461		cDOrn
  CHA0	P. fluorescens	Asp-DOrn-Lys-c(Thr-Ala-Ala-DOrn-Lys)	291
  CFBP2461	P. putida	Asp-Lys-DAsp-Ser-DThr-DAla-Thr-DLys-	292
  		cOrn
  NCPPB2192	P. tolaasii	DSer-Lys-Ser-DSer-Thr-DSer-Orn-Thr-	293
  		DSer-cDOrn
  PyC-E	P. aeruginosa	DSer-Arg-DSer-Orn-c(Lys-Orn-Thr-Thr)	294
  PyR	P. aeruginosa	DSer-Dab-Orn-DGln-Gln-DOrn-G1y	295
  PyPa TII	P. aeruginosa	DSer-DOrn-Orn-Gly-DThr-Ser-cOrn	296
  Py Pap	P. aptata	DAla-Lys-Thr-DSer-Orm-cOrn	297
  Py Pau	P. aureofaciens	DSer-DOrn-Gly-DThr-Thr-Gln-Gly-DSer-	298
  		cDOrn
  Ps	P. fluorescens	Lys-DAsp-Ala-DThr-Ala-cDOrn	299
  Py I-III	P. fluorescens	Asn-DOrn-Lys-c(Thr-DAla-DAla-DOrn-	300
  		Lys)
  Py Gm	P. fluorescens	DAla-Lys-Gly-Gly-Asp-DGln-DSer-Ala-	301
  		DAla-DAla-Ala-cOrn
  Py Pf 12	P. fluorescens	DSer-Lys-Gly-Orn-DSer-Ser-Gly-c(Lys-	302
  		DOrn-Glu-Ser)
  Py Pf	P. fluorescens	c(DSer-Dab)-Gly-Ser-Asp-Ala-Gly-DAla-	303
  2798		Gly-cOrn
  Py Pf	P. fluorescens	Ser-Lys-Gly-Orn-c(Lys-DOrn-Ser)	304
  13525
  Py Pf	P. fluorescens	DAla-DLys-Gly-Gly-Asp-DGln-Dab-Ser-	305
  17400		DAla-cOrn
  Py 51W	P. fluorescens	DAla-DLys-G1y-Gly-DAsp-DGln-DSer-Ala-	306
  		Gly-DThr-cOrn
  Py 9AW	P. fluorescens	DSer-Lys-His-DThr-Ser-cOrn	307
  Ps A225	P. fluorescens	DSer-DAla-DOrn-Gly-c(DSer-DAsp-DSer-	308
  		DThr)
  Py Pf 1.3	P. fluorescens	DAla-DLys-Gly-Gly-Asp-c(DGln-Dab)-Gly-	309
  		Ser-cOrn
  Py Pf	P. fluorescens	DSer-Lys-Gly-Orn-Ser-DSer-Gly-c(Lys-	310
  18.1		DOrn-Ser)
  Py Pf	P. fluorescens	DSer-DOrn-Ala-Gly-DThr-Ala-cOrn	311
  PL7
  Py Pf	P. fluorescens	DLys-DOrn-Ala-Gly-DThr-Ser-cOrn	312
  PL8
  Py Pf	P. fluorescens	DSer-DSer-Orn-DSer-DSer-c(DSer-Orn-	313
  BTP7		Lys-Lys)
  Ps 589A	P. putida	Asp-Lys-Asp-DSer-Thr-DAla-DGlu-DSer-	314
  		cOrn
  Py Pp
  1,2	P. putida	Ser-Thr-DSer-Orn-Asp-DGln-Dab-Ser-	315
  		DThr-cOrn
  Py Pp	P. putida	Asp-DOrn-DDab-Thr-Gly-DSer-Ser-Asp-	316
  C2,3		Thr
  Py G4R	P. putida	Asp-Orn-DAsp-Dab-Gly-Ser-cOrn	317
  Py	P. putida	Asp-DOrn-DDab-Thr-Gly-DSer-DSer-Thr-	318
  PpBTP16		Asp
  Py	P. puida	DSer-DAla-DOrn-Gly-DAla-DAsp-c(DSer-	319
  Pp39167		DThr)
  iPy Pp	P. putida	Asp-Ala-Asp-DOrn-Ser-cOrn	320
  BTP1
  Py	P. tolaasii	DSer-Lys-Ser-DSer-Thr-DSer-Orn-Thr-	321
  PT2192		DSer-Orn
  Ps 7SR1	Pseudomonas spp.	DSer-DAsp-DThr-c(DSer-D-Orn-Ala-Gly-	322
  		DSer)
  Ps A214	Pseudomonas spp.	DSer-DAla-Gly-DSer-DAla-DAsp-DThr-	323
  		DOrn
  Azoverdin	Pseudomonas spp.	Hse-DHse-Dab-DOrn-DSer-Orn	324
  		A.macrocytogenes
  PF-S024	Corynebacteria	SKRGRKRKDRRKKKANHGKRPNS	325
  	spp.
  PF-001	S. epidermidis	MNNWIIVAQLSVTVINEIIDIMKEKQKG	326
  	M. luteus	GK
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	E. faecalis
  	C. jeikeium
  PF-002	S. epidermidis	NDDAQ	327
  	P. mirabilis
  	C. albicans
  	C. jeikeium
  	C. jejuni
  PF-003	S. epidermidis	MNNWIKVAQISVTVINEVIDIMKEKQN	328
  	M. luteus	GGK
  	P. mirabilis
  	C. albicans
  	MRSA
  	C. jeikeium
  PF-004	S. epidermidis	ARLSKAIIIAVIVVYHLDVRGLF	329
  	B. subtilis
  	B. fragilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-005	S. epidermidis	MESIFKIKLMNGICRSENMNMKKKNKG	330
  	E. coli	EKI
  	MRSA
  	S. pneumoniae
  	E. faecalis
  PF-006	S. epidermidis	MGIIAGIIKFIKGLIEKFTGK	331
  	M. luteus
  	E. coli
  	P. aeruginosa
  	MRSA
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-007	S. epidermidis	MGIIAGIIKVIKSLIEQFTGK	332
  	M. luteus
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-008	S. epidermidis	MIEIGSIAYLNGGSKKYNHILNQENR	333
  	M. luteus
  	MRSA
  	C. jejuni
  PF-009	M. luteus	SKKYNHILNQENR	334
  	P. mirabilis
  	C. albicans
  PF-010	S. epidermidis	MDIDVNKLLQAFVYFKSFEKLRHNNS	335
  	M. luteus
  	E. coli
  	C. albicans
  PF-011	M. luteus	MFCYYKQHKGDNFSIEEVKNIIADNEM	336
  	E. coli	KVN
  	P. aeruginosa
  	S. pneumoniae
  	C. jeikeium
  PF-012	S. epidermidis	WRGPNTEAGGKSANNIVQVGGAPT	337
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	MRSA
  	S. pneumoniae
  	C. jeikeium
  	C. jejuni
  PF-013	M. luteus	LIQKGLNQTFIVVIRLNNFIKKS	338
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	MRSA
  	S. pneumoniae
  	C. jeikeium
  	C. jejuni
  PF-014	E. coli	HPTDNKHN	339
  	C. jeikeium
  PF-015	E. faecalis	SIDKRNLYNLKYYE	340
  	C. jeikeium
  PF-016	S. epidermidis	RKQYDDLSFNFLY	341
  	E. faecalis
  	C. jeikeium
  PF-017	E. coli	ESIIE	342
  PF-018	E. coli	YYKTYFKEV	343
  	C. jeikeium
  PF-020	S. epidermidis	MKIILLLFLIFGFIVVVTLKSEHQLTLFSI	344
  	M. luteus
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  PF-021	S. epidermidis	FSLNFSKQKYVTVN	345
  	M. luteus
  	P. mirabilis
  	E. coli
  	C. albicans
  	E. faecalis
  	C. jeikeium
  PF-022	M. luteus	MINELKNKNSGIMNNYVVTKESKL	346
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-023	M. luteus	MTKNTIISLENEKTQINDSENESSDLRKA	347
  	C. jeikeium	K
  PF-024	M. luteus	DLRKAK	348
  	C. albicans
  	MRSA
  	E. faecalis
  	C. jeikeium
  PF-025	S. epidermidis	LLIIFRLWLELKWKNKK	349
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	MRSA
  	E. faecalis
  	C. jejuni
  PF-026	S. epidermidis	SIHFIN	350
  	M. luteus
  	P. mirabilis
  	C. albicans
  	MRSA
  	E. faecalis
  	C. jeikeium
  PF-027	M. luteus	HNARKYLEFISQKIDGDKLTKEDSL	351
  	MRSA
  	E. faecalis
  	C. jejuni
  PF-028	S. epidermidis	ALDCSEQSVILWYETILDKIVGVIK	352
  	M. luteus
  	MRSA
  PF-029	S. epidermidis	NSTNE	353
  	M. luteus
  	C. albicans
  	C. jejuni
  PF-030	S. epidermidis	MTCHQAPTTTHQSNMA	354
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-031	M. luteus	MPHHSTTSSRIVVPAHQSNMASTPNLSI	355
  	C. albicans	TP
  PF-033	S. epidermidis	MFIFKTTSKSHFHNNVKSLECIKIPINKN	356
  	M. luteus	R
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  PF-034	M. luteus	EPKKKHFPKMESASSEP	357
  PF-035	S. epidermidis	SFYESY	358
  	M. luteus
  	E. coli
  	C. albicans
  	MRSA
  	C. jeikeium
  	C. jejuni
  PF-036	S. epidermidis	ILNRLSRIVSNEVTSLIYSLK	359
  	M. luteus
  	P. mirabilis
  	E. coli
  	C. albicans
  	MRSA
  	S. pneumoniae
  	C. jejuni
  PF-037	S. epidermidis	MTKKRRYDTTEFGLAHSMTAKITLHQA	360
  	M. luteus	LYK
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-038	M. luteus	MAYKDEGKETKFAVKGYKD	361
  PF-039	P. mirabilis	MLEEKNKSL	362
  	C. jeikeium
  PF-040	S. epidermidis	MIHLTKQNTMEALHFIKQFYDMFFILNF	363
  	M. luteus	NV
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-041	MRSA	ELLVILPGFI	364
  PF-042	S. epidermidis	LLLSYFRYTGALLQSLF	365
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-043	M. luteus	MIKNETAYQMNELLVIRSAYAK	366
  	C. jejuni
  PF-044	S. epidermidis	KLKKYIHKPD	367
  	M. luteus
  	MRSA
  	C. jeikeium
  PF-045	S. epidermidis	LDINDYRSTY	368
  	E. coli
  	E. faecalis
  	C. jejuni
  PF-046	E. coli	LDFYLTKHLTLML	369
  	E. faecalis
  	C. jeikeium
  PF-047	S. mutans	NQEPSLQQDKEQKDNKG	370
  PF-048	S. epidermidis	LYFAFKKYQERVNQAPNIEY	371
  	M. luteus
  	E. coli
  	MRSA
  	C. jeikeium
  	C. jejuni
  PF-049	S. epidermidis	AYYLKRREEKGK	372
  	MRSA
  	C. jeikeium
  	C. jejuni
  PF-050	S. epidermidis	SYYLKRREEKGK	373
  	M. luteus
  	E. coli
  	C. jeikeium
  PF-051	S. epidermidis	RFFNFEIKKSTKVDYVFAHVDLSDV	374
  	M. luteus
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  PF-052	S. epidermidis	QELINEAVNLLVKSK	375
  	M. luteus
  	E. coli
  	MRSA
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-053	S. epidermidis	KLFGQWGPELGSIYILPALIGSIILIAIVTL	376
  	M. luteus	ILRAMRK
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  PF-054	S. epidermidis	VSISRFIGGGHVFNGNNKRNL	377
  	E. coli
  PF-055	S. mutans	GHVFNGNNKRNL	378
  PF-056	S. epidermidis	AEQLFGKQKQRGVDLFLNRLTIILSILFF	379
  	M. luteus	VLMICISYLGM
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-057	S. epidermidis	TMIVISIPRFEEYMKARHKKWM	380
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-058	S. epidermidis	FADQSQDNA	381
  	M. luteus
  	E. coli
  	C. albicans
  	MRSA
  	C. jeikeium
  	C. jejuni
  PF-060	E. coli	HSSHL	382
  	C. albicans
  	C. jeikeium
  PF-061	S. epidermidis	GYNSYKAVQDVKTHSEEQRVTAKK	383
  	S. pneumoniae
  PF-062	S. epidermidis	MKKKRINNDILGRMIYSSSIDKRNLYNL	384
  	M. luteus	KYYE
  	E. coli
  	P. aeruginosa
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-063	S. epidermidis	IAAIIVLVLFQKGLLQIFNWILIQLQ	385
  	M. luteus
  	E. coli
  	P. aeruginosa
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-064	E. coli	DYYGKE	386
  PF-065	M. luteus	LEKNTRDNYFIHAIDRIYINTSKGLFPES	387
  	E. coli	ELVAWG
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	C. jeikeium
  	C. jejuni
  PF-066	M. luteus	IKGTVKAVDETTVVITVNGHGTELTFEK	388
  	E. coli	PAIKQVDPS
  	C. jeikeium
  PF-067	S. epidermidis	DLIVKVHICFVVKTASGYCYLNKREAQ	389
  	M. luteus	AAI
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-068	S. epidermidis	SHLINNFGLSVINPSTPICLNFSPVFNLLT	390
  	M. luteus	VYGITCN
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-069	E. faecalis	FDPVPLKKDKSASKHSHKHNH	391
  	C. jejuni
  PF-070	S. epidermidis	SMVKSEIVDLLNGEDNDD	392
  	C. jejuni
  PF-071	S. epidermidis	HCVIGNVVDIANLLKRRAVYRDIADVIK	393
  	E. coli	MR
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-073	S. epidermidis	CPSVTMDACALLQKFDFCNNISHFRHFF	394
  	M. luteus	AIKQPIER
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  PF-074	S. epidermidis	RDIHPIYFMTKD	395
  	M. luteus
  	MRSA
  PF-075	M. luteus	FVNSLIMKDLSDNDMRFKYEYYNREKD	396
  	E. coli	T
  	P. aeruginosa
  	MRSA
  	C. jeikeium
  PF-076	S. epidermidis	LYQYELLSKEEYLKCTLIINQRRNEQK	397
  	M. luteus
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-097	C. jeikeium	QPTQGEQGTRPRRPTPMRGLLI	398
  PF-099	S. epidermidis	EIIAYLEGRFANA	399
  	M. luteus
  	E. coli
  	C. jeikeium
  PF-101	S. mutans	DPVPERQEQACACHRTAKPGK	400
  PF-104	MRSA	ERTAVNDLWI	401
  	C. jeikeium
  PF-123	M. luteus	TTRPQVAEDRQLDDALKETFPASDPISP	402
  	E. coli
  PF-124	S. epidermidis	MADGQIAAIAKLHGVPVATRNIRHFQSF	403
  	M. luteus	GVELINPWSG
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	E. faecalis
  	C. jejuni
  PF-125	S. epidermidis	YVVGALVILAVAGLIYSMLRKA	404
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jejuni
  PF-126	S. epidermidis	FSPEAFGIGAAGVLGSFVTGLLIGWVAS	405
  	M. luteus	LLRKAK
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-127	S. epidermidis	MLRYLSLFAVGLATGYAWGWIDGLAA	406
  	M. luteus	SLAV
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  PF-128	M. luteus	GIKVVAARFEEIQFSENFDSIILA	407
  	P. aeruginosa
  	E. faecalis
  PF-129	S. epidermidis	MKLLARDPWVCAWNDIW	408
  	MRSA
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-130	E. faecalis	LQRSDEESMPRRHEKYS	409
  	C. jeikeium
  	C. jejuni
  PF-131	S. epidermidis	RRAAARTKGNRR	410
  	E. coli
  	MRSA
  	C. jeikeium
  PF-132	S. epidermidis	RPGDGAAEQGRSR	411
  	C. jeikeium
  PF-133	S. epidermidis	GDPTAGQKPVECP	412
  	C. jeikeium
  	C. jejuni
  	M. smegmatis
  PF-134	S. epidermidis	GKANIKRQDCSAL	413
  	C. jeikeium
  PF-135	S. epidermidis	PPARPARIPQTPTLHGASLFRQRS	414
  	M. luteus
  	E. coli
  	P. aeruginosa
  	MRSA
  	C. jeikeium
  	M. smegmatis
  PF-136	S. epidermidis	LRGRVGRITACGYPP	415
  	M. luteus
  	P. mirabilis
  	E. coli
  	MRSA
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  	M. smegmatis
  PF-137	S. epidermidis	VLGKGHDLLDVGKTALKSRVFAWLGG	416
  	P. mirabilis	S
  	S. pneumoniae
  	C. jeikeium
  	C. jejuni
  PF-138	S. epidermidis	AVHHSLLFR	417
  	M. luteus
  	P. mirabilis
  	E. coli
  	C. albicans
  	MRSA
  	C. jeikeium
  	C. jejuni
  PF-139	S. epidermidis	ALSKPAIQARTLCRRQDPP	418
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-140	S. epidermidis	FHRRVIRASEWALTTRSFSTPLRSAAR	419
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  	M. smegmatis
  PF-141	S. epidermidis	VVRRFQGM	420
  	M. luteus
  	C. albicans
  	MRSA
  	C. jeikeium
  PF-142	S. mutans	GIDRGCQAAR	421
  PF-143	S. epidermidis	LSPRPIIVSRRSRADNNNDWSR	422
  	MRSA
  	C. jeikeium
  PF-144	S. epidermidis	RSGQPVGRPSRRAWLR	423
  	M. luteus
  	E. coli
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-145	S. epidermidis	GIVLTGRAGLVSGACSMALGVGLG	424
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  	M. smegmatis
  PF-146	S. epidermidis	GCGKRRIITKSASRDTR	425
  	M. luteus
  	P. aeruginosa
  	C. albicans
  	MRSA
  	C. jeikeium
  PF-147	S. epidermidis	RRPRRRRSGHGQSASAA	426
  	M. luteus
  	MRSA
  PF-148	S. epidermidis	RRGCTERLRRMARRNAWDLYAEHFY	427
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  	M. smegmatis
  PF-149	S. epidermidis	GKVSVLTRVPRSLGGAPANQ	428
  	M. luteus
  	E. coli
  	MRSA
  	C. jeikeium
  PF-150	S. epidermidis	EIQAKGTG	429
  	MRSA
  PF-151	S. epidermidis	EEYPARVPLSGEDVTEARRH	430
  	MRSA
  	E. faecalis
  	C. jeikeium
  PF-152	S. epidermidis	VGYFIWKDSHSRKG	431
  	C. albicans
  	MRSA
  	E. faecalis
  	C. jeikeium
  PF-153	M. luteus	GILARADCSQIA	432
  	P. mirabilis
  	E. coli
  	MRSA
  PF-154	S. mutans	GIKKSKHPSTDDYVVKTTIDSL	433
  PF-155	C. jeikeium	GRYGDDSKERQGRAQ	434
  PF-156	S. epidermidis	LITAEQPATAPIAGK	435
  	C. jeikeium
  PF-157	S. epidermidis	HTAVVWLAGVSGCVALSHCEPA	436
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-158	S. epidermidis	VRLESRPADLPE	437
  PF-159	S. epidermidis	TMAFVEKAQLRVPVGDDLPV	438
  PF-160	S. epidermidis	SFHASLTKNEKPIKSTG	439
  PF-161	S. epidermidis	RGRALASTATTRPARRRR	440
  	M. luteus
  	E. coli
  	C. jejuni
  PF-162	S. epidermidis	GIRRLHSVENLNREISHRMAGLR	441
  	MRSA
  PF-163	S. epidermidis	TSWLRAAERQEIGEPTKTFGEKTTSL	442
  PF-164	S. epidermidis	EEVSRALAGIGLGLGCRIG	443
  	M. luteus
  	E. coli
  	C. jeikeium
  PF-165	MRSA	GPVSVVASLRRGTTVQRHSQNNHNKG	444
  	C. jejuni	KP
  PF-166	E. coli	SKAVSRKRSI	445
  	C. jeikeium
  PF-167	S. epidermidis	AIEGVIKKGACFKLLRHEMF	446
  	E. coli
  	C. albicans
  	MRSA
  	C. jeikeium
  	C. jejuni
  PF-168	S. epidermidis	VLPFPAIPLSRRRACVAAPRPRSRQRAS	447
  	M. luteus
  	E. coli
  	C. albicans
  	MRSA
  	C. jeikeium
  	C. jejuni
  PF-169	S. epidermidis	APGSAADSPRSRADD	448
  	E. coli
  	C. albicans
  	E. faecalis
  	C. jeikeium
  PF-170	S. epidermidis	RLARGRPTNLCGRRG	449
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jejuni
  PF-171	S. epidermidis	TQVTLCRTW	450
  	E. coli
  	P. aeruginosa
  	S. pneumoniae
  PF-172	S. epidermidis	LTGVRRPWRAPWAGTSGWALR	451
  	M. luteus
  	E. coli
  	P. aeruginosa
  	MRSA
  	E. faecalis
  	C. jejuni
  PF-173	S. epidermidis	AGRTAIVQGGG	452
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	C. jeikeium
  	C. jejuni
  PF-174	S. epidermidis	RGGDSPARRRPGLAGPGGPG	453
  	P. aeruginosa
  	C. jeikeium
  PF-175	S. epidermidis	RRRPAGQRPEKASQAMIAA	454
  	E. faecalis
  PF-176	S. epidermidis	RLTSNQFLTRITPFVFAQH	455
  	M. luteus
  	P. mirabilis
  	E. coli
  	C. albicans
  	MRSA
  	E. faecalis
  	C. jeikeium
  PF-177	M. luteus	VTSEPGIAHDIRLLPRAAAFR	456
  	MRSA
  	E. faecalis
  	C. jeikeium
  PF-178	S. epidermidis	EVYSSPTNNVAITVQNN	457
  	M. luteus
  	B. subtilis
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-180	S. epidermidis	SGLGDLGFSSEAK	458
  	M. luteus
  	P. aeruginosa
  	C. albicans
  	MRSA
  	E. faecalis
  	C. jejuni
  	M. smegmatis
  PF-181	S. epidermidis	GIAPRRNEWGAVGGR	459
  	M. luteus
  	E. coli
  	MRSA
  	E. faecalis
  	C. jeikeium
  PF-182	S. epidermidis	LPATRDKTRVPASVAGAP	460
  	M. luteus
  	E. coli
  	E. faecalis
  	C. jeikeium
  PF-183	S. epidermidis	KPGISVENRQ	461
  	M. luteus
  	E. coli
  	C. albicans
  	MRSA
  	E. faecalis
  	C. jeikeium
  PF-184	S. epidermidis	LIADRHIRA	462
  	M. luteus
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	C. jeikeium
  PF-185	E. coli	RPAQARQGPGGLIADRHIRA	463
  	P. aeruginosa
  PF-186	S. epidermidis	DADKNLSLERDRFAWRVAAP	464
  	M. luteus
  	E. coli
  	P. aeruginosa
  	MRSA
  	C. jeikeium
  PF-187	S. epidermidis	EIQKIAKGVSGQVYGPSRQITISKKR	465
  	M. luteus
  	E. coli
  	MRSA
  PF-188	S. epidermidis	ARTFAGRLGTRYFGGLMRSTKA	466
  	M. luteus
  	E. coli
  	C. albicans
  	MRSA
  	E. faecalis
  PF-189	S. epidermidis	GNLTRSREAARATQ	467
  	M. luteus
  	C. albicans
  	MRSA
  	E. faecalis
  	C. jejuni
  PF-190	S. epidermidis	HFILRKPLLFMIHSLKTGPLDRF	468
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-191	E. coli	QFCNFAWLFLASNNAQVSALA	469
  	P. aeruginosa
  	C. jejuni
  PF-192	S. epidermidis	VEEDEAPPPHY	470
  	M. luteus
  	P. aeruginosa
  	C. albicans
  	E. faecalis
  	C. jeikeium
  PF-193	S. epidermidis	PPHCPPGHAKKGWC	471
  	M. luteus
  	E. coli
  	MRSA
  	E. faecalis
  	C. jejuni
  PF-194	C. jeikeium	MKGNKLATAHEQPVKNSAPPL	472
  PF-195	S. epidermidis	EMAEGSADDRLRKTPRDC	473
  	M. luteus
  	E. faecalis
  	C. jeikeium
  PF-196	S. epidermidis	TTARYIRRQCHTSITPLSQG	474
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jejuni
  PF-197	S. epidermidis	CNALLRRGHPPSAL	475
  	M. luteus
  	C. albicans
  	E. faecalis
  	C. jejuni
  PF-200	S. epidermidis	GIELKSLIMAQIERWRQA	476
  	M. luteus
  	MRSA
  	E. faecalis
  	C. jeikeium
  PF-201	S. epidermidis	GCRPASLSDADPDGR	477
  	M. luteus
  	E. coli
  	C. albicans
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-202	S. epidermidis	ALNRASLRLALGE	478
  	M. luteus
  	E. coli
  	MRSA
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-203	S. epidermidis	SWKCHHLAI	479
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jejuni
  PF-204	S. epidermidis	ALQKQDMNLPSVKNQLVFLKSTG	480
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	C. jejuni
  PF-205	S. epidermidis	AGVLETPRCRGEYGAN	481
  	M. luteus
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-206	M. luteus	KLRSASKKSLQEKSCGIMPEKPAG	482
  	C. albicans
  	C. jeikeium
  	C. jejuni
  PF-207	M. luteus	AAGCRDLGSLSSLVTNPS	483
  	C. jeikeium
  PF-208	S. epidermidis	DAYHCHLVRSPDAHDLSMRIGFV	484
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-209	C. albicans	NYAVVSHT	485
  	C. jeikeium
  	C. jejuni
  PF-210	S. epidermidis	EREDGCDAMPLP	486
  	P. aeruginosa
  	C. albicans
  	MRSA
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-211	S. epidermidis	DSFDSLSPFRERGGEREDGCDAMPLP	487
  	M. luteus
  	E. coli
  	P. aeruginosa
  	C. albicans
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  	M. smegmatis
  PF-212	M. luteus	NDSKASN	488
  	P. aeruginosa
  PF-213	S. epidermidis	MTTGVDFIIEKV	489
  PF-214	S. mutans	GHLRVCWVFSASLLTPFRSATLI	490
  	S. epidermidis
  	M. luteus
  	E. coli
  	P. aeruginosa
  	A. baumannii
  PF-215	S. epidermidis	ELKITNYNVNTVLYRYYKWGNDLCE	491
  	M. luteus
  	P. aeruginosa
  	A. baumannii
  PF-216	S. mutans	ESVDKITEALEEDGFPAKVQ	492
  	E. coli
  PF-217	S. mutans	DWEFTHKTIPQKK	493
  PF-218	S. epidermidis	SETPEKPVGTFFYSIYYKIIL	494
  	M. luteus
  	P. aeruginosa
  	A. baumannii
  PF-219	S. epidermidis	FLALAVIAGLFKVILIYAAPYLK	495
  	M. luteus
  	P. aeruginosa
  	A. baumannii
  PF-221	S. epidermidis	VFDNIDINF	496
  	M. luteus
  	P. aeruginosa
  PF-222	S. epidermidis	HIKETR	497
  PF-223	S. epidermidis	VKFCIECQTKLERKRR	498
  	M. luteus
  	A. baumannii
  PF-224	S. epidermidis	DYFYITLSQKNTF	499
  	P. aeruginosa
  	A. baumannii
  PF-225	S. epidermidis	MNCASPEFKKLMELYK	500
  PF-226	A. baumannii	LMFFSENMDKRDTLSGKFRYFAGSKVI	501
  		KLMNWLSENGK
  PF-228	S. mutans	NQLGSQAFAQL	502
  PF-229	S. epidermidis	DPILIQIGFTRFALRKAEAEKIEIQVEEGV	503
  	M. luteus	PA
  	P. aeruginosa
  	A. baumannii
  PF-230	S. mutans	EDKPTNTIQEIKPVKWQ	504
  PF-231	S. mutans	AVRDFKKSVREEDEAASLNSPRTIDAQ	505
  		VKTSESTSVKS
  PF-232	S. epidermidis	FDQLYALEREGKLDELLA	506
  	M. luteus
  PF-233	S. epidermidis	DANAMARTTIAIVYILALIALTISYSL	507
  	M. luteus
  	P. aeruginosa
  	A. baumannii
  PF-234	S. epidermidis	RTPYILRS	508
  	M. luteus
  PF-235	S. epidermidis	GIPFSKPHKRQVNYMKSDVLAYIEQNK	509
  	M. luteus	MAHTA
  PF-236	S. mutans	KEIRTATVAELNAKRRLTSAEQALAEVS	510
  	S. epidermidis
  	E. coli
  	C. albicans
  	S. pneumoniae
  	E. faecalis
  PF-237	S. epidermidis	YVKPKVGVHE	511
  PF-238	S. mutans	RNAVVVTEATFPKYEEEITNYLNRRFGE	512
  	S. epidermidis	DWSLKLEKCSVA
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  PF-239	S. mutans	PKHNVVTGVSVDLDYKP	513
  	E. coli
  PF-240	S. mutans	RITEVPPDEHSDR	514
  	E. coli
  PF-242	S. mutans	KLFEDPLIKSKAVENFQTTWHEQCLAK	515
  	E. coli	ELAKNM
  PF-244	S. epidermidis	HMRTISYLLAFAKFSLFIPPKQSLKRL	516
  	M. luteus
  	P. aeruginosa
  	A. baumannii
  PF-245	S. epidermidis	MNDVKPVVQPKQTLKAFLVQLLSVRA	517
  	M. luteus	GVYIKQNNQLPKTKG
  	P. aeruginosa
  	A. baumannii
  PF-246	S. mutans	QPDEKAEFFDPSLDKVYRHPTFYHIPDG	518
  		IEHM
  PF-247	S. epidermidis	ETAASETH	519
  PF-248	S. mutans	ILSKLWFWMINSLGVVLLVSYWLLAK	520
  	S. epidermidis	WGVA
  	M. luteus
  	E. coli
  	P. aeruginosa
  	A. baumannii
  PF-249	S. epidermidis	INSRYKISF	521
  	M. luteus
  PF-252	S. mutans	MKKLVAALAVIVILTGCVYDPVNYDKI	522
  		HDQEFQDHLRQNG
  PF-253	S. epidermidis	VRDDDS	523
  	M. luteus
  PF-254	S. epidermidis	FIYGVGFVPHFWLWKWLFSPWIAWPL	524
  	M. luteus	MLLGYYIWFLT
  	P. aeruginosa
  	A. baumannii
  PF-255	P. aeruginosa	DHKINESQHNPFRSDSNKQNVDFF	525
  PF-256	S. epidermidis	EYFKQVYVKNEKIYSFWICKDLSPKEA	526
  		AKRAEDILVKLK
  PF-257	S. epidermidis	VWENRKKYLENEIERHNVFLKLGQEVI	527
  		KGLNALASRGR
  PF-259	S. epidermidis	LPFSKIGRRVSYKKKDVLKYEQSKTVL	528
  	P. aeruginosa	NTAQLATV
  	A. baumannii
  PF-262	S. mutans	DPHSEIDVTRYCQLHHFTCQTMQISERE	529
  	S. epidermidis	FHYLIETQ
  	M. luteus
  	E. coli
  	P. aeruginosa
  	A. baumannii
  PF-263	S. epidermidis	NLKKCPC	530
  	M. luteus
  	A. baumannii
  PF-265	S. epidermidis	MKTLFFPLFLIIFVLIIQALDQSYQKKIGI	531
  	M. luteus	SKPQKHPEFMQ
  	A. baumannii
  PF-266	S. mutans	DQEKKNKTEESTEQ	532
  PF-267	M. luteus	SDDKRTD	533
  PF-268	S. mutans	EVLLSDLRPDIFSET534
  PF-270	S. epidermidis	MYLTPYAWIAVGSIFAFSVTTIKIGDQN	535
  	M. luteus	DEKQKSHKNDVHKR
  	P. aeruginosa
  PF-271	S. epidermidis	AAQPQTTSP	536
  	M. luteus
  	P. aeruginosa
  	A. baumannii
  PF-273	S. epidermidis	LVGALLIFVALIYMVLKGNADKN	537
  	M. luteus
  	P. aeruginosa
  	A. baumannii
  PF-275	S. mutans	LVSGVANTVKNTAHTVGNTAKHAGHV	538
  		AADTTVKATKKQQVK
  PF-276	S. epidermidis	LDLALSTNSLNLEGFSF	539
  PF-278	M. luteus	LSLATFAKIFMTRSNWSLKRFNRL	540
  	A. baumannii
  PF-279	S. mutans	SHIGFISISACLAVLLGIARLFVWTWVKF	541
  	S. epidermidis	FA
  	M. luteus
  	E. coli
  	P. aeruginosa
  	A. baumannii
  PF-281	S. mutans	SYNTYYNKLIHGQRTPDGM	542
  	E. coli
  PF-282	S. mutans	QNNDTSAWCGSAHKNGNS	543
  PF-283	B. subtilis	MIRIRSPTKKKLNRNSISDWKSNTSGRF	544
  	B. fragilis	FY
  	C. difficile
  PF-284	C. difficile	MRYITYSLIPRLLSKKVIHQQ	545
  PF-285	S. mutans	VPAKLLRVIDEIPE	546
  PF-288	S. mutans	IYQLLNIEYSEDD	547
  	E. coli
  PF-289	C. difficile	MGRHLWNPSYFVATVSENTEEQIRKYR	548
  		KNK
  PF-291	S. mutans	DVDGAIESEL	549
  	E. coli
  PF-292	S. epidermidis	SFVSTTVRLIFEESKRYKF	550
  	B. subtilis
  	B. fragilis
  PF-294	S. epidermidis	DFLVNFLWFKGELNWGKKRYK	551
  	C. difficile
  PF-295	C. difficile	NIQVYESECGNYIFKKSDESFLIDIFDKN	552
  		GTH
  PF-297	S. epidermidis	ISKGIDDIVYVINKILSIGNIFKIIKRK	553
  	B. subtilis
  	B. fragilis
  PF-299	B. subtilis	LATKLKYEKEHKKM	554
  PF-300	B. subtilis	VKDVLLELFNKIIGA	555
  	C. difficile
  PF-301	C. difficile	GIVLIGLKLIPLLANVLN	556
  PF-304	S. mutans	LVKDTSDIKNDLNNIEIVTSKNSNDIAKL	557
  		KSVK
  PF-305	C. difficile	MREWICPSCNETHDRDINASINILKEGL	558
  		RLITIQNK
  PF-306	C. difficile	GCILPHKKDNYNYIMSKFQDLVKITSKK	559
  PF-307	S. epidermidis	MKRRRCNWCGKLFYLEEKSKEAYCCK	560
  	B. subtilis	ECRKKAKKVKK
  	B. fragilis
  	C. difficile
  PF-308	C. difficile	QQYLILDRM	561
  PF-309	S. mutans	GIPGMTAAPAEENEQEENADEE	562
  	E. coli
  PF-311	C. difficile	IDAVTKKKTTCMIRAPTKIPIAHTDN	563
  PF-313	S. epidermidis	YITSHKNARAIIKKFERDEILEEVITHYL	564
  	C. difficile	NRK
  PF-314	S. mutans	ECLKKAIKSKALNKAFKIDVPDEVYDN	565
  		LLMELEEYEK
  PF-317	S. mutans	LILVSDI	566
  PF-319	S. epidermidis	SIGSMIGMYSFREIKTKHIKFTFGIPFILFL	567
  	B. subtilis	QFLLVYFYILK
  	C. difficile
  PF-320	S. mutans	DSGYYALLENKEERVVWDGEVVANNI	568
  	E. coli	FNNLWIVVNKVKTG
  PF-323	S. mutans	ARESIEKSHVPVDATIVGVVDSFEVFDE	569
  PF-324	C. dffficile	HFSLL	570
  PF-325	S. mutans	LTIDEKLRNHR	571
  	E. coli
  PF-326	S. mutans	VIVGNLGAQKEKRNDTPISAKKDIIVIGD	572
  	E. coli	KTVRVRADLHH
  PF-328	S. mutans	NGNEKAFSEVENLVK	573
  PF-329	S. epidermidis	IGILFDKSVRKY	574
  PF-333	S. mutans	YMTKKLVEMAEQQMAGKSNR	575
  PF-334	S. epidermidis	QQYLILDRM	576
  	C. dffficile
  PF-336	S. mutans	MLTSRKKRLKKIVEEQNKKDESI	577
  	E. coli
  PF-337	S. epidermidis	YMTKKLVEMAERQMAGK	578
  PF-338	S. mutans	KGTSCPDQLSKAIRQSI	579
  PF-340	S. mutans	VKDVLLELFNKIIGA	580
  	E. coli
  PF-344	B. subtilis	DERLPEAKAIRNFNGSVMVLGR	581
  	C. jejuni
  PF-347	S. epidermidis	GIFTGVTVVVSLKHC	582
  	B. subtilis
  	B. fragilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  PF-348	B. subtilis	ESASAAEWYNPNMNVKKAICMG	583
  	E. coli
  	P. aeruginosa
  	C. albicans
  	E. faecalis
  	C. jejuni
  PF-349	S. epidermidis	MPKSCHVPVLCDFFFLVIIKFLALFKTIQ	584
  	B. subtilis	S
  	B. fragilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-350	S. epidermidis	LAVILRAIVY	585
  	E. coli
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-351	S. mutans	YLFFKGKKVAEEEATKDEVKR	586
  PF-352	C. jeikeium	RVKKIG	587
  PF-353	S. epidermidis	EKTNFKGVKRNFYKKASFFV	588
  	M. luteus
  	B. subtilis
  	E. coli
  	C. albicans
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-354	S. epidermidis	FTFSKCRASNGRGFGTLWL	589
  	B. subtilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-355	S. epidermidis	WIAIGLLLYFSLKNQ	590
  	B. subtilis
  	B. fragilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-356	S. epidermidis	VSIKIGAIVIGMIGLMELLTE	591
  	B. subtilis
  	B. fragilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-357	S. epidermidis	MLTIIIGFIFWTMTLMLGYLIGEREGRK	592
  	M. luteus	RE
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-358	S. epidermidis	RNTAHNIKWRSKN	593
  	B. subtilis
  	E. coli
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-359	S. epidermidis	MTVMEDPGSEQRNKIQSPMKGEDFSAL	594
  	B. fragilis	FGR
  	P. aeruginosa
  	C. albicans
  	MRSA
  	E. faecalis
  	C. jeikeium
  PF-360	S. epidermidis	MEQKVKVIFVPRSKPDNQLKTFVSAVL	595
  	B. subtilis	FKA
  	E. coli
  	P. aeruginosa
  	C. albicans
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-361	S. epidermidis	NQVTEGIRLLVE	596
  	E. coli
  	E. faecalis
  	C. jejuni
  PF-362	S. epidermidis	NIERILKEKVWMIRCVE	597
  	E. coli
  	P. aeruginosa
  	C. albicans
  	E. faecalis
  	C. jejuni
  PF-363	B. subtilis	SMLSVTVMCLMHASVAANQAMEKKV	598
  	E. coli
  	P. aeruginosa
  	C. albicans
  	S. pneumoniae
  	E. faecalis
  PF-364	S. epidermidis	LVNGIKI	599
  	B. fragilis
  	P. aeruginosa
  	C. jeikeium
  	C. jejuni
  PF-365	S. epidermidis	LYKQKIQLEEELEKLKDDRQ	600
  	B. subtilis
  	B. fragilis
  	P. aeruginosa
  	C. albicans
  PF-366	S. epidermidis	ALCSVIKAIELGIINVHLQ	601
  	M. luteus
  	B. fragilis
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-367	B. subtilis	TKTPGTFTPGTGIQKTAVPL	602
  PF-368	C. jeikeium	MLKQTA	603
  	C. jejuni
  PF-369	B. subtilis	MSEAVNLLRGARYSQRYAKNQVPYEVI	604
  	B. fragilis	IEK
  	E. coli
  	P. aeruginosa
  	C. albicans
  	S. pneumoniae
  	C. jeikeium
  	C. jejuni
  PF-370	S. epidermidis	VIFLHKESGNLKEIFY	605
  	E. coli
  	P. aeruginosa
  	E. faecalis
  	C. jejuni
  PF-371	S. epidermidis	TFIYNEF	606
  	B. fragilis
  	C. jejuni
  PF-372	C. jeikeium	KKQDKRIEDKYKRMKKGD	607
  	C. jejuni
  PF-373	S. epidermidis	HFYLLFER	608
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	E. faecalis
  	C. jejuni
  PF-374	S. epidermidis	HLFFVKGMFILCQKNQINDE	609
  	B. subtilis
  	B. fragilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-375	S. epidermidis	MDSAKAQTMRTDWLAVSCLVASAYLR	610
  	B. subtilis	SMLA
  	B. fragilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-376	S. epidermidis	MTVFEALMLAIAFATLIVKISNKNDKK	611
  	B. subtilis
  	B. fragilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-378	B. subtilis	ESAKSNLNFLMQEEWALFLLL	612
  	B. fragilis
  	E. coli
  	P. aeruginosa
  	C. jeikeium
  PF-379	S. epidermidis	VFVVLFIIYLASKLLTKLFPIKK	613
  	B. subtilis
  	B. fragilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-380	S. epidermidis	KKIIPLITLFVVTLVG	614
  	B. subtilis
  	B. fragilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-381	E. coli	QGANPCQQVGFTVNDPDCRLAKTV	615
  	P. aeruginosa
  	C. jejuni
  PF-382	S. epidermidis	KYKCSWCKRVYTLRKDHKTAR	616
  	B. subtilis
  	B. fragilis
  	E. coli
  	P. aeruginosa
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-383	S. epidermidis	WSEIEINTKQSN	617
  	B. subtilis
  	B. fragilis
  	E. coli
  	C. jejuni
  PF-384	E. faecalis	HISKERFEAY	618
  	C. jeikeium
  	C. jejuni
  PF-385	S. epidermidis	MIKKSILKIKYYVPVLISLTLILSA	619
  	E. coli
  	P. aeruginosa
  	C. albicans
  	E. faecalis
  PF-386	S. epidermidis	FTLTLITTIVAILNYKDKKK	620
  	B. subtilis
  	B. fragilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-387	B. subtilis	GAVGIAFFAGNMKQDKRIADRQNKKSE	621
  	E. coli	KK
  	P. aeruginosa
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-388	E. faecalis	ITPLLDEIGKVCIDKISK	622
  	C. jeikeium
  	C. jejuni
  PF-389	S. epidermidis	GLQFKEIAEEFHITTTALQQWHKDNGY	623
  	C. albicans	PIYNKNNRK
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-390	S. epidermidis	VVAYVITQVGAIRF	624
  	P. aeruginosa
  	C. albicans
  	MRSA
  PF-392	S. epidermidis	DPAGCNDIVRKYCK	625
  	B. subtilis
  	S. pneumoniae
  	C. jeikeium
  	C. jejuni
  PF-393	S. epidermidis	DLVQSILSEFKKSG	626
  	E. coli
  	C. albicans
  	MRSA
  	S. pneumoniae
  	C. jejuni
  PF-394	S. epidermidis	VLKEECYQKN	627
  	MRSA
  	C. jejuni
  PF-395	S. epidermidis	YCVPLGNMGNMNNKIW	628
  	E. coli
  	P. aeruginosa
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-396	S. epidermidis	LIYTILASLGVLTVLQAILGREPKAVKA	629
  	E. coli
  	P. aeruginosa
  	C. albicans
  	E. faecalis
  	C. jeikeium
  PF-397	S. epidermidis	VEDLMEDLNA	630
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jejuni
  PF-398	S. epidermidis	ILVVLAGILLVVLSYVGISKFKMNC	631
  	B. subtilis
  	B. fragilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-399	S. epidermidis	FPIISALLGAIICIAIYSFIVNRKA	632
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jejuni
  PF-400	S. epidermidis	VIAWKFRNKFENSGV	633
  	E. coli
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-401	S. epidermidis	YWLSRVTTGHSFAFEKPVPLSLTIK	634
  	E. coli
  	P. aeruginosa
  	MRSA
  	E. faecalis
  	C. jejuni
  PF-402	S. epidermidis	FIDVLKSKINEFLN	635
  	P. aeruginosa
  	E. faecalis
  	C. jejuni
  PF-403	E. coli	LLSTEQLLKYYDGETFDGFQLPSNE	636
  	P. aeruginosa
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-404	S. epidermidis	VLYFQATVV	637
  	E. coli
  	P. aeruginosa
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-405	S. epidermidis	LVRIEVDDLEEWYERNFI	638
  	E. coli
  	E. faecalis
  PF-406	E. coli	YLEMNADYLSNMDIFDELWEKYLENN	639
  	C. jejuni	K
  PF-407	S. epidermidis	KPKNKKEKTVISYEKLLSMY	640
  	B. subtilis
  	E. coli
  	P. aeruginosa
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-408	S. epidermidis	YCVPLGNMGNMNNKIW	641
  	E. coli
  	P. aeruginosa
  	MRSA
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-409	S. epidermidis	DLVQSILSEFKKSG	642
  	MRSA
  	C. jeikeium
  	C. jejuni
  PF-410	S. epidermidis	FALELIALCRNLFIVYFP	643
  	M. luteus
  	B. fragilis
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  PF-411	M. luteus	WVAVAILLNIALQTQLT	644
  	B. subtilis
  	B. fragilis
  	P. mirabilis
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-412	M. luteus	TSGWLGQLEQ	645
  	E. coli
  	C. albicans
  	C. jeikeium
  	C. jejuni
  PF-413	P. aeruginosa	TFAGSIKIGVPDLVHVTFNCKR	646
  	C. albicans
  	C. jejuni
  PF-414	E. coli	LLNKKLE	647
  	C. albicans
  	C. jeikeium
  PF-416	S. pneumoniae	SKAGLYGKIERSDKRE	648
  	C. jeikeium
  PF-417	S. epidermidis	DSYFRS	649
  	C. jeikeium
  	C. jejuni
  PF-418	S. epidermidis	FFLVHFYIRKRKGKVSIFLNYF	650
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-421	C. jeikeium	KHCFEITDKTDVV	651
  PF-422	C. albicans	MSRKKYENDEKSQKKLKIGRKSDVFYG	652
  	MRSA	IID
  	C. jeikeium
  PF-423	S. epidermidis	AGKKERLLSFREQFLNKNKKK	653
  	M. luteus
  	E. coli
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-424	S. epidermidis	IAAFVTSRAFSDTVSPI	654
  	C. albicans
  	MRSA
  PF-425	S. epidermidis	MMELVLKTIIGPIVVGVVLRIVDKWLN	655
  	M. luteus	KDK
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	C. jeikeium
  PF-426	S. epidermidis	MLQKYTQMISVTKCIITKNKKTQENVD	656
  	E. coli	AYN
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-427	M. luteus	YVLEYHGLRATQDVDAFMAL	657
  	P. aeruginosa
  	C. albicans
  	C. jejuni
  PF-428	S. epidermidis	ENEESIF	658
  	C. albicans
  	E. faecalis
  	C. jeikeium
  PF-429	S. epidermidis	AATLICVGSGIMSSL	659
  	S. pneumoniae
  	C. jeikeium
  PF-430	S. epidermidis	AVVCGYLAYTATS	660
  	M. luteus
  	E. coli
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-431	S. epidermidis	VAYAAICWW	661
  	M. luteus
  	E. coli
  	P. aeruginosa
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-432	S. epidermidis	FNGDSEFFLCIAF	662
  	M. luteus
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-433	S. epidermidis	MRKEFHNVLSSGQLLADKRPARDYNR	663
  	E. coli	K
  	S. pneumoniae
  	C. jeikeium
  PF-434	S. epidermidis	GQLLADKRPARDYNRK	664
  	M. luteus
  	S. pneumoniae
  	C. jeikeium
  PF-435	C. jeikeium	MSRWDGHSDKGEAPAGKPPMHGFGLN	665
  		GENK
  PF-436	C. jeikeium	KKHVLVGKQEKNG	666
  PF-438	S. epidermidis	QPYFQNQFKKITGYTPLQYRKEKR	667
  	E. coli
  	S. pneumoniae
  	C. jeikeium
  	C. jejuni
  PF-439	S. epidermidis	RVLVLKKFHGIMDGNRNVAVFFVGQ	668
  	M. luteus
  	B. fragilis
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-440	S. epidermidis	MFIISPDLFNIAVILYILFFIHDILLLILS	669
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-441	C. jeikeium	TQVHKMARGIDPGPANGIYR	670
  PF-442	S. epidermidis	MQIFYIKTKIFLSFFLFLLIFSQCFYKIEE	671
  	E. coli
  	C. albicans
  	S. pneumoniae
  	E. faecalis
  PF-443	S. epidermidis	KLLYFFNYFENLQQVHLLVQL	672
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-444	M. luteus	MAAKLWEEGKMVYASSASMTKRLKL	673
  	C. albicans	AMSKV
  	S. pneumoniae
  	C. jeikeium
  PF-445	M. luteus	ASMTKRLKLAMSKV	674
  	S. pneumoniae
  	C. jeikeium
  PF-446	M. luteus	SGNEKV	675
  	C. jeikeium
  PF-447	S. epidermidis	IDKSRNKDQFSHIFGLYNICSG	676
  	M. luteus
  	E. coli
  	S. pneumoniae
  PF-448	S. epidermidis	SLQSQLGPCLHDQRH	677
  	M. luteus
  	P. mirabilis
  	E. coli
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-450	S. epidermidis	HRNLIILQRTIFI	678
  	M. luteus
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-451	S. epidermidis	MVNYIIGSYMLYREQNNNEALRKFDIT	679
  	M. luteus	LAM
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  	M. smegmatis
  PF-452	M. luteus	MNNWIKVAQISVTVINEVIDIMKEKQN	680
  	P. aeruginosa	GGK
  	C. albicans
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	M. smegmatis
  PF-453	M. luteus	IIQDIAHAFGY	681
  	E. coli
  	P. aeruginosa
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-454	S. epidermidis	MSVFVPVTNIFMFIMSPIFNVNLLHFKV	682
  	M. luteus	YI
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  	M. smegmatis
  PF-456	C. albicans	TCVKPRTIN	683
  	MRSA
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-457	C. albicans	INKYHHIA	684
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-458	S. epidermidis	ISLIIFIMLFVVALFKCITNYKHQS	685
  	M. luteus
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-459	P. aeruginosa	EKRMSFNENQSHRPLL	686
  PF-460	S. epidermidis	MEHVLPFQNTPPNIVIIYKDFTHLKSITF	687
  	M. luteus	S
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  	M. smegmatis
  PF-461	E. coli	MTLAIKNCSVTKCLGFGDFVNDDSDSY	688
  	S. pneumoniae	FDA
  PF-462	E. faecalis	KNKTDTL	689
  	C. jeikeium
  PF-463	S. epidermidis	MVILVFSLIFIFTDNYLVYQSKSIKEDVM	690
  	E. coli	I
  	P. aeruginosa
  	C. albicans
  	S. pneumoniae
  	E. faecalis
  	M. smegmatis
  PF-464	S. epidermidis	VDMVNRFLGN	691
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-465	S. epidermidis	KPVGKALEEIADGKIEPVVPKEYLG	692
  	M. luteus
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-466	MRSA	VRKSDQ	693
  	C. jeikeium
  	C. jejuni
  PF-467	MRSA	YYKDYFKEI	694
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-469	S. epidermidis	YKVNYNNIDNHFNTLRH	695
  	M. luteus
  	P. mirabilis
  	E. coli
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-470	M. luteus	PYSDSYATRPHWEQHRAR	696
  	E. coli
  	MRSA
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-471	S. epidermidis	MVGKIRGVTPRNDLLNANITGQLNLNY	697
  	M. luteus	RLI
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-472	S. epidermidis	MHISHLLDEVEQTEREKAVNVLENMNG	698
  	E. coli	NVI
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-473	S. epidermidis	MAADIISTIGDLVKWIIDTVNKFKK	699
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  PF-474	S. epidermidis	MHRNLVLVKMEPIPHIMIIANQIGIIIEKA	700
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  	M. smegmatis
  PF-475	S. epidermidis	MREKVRFTQAFKLFWTNYFNFKGRSRR	701
  	M. luteus	SEY
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-476	M .luteus	WADAQYKLCENCSE	702
  	P. mirabilis
  	C. albicans
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-477	S. epidermidis	HKNKLNIPHIKS	703
  	M. luteus
  	C. albicans
  	S. pneumoniae
  	C. jeikeium
  	C. jejuni
  PF-478	S. epidermidis	HLFILKSHLKPFPPFRYTYD	704
  	M. luteus
  	P. mirabilis
  	E. coli
  	C. albicans
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF -479	S. epidermidis	AYILKRREEKNK	705
  	M. luteus
  	P. mirabilis
  	E. coli
  	C. albicans
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-480	S. epidermidis	MVEILVNTAISVYIVALYTQWLSTRDNL	706
  	M. luteus	KA
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  	M. smegmatis
  PF-481	C. jeikeium	DELYEIMDKVIEEFNKDIEQNNNNGNN	707
  		EDLTENKIN
  PF-482	S. epidermidis	LVGYVRTSGTVRSYKIN	708
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-483	P. mirabilis	EDNKDKKDKKDK	709
  	C. jeikeium
  	C. jejuni
  PF-484	S. epidermidis	HKKDIRKQVFKN	710
  	M. luteus
  	P. mirabilis
  	E. coli
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-486	S. mutans	MQKEGEEDY	711
  PF-487	S. mutans	MYKAIAVLAMTIMAFFIFVYPFFIVGLIL	712
  	E. coli	G
  PF-488	S. mutans	YPNEQGHHKNNLKNIIIE	713
  	E. coli
  PF-489	S. mutans	KVDRVSTTITEKIK	714
  PF-490	S. mutans	RLILVSGNATVQK	715
  	E. coli
  PF-491	S. mutans	IHQYSSKPDIVGQEAKTVQQINS	716
  	E. coli
  PF-492	S. mutans	IQIDAASFYSISKSTIK	717
  	B. subtilis
  	E. coli
  PF-493	S. mutans	PGAFFFCRGRGCWCGIGW	718
  	B. subtilis
  	E. coli
  PF-494	S. mutans	FTEPLRPLQAKGQIISIKPSTSSS	719
  PF-495	S. mutans	KGIYKKRTY	720
  	E. coli
  PF-496	S. mutans	EVTKRLVALAQQQLRG	721
  	E. coli
  PF-497	S. mutans	LVLRICTDLFTFIKWTIKQRKS	722
  	B. subtilis
  	E. coli
  PF-498	S. mutans	MSEEEEVSEKVYNYLRRNEFFEVRKEE	723
  	E. coli	FSA
  PF-499	S. mutans	VYSFLYVLVIVRKLLSMKKRIERL	724
  	E. coli
  PF-500	S. mutans	MGIFKEEKIKFIDCKGEEVILKIKIKDIKK	725
  	E. coli
  PF-501	S. mutans	GSTAHKSPIGSTNNQWGMKKTPTD	726
  PF-502	S. mutans	NKGKQMQDQTGKQPIVDNG	727
  PF-503	S. mutans	VVTLKDIVAVIEDQGYDVQ	728
  PF-504	S. mutans	ILSVELSTKTSASGS	729
  	E. coli
  PF-505	S. mutans	GYTKDPGTGI	730
  PF-506	S. mutans	SGRGFALIVVLFILLIIVGAACIR	731
  	E. coli
  PF-507	S. mutans	LALSIANLFKKKA	732
  	E. coli
  PF-508	S. mutans	VSTFGKVVKVVDEK	733
  PF-509	S. mutans	EAKVQAKGEQIACNNY	734
  	B. subtilis
  	E. coli
  PF-510	S. mutans	WYLYKKQSNQNDRGIPK	735
  	E. coli
  PF-511	E. coli	VMQSLYVKPPLILVTKLAQQN	736
  	P. aeruginosa
  	S. pneumoniae
  	C. jeikeium
  PF-512	S. pneumoniae	SFMPEIQKNTIPTQMK	737
  	C. jeikeium
  PF-513	C. albicans	SNGVGLGVGIGSGIRF-NH2	738
  PF-514	S. epidermidis	QRFYKLFYHIDLTNEQALKLFQVK	739
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-515	S. epidermidis	DKSTQDKDIKQAKLLAQELGL-NH2	740
  	C. albicans
  	S. pneumoniae
  	C. jeikeium
  PF-517	C. jejuni	VKPTMTASLISTVC	741
  PF-518	S. epidermidis	SFYSKYSRYIDNLAGAIFLFF	742
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  PF-519	M. luteus	YLVYSGVLATAAAF-NH2	743
  	E. faecalis
  	C. jeikeium
  PF-520	S. epidermidis	LGLTAGVAYAAQPTNQPTNQPTNQPTN	744
  	M. luteus	QPTNQPTNQPRW-NH2
  	E. coli
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-521	S. epidermidis	CGKLLEQKNFFLKTR	745
  	E. coli
  	P. aeruginosa
  	S. pneumoniae
  	E. faecalis
  PF-522	S. epidermidis	FELVDWLETNLGKILKSKSA-NH2	746
  	E. coli
  	P. aeruginosa
  	S. pneumoniae
  	E. faecalis
  PF-523	S. epidermidis	ASKQASKQASKQASKQASKQASRSLKN	747
  	M. luteus	HLL
  	C. albicans
  	S. pneumoniae
  	C. jeikeium
  	C. jejuni
  PF-524	S. epidermidis	PDAPRTCYHKPILAALSRIVVTDR	748
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-526	S. epidermidis	VLLLFIFQPFQKQLL-NH2	749
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-527	S. epidermidis	GSVIKKRRKRMAKKKHRKLLKKTRIQR	750
  	M. luteus	RRAGK
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-528	S. epidermidis	LVDVVVLIRRHLPKSCS-NH2	751
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  PF-529	S. epidermidis	LSEMERRRLRKRA-NH2	752
  	E. coli
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-537	S. epidermidis	LANDYYKKTKKSW	753
  	M. luteus
  	P. mirabilis
  	E. coli
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-539	S. epidermidis	SIILTKKKRRKIPLSIDSQIYKYTFKQ	754
  	M. luteus
  	B. subtilis
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-540	C. albicans	KSILILIKVIFIGQTTIIL	755
  PF-542	C. jeikeium	KKDNPSLNDQDKNAVLNLLALAK	756
  PF-543	S. epidermidis	NILFGIIGFVVAMTAAVIVTAISIAK	757
  	M. luteus
  	B. subtilis
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-544	S. epidermidis	FGEKQMRSWWKVHWFHP	758
  	M. luteus
  	P. mirabilis
  	P. aeruginosa
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-545	S. epidermidis	RESKLIAMADMIRRRI-NH2	759
  	E. coli
  	P. aeruginosa
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-546	S. epidermidis	PIIAPTIKTQIQ	760
  	E. coli
  	C. albicans
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-547	S. epidermidis	WSRVPGHSDTGWKVWHRW-NH2	761
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  PF-548	M. luteus	ARPIADLIHFNSTTVTASGDVYYGPG	762
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-549	E. coli	TGIGPIARPIEHGLDS	763
  	C. albicans
  	S. pneumoniae
  	C. jeikeium
  PF-550	S. pneumoniae	STENGWQEFESYADVGVDPRRYVPL	764
  PF-551	S. pneumoniae	QVKEKRREIELQFRDAEKKLEASVQAE	765
  PF-552	S. pneumoniae	ELDKADAALGPAKNLAPLDVINRS	766
  PF-553	S. epidermidis	LTIVGNALQQKNQKLLLNQKKITSLG	767
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	C. jeikeium
  PF-554	S. pneumoniae	AKNFLTRTAEEIGEQAVREGNINGP	768
  PF-555	MRSA	EAYMRFLDREMEGLTAAYNVKLFTEAI	769
  	S. pneumoniae	S
  	C. jeikeium
  PF-556	S. epidermidis	SLQIRMNTLTAAKASIEAA	770
  	M. luteus
  	B. fragilis
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  PF-557	S. pneumoniae	AANKAREQAAAEAKRKAEEQAR	771
  PF-558	S. epidermidis	ADAPPPLIVRYS	772
  	E. coli
  	C. albicans
  	C. jeikeium
  	C. jejuni
  PF-559	S. epidermidis	SRPGKPGGVSIDVSRDRQDILSNYP	773
  	M. luteus
  	C. albicans
  	C. jeikeium
  	C. jejuni
  PF-560	S. epidermidis	FGNPFRGFTLAMEADFKKRK	774
  	M. luteus
  	E. coli
  	S. pneumoniae
  	C. jeikeium
  	C. jejuni
  PF-562	S. epidermidis	TPEQWLERSTVVVTGLLNRK	775
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-563	S. epidermidis	RPELDNELDVVQNSASLDKLQASYN	776
  	M. luteus
  	C. jeikeium
  PF-564	S. epidermidis	TIILNDQINSLQERLNKLNAETDRR	777
  	C. albicans
  	S. pneumoniae
  	C. jeikeium
  PF-566	P. mirabilis	EAQQVTQQLGADFNAITTPTATKV	778
  	S. pneumoniae
  PF-567	S. epidermidis	QQRVKAVDASLSQVSTQVSGAVASA	779
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	C. jeikeium
  PF-568	S. epidermidis	TQAVQVKTAQAQQQ	780
  PF-569	M. luteus	KSKISEYTEKEFLEFVEDIYTNNK	781
  	P. mirabilis
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-570	S. pneumoniae	KKFPTEESHIQAVLEFKKLTEHPSG	782
  	C. jeikeium
  PF-572	S. epidermidis	WRASKGLPGFKAG	783
  	M. luteus
  	E. coli
  	S. pneumoniae
  	C. jeikeium
  PF-573	S. epidermidis	EKKLIVKLIDSIGKSHEEIVGAG	784
  	S. pneumoniae
  PF-575	M. luteus	LNFRAENKILEKIHISLIDTVEGSA	785
  	E. coli
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-576	M. luteus	AYSGELPEPLVRKMSKEQVRSVMGK	786
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	S. pneumoniae
  PF-577	S. epidermidis	PFETRESFRVPVIGILGGWDYFMHP	787
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. .faecalis
  PF-578	S. epidermidis	QKANLRIGFTYTSDSNVCNLTFALLGSK	788
  	M. luteus
  	P. mirabilis
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-579	S. epidermidis	MILVCAAVIWGRVLFILKFPIYFSIRLAF	789
  	M. luteus	L
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-580	S. epidermidis	EILNNNQVIKELTMKYKTQFESNLGGW	790
  	M. luteus	TARARR
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-581	S. epidermidis	WTARARR	791
  	M. luteus
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-583	S. epidermidis	KFQGEFTNIGQSYIVSASHMSTSLNTGK	792
  	M. luteus
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-584	S. epidermidis	SYIKNLSNQKFLIAF	793
  	M. luteus
  	P. mirabilis
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-585	S. epidermidis	DYNHLLNVVQDWVNTN	794
  	E. coli
  	C. albicans
  	MRSA
  	S. pneumoniae
  	C. jeikeium
  PF-586	S. epidermidis	FFNQANYFFKEF	795
  	M. luteus
  	E. coli
  	P. aeruginosa
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-587	S. epidermidis	ASGKYQSYLLNVYVDSKKDRLDIFDKL	796
  	M. luteus	KAKAKFVL
  	E. coli
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-588	S. epidermidis	ESVEAIKAKAIK	797
  	E. coli
  	C. albicans
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-589	S. epidermidis	APLRIDEIRNSNVIDEVLDCAPKKQEHFF	798
  	C. albicans	VVPKIIE
  	MRSA
  	S. pneumoniae
  PF-590	S. epidermidis	YYQAKLFPLL	799
  	M. luteus
  	E. coli
  	E. faecalis
  	C. jeikeium
  PF-592	S. epidermidis	IMKNYKYFKLFIVKYALF	800
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-593	C. jeikeium	MEISTLKKEKLHVKDELSQYLANYKK	801
  PF-594	C. jeikeium	IVSAIV	802
  PF-595	S. epidermidis	LQNKIYELLYIKERSKLCS	803
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-596	S. epidermidis	SKMWDKILTILILILELIRELIKL	804
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	MRSA
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-597	P. mirabilis	DEIKVSDEEIEKFIKENNL	805
  PF-598	S. epidermidis	MKFMLEVRNKAISAYKEITRTQI	806
  	M. luteus
  	P. mirabilis
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	C. jeikeium
  PF-599	S. epidermidis	LFEIFKPKH	807
  	P. mirabilis
  	E. coli
  	C. albicans
  	MRSA
  	S. pneumoniae
  	C. jeikeium
  PF-600	S. epidermidis	TKKIELKRFVDAFVKKSYENYILERELK	808
  	M. luteus	KLIKAINEELPTK
  	B. subtilis
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-601	C. jeikeium	YRVTVKALE	809
  PF-602	P. mirabilis	LEKEKKEYIEKLFKTK	810
  	C. jeikeium
  PF-603	S. epidermidis	IDKLKKMNLQKLSYEVRISQDGKSIYAR	811
  	M. luteus	IK
  	B. subtilis
  	E. coli
  	P. aeruginosa
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-604	S. epidermidis	LMEQVEV	812
  	C. albicans
  	C. jeikeium
  PF-605	S. epidermidis	HYRWNTQWWKY	813
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-607	S. epidermidis	YIESDPRKFDYIFGAIRDH	814
  	P. mirabilis
  	E. coli
  	MRSA
  	S. pneumoniae
  	C. jeikeium
  PF-609	P. mirabilis	TEIKLDNNEYLVLNLDDILGILK	815
  	E. coli
  	S. pneumoniae
  PF-610	S. epidermidis	VFLKLKTSKIDLASIIFYP	816
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-612	S. epidermidis	GTTLKYGLERQLKIDIHPEITIINLNGGA	817
  	M. luteus	DEFAKL
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-613	C. jeikeium	ADEFAKL	818
  PF-614	S. epidermidis	GLDIYA	819
  	E. coli
  	C. jeikeium
  PF-615	S. epidermidis	FLNRFIFYIFTVKTKSALIKNLFLD	820
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	C. jeikeium
  	C. jejuni
  PF-616	C. jeikeium	IVFVVTKEKK	821
  PF-617	P. aeruginosa	PMNAAEPE	822
  	C. albicans
  PF-619	S. epidermidis	WSRVPGHSDTGWKVWHRW	823
  	M. luteus
  	B. subtilis
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-621	S. epidermidis	PPSSFLV	824
  	C. albicans
  PF-622	S. epidermidis	TREDVFSVRLINNIVNKQA	825
  	P. aeruginosa
  	C. albicans
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-623	S. epidermidis	VLFAVYLGALDWLFSWLTQKM	826
  	P. aeruginosa
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-625	S. epidermidis	SDSTNNARTRKKARDVTTKDIDK	827
  	M. luteus
  	S. pneumoniae
  	C. jeikeium
  PF-626	S. epidermidis	KYDFDDFEPEEA	828
  	M. luteus
  	E. coli
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-627	S. epidermidis	INDLLSYFTLHEK	829
  	P. aeruginosa
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-629	S. epidermidis	GLAAIATVFALY	830
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-630	S. epidermidis	IPATPIIHS	831
  	M. luteus
  	P. mirabilis
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-631	S. epidermidis	LIIYFSKTGNTARATRQI	832
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-632	S. epidermidis	TTIQGVASLEKHGFRYTIIYPTRI	833
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-634	S. epidermidis	MPKARPVNHNKKKSKITIKSNFTLFYM	834
  	M. luteus	FNP
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-635	S. epidermidis	MNAHGHSLIFQKMIVHAFAFFSKQKNY	835
  	P. aeruginosa	LYF
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-636	S. epidermidis	LVRLA	836
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  PF-637	S. epidermidis	SRIKQDARSVRKYDRIGIFFYSFKSA	837
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-638	S. epidermidis	TFILPK	838
  	C. albicans
  	MRSA
  	C. jeikeium
  PF-639	S. pneumoniae	QATQIKSWIDRLLVSED	839
  	C. jeikeium
  PF-640	C. albicans	MGDINRNF	840
  PF-641	S. epidermidis	SWKCHHLAIGGSWKCHHLAI	841
  	M. luteus
  	E. coli
  	C. albicans
  	MRSA
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-642	M. luteus	FTTPMIGIPAGLLGGSYYLKRREEKGK	842
  	MRSA
  	C. jeikeium
  PF-643	Mycobacteria spp	VRCRL	843
  PF-644	Mycobacteria spp	TSGLIIGENGLNGL	844
  PF-645	Mycobacteria spp	SNSVQQG	845
  PF-646	Mycobacteria spp	APASPGRRPG	846
  PF-647	Mycobacteria spp	GTFLGQKCAAATAS	847
  PF-648	S. mutans	ARRYPAAGS	848
  	E. coli
  PF-649	Mycobacteria spp	CPRYPFVDVGPAGPWRARWRVGS	849
  PF-650	Mycobacteria spp	IRSDQPGRQSRSSPRWPTGAGRHR	850
  PF-651	Mycobacteria spp	PRWPTGAGRHR	851
  PF-652	Mycobacteria spp	FLAPARPDLQAQRQALAQ	852
  PF-653	Mycobacteria spp	QSVHPLPAETPVADVI	853
  PF-654	Mycobacteria spp	LSGRLAGRR	854
  PF-655	M. smegmatis	DAPCFDDQFGDLKCQMC	855
  PF-656	Mycobacteria spp	RGMFVPFHDVDCVQ	856
  PF-657	Mycobacteria spp	YVANYTITQFGRDFDDRLAVAIHFA	857
  PF-658	Mycobacteria spp	PTTPPPTTPPEIPTGGTVIST	858
  PF-659	Mycobacteria spp	TVIST	859
  PF-660	Mycobacteria spp	TDPQATAAPRRRTSPR	860
  PF-661	Mycobacteria spp	PDEDIRRRAILPPAGPCRPMSPE	861
  PF-662	Mycobacteria spp	GKQSRAHGPVASRREFRRKSG	862
  PF-663	Mycobacteria spp	ATLIPRKA	863
  PF-664	M. smegmatis	DQLCVEYPARVSTG	864
  PF-665	Mycobacteria spp	VLRVATAVGEVPTGL	865
  PF-666	Mycobacteria spp	PNRRSRPR	866
  PF-667	Mycobacteria spp	PAHQRLRIDQRLVADRDMVQDYES	867
  PF-668	Mycobacteria spp	TNAESMALAFRGRVHMSVNIAGLT	868
  PF-669	Mycobacteria spp	RADRIESYPADGDRVITLWRNPYR	869
  PF670	Mycobacteria spp	TVIVAPMHSGV	870
  PF-671	S. mutans	TVSAFRTVH	871
  	E. coli
  PF-673	S. mutans	VRRLRM	872
  	E. coli
  PF-674	S. mutans	DGCDSEPALTYR	873
  	E. coli
  PF-675	Mycobacteria spp	EIIPISPTRRCEMHTMSSAEYRGL	874
  PF-676	S. mutans	AEYRGL	875
  	E. coli
  PF-677	Mycobacteria spp	TCRGAGMH	876
  PF-678	Mycobacteria spp	RDRRWTRRDMYDWLESARV	877
  PF-679	S. mutans	CRARFIRR	878
  	E. coli
  PF-680	Mycobacteria spp	ADPHPTTGI	879
  PF-681	M. smegmatis	TALTTVGVSGARLITYCVGVEDI	880
  PF-682	Mycobacteria spp	RRGKSEQGLSRR	881
  PF-683	Mycobacteria spp	LWPVA	882
  PF-684	Mycobacteria spp	RKLSLASGFALWRRSLV	883
  PF-685	Mycobacteria spp	PTLWLACL	884
  PF-686	M. smegmatis	LAVLMGYIGYRGWSGKRHINRQ	885
  PF-687	Mycobacteria spp	AKRVLSLAVAPHRRQPVQGT	886
  PF-688	Mycobacteria spp	ARNHAVIPAG	887
  PF-689	S. mutans	SAPSG	888
  	E. coli
  PF-690	Mycobacteria spp	MIPLAGDPVSSHRTVEFGVLGTYLVSG	889
  		GSL
  PF-691	Mycobacteria spp	HRTVEFGVLGTYLVSGGSL	890
  PF-692	Mycobacteria spp	GVAREDPLEPDPLAPIIDDSR	891
  PF-693	Mycobacteria spp	PDPAR	892
  PF-694	Mycobacteria spp	DLIRPLYSMSAPSVA	893
  PF-695	Mycobacteria spp	ALSVMLGNIPLVVPNANQL	894
  PF-696	Mycobacteria spp	IRSGISAAYARPLR	895
  PF-697	Mycobacteria spp	RADARAK	896
  PF-698	Mycobacteria spp	SSGRAGVKCRRPTGR	897
  PF-699	Mycobacteria spp	GRAGVKCRRPTGR	898
  PF-700	Mycobacteria spp	LNWPFTGR	899
  PF-701	S. mutans	PRGAQSGHG	900
  PF-702	Mycobacteria spp	LSGRLAGRR	901
  PF-703	Mycobacteria spp	MTTVDNIVGLVIAVALMAFLFAALLFPE	902
  		KF
  PF-704	Mycobacteria spp	APAARAAL	903
  PF-705	S. mutans	GEEEGTVAD	904
  	E. coli
  PF-706	L. pneumophila	LGYGAWIGCGLGLNGFHRID	905
  PF-707	S. mutans	IDPESIVTTNNKQDNVDEQ	906
  	E. coli
  PF-709	S. mutans	NKKHSPMD	907
  PF-711	S. mutans	KTAGPTGTIYKTN	908
  PF-712	S. mutans	QIYRHVHKVQAKSANLRLY	909
  	E. coli
  PF-714	L. pneumophila	FVVTQRMLRMYKK	910
  PF-716	S. mutans	HGENHEIFIKSDEKDNDSSEKKD	911
  PF-717	E. coli	PQSEVTFENIYAPKANGGGLYGI	912
  PF-720	S. mutans	SLDMGK	913
  PF-724	L. pneumophila	CYRFLTPKRPTRIS	914
  PF-727	S. mutans	AYARCRHDYPFTLGQMQTH	915
  	E. coli
  PF-728	S. mutans	AIGQEQDRREYYYYSGYPYYY	916
  	E. coli
  PF-731	L. pneumophila	RHKLIRLPLSESVFCFLNNPKI	917
  PF-732	E. coli	DRPSQTTHHTLSSSRITGPS	918
  PF-733	S. mutans	VISRQMGSEAVLELFIIM	919
  	E. coli
  PF-735	S. mutans	YDPLFPNDKN	920
  	E. coli
  PF-737	S. epidermidis	KSSGSSASASSTAGGSSSK	921
  	S. pneumoniae
  PF-738	S. epidermidis	KSGATSAASGAKSGASS	922
  	C. albicans
  	C. jeikeium
  PF-741	S. epidermidis	AKREDTVAAQIGANILNLIQ	923
  	M. luteus
  	P. mirabilis
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. .faecalis
  PF-744	S. epidermidis	LGVGTFVGKVLIKNQQKQKSKKKAQ	924
  	M. luteus
  	E. coli
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-745	S. epidermidis	ANSQNSLFSNRSSFKSIFDKKSNITTNAT	925
  	M. luteus	TPNSNIIIN
  	C. albicans
  PF-746	S. epidermidis	FLGNSQYFTRK	926
  	M. luteus
  	E. coli
  	C. albicans
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-748	S. epidermidis	FQGFFDVAVNKWWEEHNKAKLWKNV	927
  	M. luteus	KGKFLEGEGEEEDDE
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-749	S. epidermidis	GVNKWWEEHNKAKLWKNVKGKFLEG	928
  	M. luteus	EGEEEDDE
  	E. coli
  	P. aeruginosa
  	C. albicans
  	S. pneumoniae
  	C. jeikeium
  PF-750	M. luteus	AESSPAKTTA	929
  	C. jeikeium
  PF-751	S. epidermidis	AESSPAQETT	930
  	E. coli
  	C. albicans
  	C. jeikeium
  PF-752	S. epidermidis	LHVIRPRPELSELKFPITKILKVNKQGLK	931
  	E. coli	K
  	MRSA
  	S. pneumoniae
  	E. faecalis
  PF-756	S. epidermidis	DALLRLA	932
  	M. luteus
  	C. albicans
  	MRSA
  	C. jeikeium
  PF-757	M. luteus	PQAISSVQQNA	933
  	C. albicans
  	MRSA
  PF-758	S. epidermidis	PEIIKIVSGLL	934
  	M. luteus
  	E. coli
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-760	S. epidermidis	DHITLDDYEIHDGFNFELYYG	935
  	M. luteus
  PF-761	S. epidermidis	SKFELVNYASGCSCGADCKCASETECK	936
  	M. luteus	CASKK
  	P. mirabilis
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  PF-762	M. luteus	PAPAPSAPAPAPEQPEQPA	937
  	C. albicans
  PF-763	S. epidermidis	GIWMARNYFHRSSIRKVYVESDKEYER	938
  	M. luteus	VHPMQKIQYEGNYKSQ
  	E. coli
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  PF-764	S. epidermidis	GYFEPGKRD	939
  	M. luteus
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-765	S. epidermidis	YLYWEVEHKPIIAKRDAYYAQLRKQKE	940
  	M. luteus	IEEGA
  	E. coli
  	MRSA
  	E. faecalis
  	C. jeikeium
  PF-766	S. epidermidis	DAYYAQLRKQKEIEEGA	941
  	M. luteus
  	C. albicans
  	MRSA
  	E. faecalis
  	C. jeikeium
  PF-767	S. epidermidis	DGKQGEPVALKPTDN	942
  	M. luteus
  	E. coli
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-768	S. epidermidis	GFRGGKRGGARG	943
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-770	S. epidermidis	GVGIGFIMMGVVGYAVKLVHIPIRYLIV	944
  	M. luteus
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  PF-772	S. epidermidis	TKESSS	945
  	C. albicans
  	MRSA
  	S. pneumoniae
  	C. jeikeium
  PF-773	S. epidermidis	TLKESK	946
  	C. albicans
  	C. jeikeium
  PF-776	S. epidermidis	VSILLYLSATIMPNVLRLLVARAIIVRV	947
  	M. luteus
  	P. mirabilis
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  PF-777	Mycobacteria spp.	PGADGKLAEASAAIARLVRS	948
  PF-778	Mycobacteria spp.	MNLILTAHGT	949
  PF-779	Mycobacteria spp.	IYGDFFNFYLCDISLKVNGLQPGGPVRT	950
  		VKLFGQPTGRCTPQ
  PF-780	Mycobacteria spp.	AVYDALVALAAAEHRAELATRDARAK	951
  		DTYEKIGVHVVVAA
  PF-781	Mycobacteria spp.	PLVVVNHRRAERSRG	952
  PF-782	Mycobacteria spp.	TGPRRGIDLTSNRALSEVLDEGLELNSR	953
  		K
  PF-783	Mycobacteria spp.	FTSEVRGVFTYRVNKAGLITNMRGYW	954
  		NLDMMTFGNQE
  PF-784	Mycobacteria spp.	MAMTTVDNIVGLVIAVALMAFLFAALL	955
  		FPEKF
  PF-785	Mycobacteria spp.	MRPQHSPAGKAFVVKKITHEQS	956
  PF-786	Mycobacteria spp.	LSERERRRLKRGII	957
  PF-787	Mycobacteria spp.	MTERQRRALLKQHPEVVSWSDYLEKR	958
  		KRRTGTAG
  PF-788	Mycobacteria spp.	GLITVFAGTARILQLRRAAKKTHAAAL	959
  		R
  PF-789	Mycobacteria spp.	PRGAQSGHG	960
  PF-790	Mycobacteria spp.	PAGPDHLDQRDHR	961
  PF-791	S. mutans	IFLTTQNTDYSEHNAA	962
  PF-792	S. mutans	ALHASGIQAI	963
  PF-793	S. mutans	YTQUNNASAYAMLLTNKDTVP	964
  PF-794	S. mutans	NLYFENQGN	965
  PF-795	S. mutans	ALHKSGIQVIADWVPDQIYN	966
  PF-796	S. mutans	YTQSNIPTAYALMLSNKDSI	967
  PF-797	S. mutans	WYYFDNNGYM	968
  PF-798	S. mutans	ALHSKGIKVMADWVPDQMYA	969
  PF-799	S. mutans	YTHYNTALSYALLLTNKSSVP	970
  PF-800	S. mutans	WYYFDNNGYM	971
  PF-0003	A. naeslundii	FCSVDHDVITIAADHVKQGAEA	972
  	P. gingivalis
  	S. mutans
  PF-0008	A. naeslundii	AQPRRTWLVNFGEVPSPGLTNDGMPDH	973
  PF-0034	S. mutans	HPMPITVRSRKPGPLTAPSEH	974
  	E. coli
  PF-0045	A. naeslundii	FREGMGWPLSNEGSPTAPLPKHRNQV	975
  	T. denticola
  PF-0050	A. naeslundii	QGLARPVLRRIPL	976
  	S. mutans
  PF-0052	A. naeslundii	SRFRNGV	977
  	F. nucleatum
  	S. mutans
  PF-0055	A. naeslundii	YNLSIYIYFLHTITIAGLITLPFII	978
  	F. nucleatum
  	P. gingivalis
  	S. mutans
  PF-0057	A. naeslundii	YFWWYWVQDCIPYKNNEVWLELSNN	979
  	F. nucleatum	MK
  	P. gingivalis
  	S. mutans
  PF-0058	A. naeslundii	FETGFGDGYYMSLWGLNEKDEVCKVV	980
  	F. nucleatum	IPFINPELID
  	P. gingivalis
  	S. mutans
  PF-0061	A. naeslundii	TLNYKKMFFSVIFLLGLNYLICNSPLFFK	981
  	F. nucleatum	QIEF
  	P. gingivalis
  	S. mutans
  	T. denticola
  PF-0062	A. naeslundii	PLARATEVVATLFIICSLLLYLTR	982
  	F. nucleatum
  	P. gingivalis
  	S. mutans
  	T. denticola
  PF-0063	A. naeslundii	SHFRKGD	983
  	F. nucleatum
  	S. mutans
  PF-0064	A. naeslundii	DEEALEMGANLYAQFAIDFLNSKK	984
  	F. nucleatum
  	P. gingivalis
  	S. mutans
  	T. denticola
  PF-0065	A. naeslundii	DEERYSDSYFLKEKVFYLILALFLILFHQ	985
  	F. nucleatum	KYLYFLEIITI
  	P. gingivalis
  	S. mutans
  PF-0068	A. naeslundii	LNLFASI	986
  	F. nucleatum
  	S. mutans
  PF-0069	A. naeslundii	NALMLREMQLAKNIKVEVTDVLSNKK	987
  	F. nucleatum	YC
  	P. gingivalis
  	S. mutans
  	T. denticola
  PF-0071	A. naeslundii	QVIVKIL	988
  	F. nucleatum
  	S. mutans
  PF-0072	A. naeslundii	KKMFSLIRKVNWIFFILFIVLDLTNVFPLI	989
  	F. nucleatum	RTILFAILSRQ
  	P. gingivalis
  	S. mutans
  	T. denticola
  PF-0075	A. naeslundii	KALVISVFAIVFSIIFVKFFYWRDKK	990
  	F. nucleatum
  	P. gingivalis
  	S. mutans
  	T. denticola
  PF-0080	A. naeslundii	INIPGLF	991
  	F. nucleatum
  	S. mutans
  PF-0084	A. naeslundii	FFSVIFLFGLNYLICNSPLFNILR	992
  	F. nucleatum
  	P. gingivalis
  	S. mutans
  PF-0085	A. naeslundii	KKFKIFVIINWFYHKYIILNFEENF	993
  	F. nucleatum
  	P. gingivalis
  	S. mutans
  	T. denticola
  PF-0086	A. naeslundii	ELFFTILSDCNELFLLHLLQQPLFYIKKG	994
  	F. nucleatum	K
  	P. gingivalis
  	S. mutans
  	T. denticola
  PF-0088	A. naeslundii	DIANNILNSVSERLIIA	995
  	F. nucleatum
  	P. gingivalis
  	S. mutans
  	T. denticola
  PF-0091	A. naeslundii	ASNTPRFVRLTLFNFYSKIWNVTHLFLF	996
  	F. nucleatum	NNL
  	P. gingivalis
  	S. mutans
  	T. denticola
  PF-0093	A. naeslundii	EKLGTMV	997
  	F. nucleatum
  	S. mutans
  PF-0095	A. naeslundii	LLALNIVINEDTYYFELFFIFDNQNKKWL	998
  	F. nucleatum	IFDLKERG
  	P. gingivalis
  	S. mutans
  PF-0098	A. naeslundii	PETKGKVSAFVFGIVVANVIAVVYILYM	999
  	F. nucleatum	LREIGIIQ
  	P. gingivalis
  	S. mutans
  	T. denticola
  PF-C120	A. naeslundii	ASLSTMTFKVMELKELIILLCGLTMLMI	1000
  	F. nucleatum	QTEFV
  	P. gingivalis
  	S. mutans
  	T. denticola
  PF-C131	A. naeslundii	QWIVAKREIRMHIYCHISVIHVIIFFG	1001
  	F. nucleatum
  	P. gingivalis
  	S. mutans
  PF-C134	A. naeslundii	NELMKYPATLTATATTPGIKYSHLCSVC	1002
  	F. nucleatum	L
  	P. gingivalis
  	S. mutans
  	T. denticola
  PF-C135	A. naeslundii	KNTHAYLRVLRLSSLILSYQASVYPLFA	1003
  	F. nucleatum	YLCQQKDY
  	P. gingivalis
  	S. mutans
  PF-C136	A. naeslundii	LILSYQASVYPLFAYLCQQKDY	1004
  	F. nucleatum
  	P. gingivalis
  	S. mutans
  	T. denticola
  PF-C137	A. naeslundii	QRMYWFKRGFETGDFSAGDTFAELK	1005
  	F. nucleatum
  	P. gingivalis
  	S. mutans
  PF-C139	A. naeslundii	LLASHPERLSLGVFFVYRVLHLLLENT	1006
  	F. nucleatum
  	P. gingivalis
  	S. mutans
  	T. denticola
  PF-C142	A. naeslundii	DFPPLSFFRRRFHAYTAPIDNFFGANPF	1007
  	F. nucleatum
  	P. gingivalis
  	S. mutans
  	T. denticola
  PF-C143	A. naeslundii	VVFGGGDRLV	1008
  	F. nucleatum
  	P. gingivalis
  	S. mutans
  	T. denticola
  PF-C145	A. naeslundii	YGKESDP	1009
  	F. nucleatum
  	P. gingivalis
  	S. mutans
  	T. denticola
  PF-C160	F. nucleatum	AASGFTYCASNGVWHPY	1010
  PF-C180	F. nucleatum	TVEELDKAFTWGAAAALAIGVIAINVG	1011
  	P. gingivalis	LAAGYCYNNNDVF
  	S. mutans
  	T. denticola
  PF-C181	P. gingivalis	KMRAGQVVFIYKLILVLLFYVLQKLFD	1012
  		LKKGCF
  PF-C194	A. naeslundii	NTNDLLQAFELMGLGMAGVFIVLGILYI	1013
  	F. nucleatum	VAELLIKIFPVNN
  	P. gingivalis
  	S. mutans
  	T. denticola
  PF-C259	F. nucleatum	AEIQPHCLSVL	1014
  	S. mutans
  PF-C271	A. naeslundii	FFPSYYSIIITYF	1015
  	F. nucleatum
  	P. gingivalis
  	S. mutans
  	T. denticola
  PF-C273	A. naeslundii	KNMLKRRMKQKRLFDEEDRLRVLSKY	1016
  	P. gingivalis	TKSYY
  	S. mutans
  	T. denticola
  PF-C281	A. naeslundii	KKEKLLTAIRLQHRAEIRGYFTIFFLFFRI	1017
  	F. nucleatum
  	P. gingivalis
  	S. mutans
  	T. denticola
  PF-C285	A. naeslundii	FTIIELKKQKIKHGENNKKTAHPLNEPF	1018
  	F. nucleatum	CARA
  	P. gingivalis
  	S. mutans
  	T. denticola
  PF-C290	A. naeslundii	GNVHPESDFHNLIQFIKTFLYFTIFFKYF	1019
  	F. nucleatum	L
  	P. gingivalis
  	S. mutans
  	T. denticola
  PF-C291	A. naeslundii	HPFLTGTGCPLFLIFRLFFVKAYFSFTVF	1020
  	F. nucleatum
  	P. gingivalis
  	S. mutans
  PF-S003	S. epidermidis	ALALLKQDLLNFEGRGRIITSTYLQFNE	1021
  	M. luteus	GCVP
  	P. mirabilis
  	E. coli
  	P. aeruginosa
  	C. albicans
  	MRSA
  	S. pneumoniae
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  	M. smegmatis
  PF-S004	S. epidermidis	VLLNIFRTLLEFFSPSNAPGAEDVPLPDT	1022
  	MRSA	QA
  	C. jeikeium
  PF-S007	S. epidermidis	VVAGVVLLTALAVGSKRKEKKQIKEIQ	1023
  	MRSA	RLLAATR
  PF-S015	S. epidermidis	IENLERGARRPP	1024
  	MRSA
  	C. jeikeium
  PF-S018	S. epidermidis	GMPQIPRLRI	1025
  	M. luteus
  	C. albicans
  	MRSA
  	E. faecalis
  	C. jeikeium
  	C. jejuni
  PF-S023	S. epidermidis	MAEDERRALKRRTNRGRTRTRKRITV	1026
  	MRSA
  PF-S026	S. epidermidis	TELKYNGEEYLLLTQRDILAVIEK	1027
  	MRSA
  	C. jeikeium
  PF-S029	M. luteus	TSDTQSQSPWLFDNADIVNIYPVQLMHS	1028
  	P. mirabilis	SDND
  	E. coli
  	C. albicans
  	C. jeikeium
  	C. jejuni
  *Peptide binding was conducted in aqueous buffers that varied depending on peptidesolubility. For example: Brain Heart Infusion (BHI) Media; 1X Phosphate-buffered saline(PBS); 0.05% v/v Tween-20; 0.05% v/v Tween-80; 1% v/v Glycerol; 50 μM Guanidine hydrochloride; 0.05% v/v Acetic acid; 50 Urea; 1% v/v Polyethylene glycol 400 (PEG 400); 20 mM Sodium glutamate; 50 μM Piperazine-1,4-bis(2-ethanesulfonic acid) (PIPES); 50 mM Sodium acetate; 1% v/v Pluronic 17R4; 1% w/v Pluronic F108; 1% w/v Pluronic P123; 0.2% v/v Cetyl trimethylammonium bromide (CTAB); 0.8% v/v β-D-Octyl glucoside (BOG); 0.2% CTAB and 0.05% Tween-20; 0.2% CTAB and 0.05% Tween-80; 0.2% CTAB and 1% glycerol; and 20 mM HEPES (4-(2-hydroxyethyl)-1- piperazineethanesulfonic acid), 150 mM sodium chloride, 1mM magnesium chloride and 0.1% CTAB. Preferably, binding was evaluated in lx PBS.
  **Three-amino acid code: Dab: Diaminobutyric acid; Orn: Ornithine; cDOrn, cOrn: side- chain cyclical Ornithine; Abreviations: c(X...Y) indicates amino acids are cyclic, connected X to Y; DX indicates D-isoform amino acids.

• In certain embodiments, the amino acid sequence of the targeting peptides comprises or consists of a single amino acid sequence, e.g., as listed above in Table 3. In certain embodiments the amino acid sequence of the targeting peptides comprises two copies, three copies, four copies, five copies six copies or more of one or more of the amino acid sequences listed in Table 3, and/or Table 10, and/or Table 12. Thus, compound targeting constructs are contemplated where the construct comprises multiple domains each having targeting activity. The targeting domains comprising such a construct can be the same or different. In certain embodiments the construct comprises at least 2, at least 3, at least 4, at least 5, at least 6, at least 7, or at least 8 different targeting domains each domain comprising a different targeting sequence.
• Various targeting domains comprising such a construct can be joined directly to each other or two or more of such domains can be attached to each other via a linker. An illustrative, but non-limiting, list of suitable linkers is provided in Table 16. Thus, in certain embodiments, two or more targeting domains comprising a compound/multiple targeting construct are chemically conjugated together.
• In certain embodiments the two or more targeting domains comprising the construct are joined by a peptide linker. Where all the targeting domains are attached directly to each other or are joined by peptide linkers, the entire construct can be provided as a single-chain peptide (fusion protein).
• In various embodiments, the targeting peptides described herein comprise one or more of the amino acid sequences shown in Table 3, and/or Table 10, and/or Table 12 (and/or the retro, inverso, retroinverso, etc. forms of such sequences). In certain embodiments the peptides range in length up to about 100 amino acids in length, preferably up to about 80, about 70, about 60, or about 51 amino acids in length. In certain embodiments the peptides range in length from about 8 amino acids up to about 100 amino acids 80 amino acids, 60 amino acids or about 51 amino acids in length. In certain embodiments the peptides range in length from about 8 up to about 50, 40, 30, 20, 15, 15, 13, or 12 amino acids in length.
• As shown in Tables 3, 10, and 12 the various amino acid sequences described herein target particular microorganisms. The range of activity of the peptides or compositions comprising such peptides can be increased by including amino acid sequences that target different microorganisms either as separate components and/or as multiple domains within a single construct.
• In some embodiments greater specificity and/or avidity can be obtained by including multiple different amino acid sequences that target the same microorganism.
II. Antimicrobial Peptides.
• A) Uses of Antimicrobial Peptides.
• The antimicrobial peptides described herein also have a wide variety of uses. For example, the peptides can be formulated individually, in combination, in combination with other antimicrobial peptides, and/or in combination with various antibacterial agents to provide antimicrobial pharmaceuticals.
• In various embodiments, the antimicrobial peptides described herein can be formulated individually, in combination, in combination with other antimicrobial peptides, and/or in combination with various antibiotic (e.g., antibacterial) agents in “home healthcare” formulations. Such formulations include, but are not limited to toothpaste, mouthwash, tooth whitening strips or solutions, contact lens storage, wetting, or cleaning solutions, dental floss, toothpicks, toothbrush bristles, oral sprays, oral lozenges, nasal sprays, aerosolizers for oral and/or nasal application, wound dressings (e.g., bandages), and the like.
• In various embodiments the antimicrobial peptides described herein can be formulated individually, in combination, in combination with other antimicrobial peptides, and/or in combination with various antibiotic (e.g., antibacterial) agents in various cleaning and/or sterilization formulations for use in agriculture, in fool preparation and transport, in the home, workplace, clinic, or hospital.
• In certain embodiments the antimicrobial peptides described herein are attached to one or more targeting moieties to specifically and/or to preferentially deliver the peptide(s) to a target (e.g. a target microorganism, biofilm, bacterial film, particular tissue, etc.).
• Other possible uses of the targeting and/or antimicrobial peptides disclosed herein include, but are not limited to biofilm dispersal, biofilm retention, biofilm formation, anti-biofilm formation, cell agglutination, induction of motility or change in motility type, chemoattractant or chemorepellent, extracellular signal for sporogenesis or other morphological change, induction or inhibition of virulence gene expression, utilized as extracellular scaffold, adhesin or binding site, induction or suppression of host immune response, induction or suppression of bacterial/fungal antimicrobial molecule production, quorum-sensing, induction of swarming behavior, apoptosis or necrosis inducing in eukaryotic cells, affecting control of or inducing the initiation of cell cycle in eukaryotes, in archaea or prokaryotes, induces autolysis or programmed cell death, inhibition of phage/virus attachment or replication, evasion of innate immunity, induction or inhibition of genetic transformation or transduction competence, induction or inhibition of pilus-mediated conjugation, induction or inhibition of mating behavior in bacteria and fungi, induction or inhibition of nodule formation or metabolic compartmentalization, metal, ion, or nutrient binding, acquisition or inhibition of metal, ion, or nutrient binding and acquisition, and the like.
• In certain embodiments, compositions and methods are provided for decreasing the infectivity, morbidity, and rate of mortality associated with a variety of pathogens. The present invention also relates to methods and compositions for decontaminating areas, samples, solutions, and foodstuffs colonized or otherwise infected by pathogens and microorganisms. Certain embodiments of the present compositions are nontoxic and may be safely ingested by humans and other animals. Additionally, certain embodiments of the present invention are chemically stable and non-staining.
• In some embodiments, the present invention provides compositions and methods suitable for treating animals, including humans, exposed to pathogens or the threat of pathogens. In some embodiments, the animal is contacted with effective amounts of the compositions prior to exposure to pathogenic organisms. In other embodiments, the animal or human is contacted with effective amounts of the compositions after exposure to pathogenic organisms. Thus, the present invention contemplates both the prevention and treatment of microbiological and other infections.
• In certain embodiments compositions and methods are provided for decontaminating solutions and surfaces, including organic and inorganic samples that are exposed to pathogens or suspected of containing pathogens. In still other embodiments of the present invention, the compositions are used as additives to prevent the growth of harmful or undesired microorganisms in biological and environmental samples.
• These applications of the peptides described herein are intended to be illustrative and not limiting. Using the teaching provided herein, other uses will be recognized by one of skill in the art.
• B Illustrative Novel Antimicrobial Peptides.
• Antimicrobial peptides (also called host defense peptides) are an evolutionarily conserved component of the innate immune response and are found among all classes of life. Unmodified, these peptides are potent, broad spectrum antibiotics which demonstrate potential as novel therapeutic agents. Antimicrobial peptides have been demonstrated to kill Gram-negative and Gram-positive bacteria (including strains that are resistant to conventional antibiotics), mycobacteria (including Mycobacterium tuberculosis), enveloped viruses, and fungi.
• Naturally-occurring antimicrobial peptides are typically short peptides, generally between 12 and 50 amino acids. These peptides often include two or more positively charged residues provided by arginine, lysine or, in acidic environments, histidine, and frequently a large proportion (generally >50%) of hydrophobic residues (see, e.g., Papagianni et al. (2003) Biotechnol Adv 21: 465; Sitaram and Nagaraj (2002) Curr Pharm Des 8: 727; Durr et al. (2006) Biochim. Biophys. Acta 1758: 1408-1425).
• Frequently the secondary structures of these molecules follow 4 themes, including i) α-helical, ii) β-stranded due to the presence of 2 or more disulfide bonds, iii) β-hairpin or loop due to the presence of a single disulfide bond and/or cyclization of the peptide chain, and iv) extended. Many of these peptides are unstructured in free solution, and fold into their final configuration upon partitioning into biological membranes. The ability to associate with membranes is a definitive feature of antimicrobial peptides although membrane permeabilisation is not necessary. These peptides have a variety of antimicrobial activities ranging from membrane permeabilization to action on a range of cytoplasmic targets.
• The modes of action by which antimicrobial peptides kill bacteria is varied and includes, but is not limited to disrupting membranes, interfering with metabolism, and targeting cytoplasmic components. In many cases the exact mechanism of killing is not known.
• In certain embodiments the antimicrobial peptides include peptides comprising or consisting of one or more of the amino acid sequences shown in Tables 4 (SEQ ID NOs:1029-1078), and/or Table 5 (SEQ ID NOs:1079-1566). In various embodiments the peptides include peptides comprising or consisting of the retro, inverso, retro-inverso, and/or beta form of one or more of the amino acid sequences shown in Tables 4 (SEQ ID NOs:1029-1078), and/or Table 5 (SEQ ID NOs:1079-1566). The peptides can comprise all “L” amino acids, all “D” amino acids, or combinations of “L” and “D” amino acids. Also contemplated are circular permutations of these sequences as well as peptides comprising or consisting of the retro, inverso, retro-inverso, and/or beta form of such circular permutations.
• It will also be recognized, that in certain embodiments, any peptide or compound AMP described herein can be circularized.
• In various embodiments the peptides can optionally bear one or more protecting groups, e.g., and the amino and/or carboxyl termini, and/or on side chains.
• Also contemplated are peptides comprising one, two, three four, or five conservative substitutions of these amino acid sequences.

• TABLE 4
  Novel antimicrobial peptides, target microorganisms and MIC values.

  	Organism MIC		SEQ
  ID	(μM)	Structure/sequence	ID NO
  K-1	S. mutans, 25	GLGRVIGRLIKQIIWRR	1029
  K-2	S. mutans, 12.5	VYRKRKSILKIYAKLKGWH	1030
  K-7	S. mutans, 12.5	NYRLVNAIFSKIFKKKFIKF	1031
  K-8	S. mutans, 4	KILKFLFKKVF	1032
  K-9	S. mutans, 4	FIRKFLKKWLL	1033
  K-10	S. mutans, 4	KLFKFLRKHLL	1034
  K-11	S. mutans, 4	KILKFLFKQVF	1035
  K-12	S. mutans, 8	KILKKLFKFVF	1036
  K-13	S. mutans, 16	GILKKLFTKVF	1037
  K-14	S. mutans, 8	LRKFLHKLF	1038
  K-15	S. mutans, 4	LRKNLRWLF	1039
  K-16	S. mutans, 8	FIRKFLQKLHL	1040
  	P. aeruginosa, 12.5
  	MRSA,	25
  K-17	S. mutans, 8	FTRKFLKFLHL	1041
  K-18	S. mutans, 16	KKFKKFKVLKIL	1042
  K-19	S. mutans, 16	LLKLLKLKKLKF	1043
  K-20	S. mutans, 8	FLKFLKKFFKKLKY	1044
  K-21	S. mutans, 8	GWLKMFKKIIGKFGKF	1045
  K-22	S. mutans, 8	GIFKKFVKILYKVQKL	1046
  1T-88		GRLVLEITADEVKALGEALANAKI	1047
  PF-531	A. baumannii, 25	YIQFHLNQQPRPKVKKIKIFL-NH2	1048
  	P. aeruginosa, 50
  	T. rubrum, 50
  	A. niger, 25
  	B. subtilis, 25
  	C. difficile, 12.5
  	C. jeikeium, 6.25
  	S. epidermidis, 50
  	S. mutans, 12.5
  PF-527	P. aeruginosa, 50	GSVIKKRRKRMAKKKHRKLLKKTRIQR	1049
  	T. rubrum, 25	RRAGK
  	A. niger, 50
  	B. subtilis, 12.5
  	C. jeikeium, 6.25
  	MRSA, 50
  	S. epidermidis, 25
  PF-672	C. albicans, 1.56	MRFGSLALVAYDSAIKHSWPRPSSVRR	1050
  	T. rubrum, 0.78	LRM
  	A. niger, 3
  	B. subtilis, 0.78
  	E. faecalis, 3.13
  	MRSA, 1.56
  	S. epidermidis, 0.39
  PF-606	E. coli, 50	FESKILNASKELDKEKKVNTALSFNSHQ	1051
  	MRSA, 50	DFAKAYQNGKI
  	S. epidermidis, 50
  	S. mutans, 50
  	S. pneumoniae, 50
  PF-547	T. rubrum, 25	WSRVPGHSDTGWKVWHRW-NH2	1052
  	B. subtilis, 25
  	S. mutans, 12.5
  PF-006	A. baumannii, 50	MGIIAGIIKFIKGLIEKFTGK	1053
  	B. subtilis, 25
  	MRSA, 50
  PF-545	A. niger, 50	RESKLIAMADMIRRRI-NH2	1054
  	B. subtilis, 25
  	MRSA, 50
  PF-278	C. albicans, 50	L SLATFAKIFMTRSNWSLKRFNRL	1055
  	T. rubrum, 50
  	S. epidermidis, 50
  PF-283	T. rubrum, 50	MIRIRSPTKKKLNRNSISDWKSNTSGRF	1056
  	B. subtilis, 50	FY
  	S. epidermidis, 50
  PF-307	C. albicans, 50	MKRRRCNWCGKLFYLEEKSKEAYCCK	1057
  	T. rubrum, 50	ECRKKAKKVKK
  	B. subtilis, 50
  PF-168	T. rubrum, 50	VLPFPAIPLSRRRACVAAPRPRSRQRAS	1058
  	A. niger, 50
  	MRSA, 50
  PF-538	A. baumannii, 25	KNKKQTDILEKVKEILDKKKKTKSVGQ	1059
  	C. difficile, 25	KLY
  PF-448	A. niger, 25	SLQSQLGPCLHDQRH	1060
  	S. pneumoniae, 50
  PF-583	MRSA, 50	KFQGEFTNIGQSYIVSASHMSTSLNTGK	1061
  	S. epidermidis, 50
  PF-600	E. coli, 50	TKKIELKRFVDAFVKKSYENYILERELK	1062
  	S. pneumoniae, 50	KLIKAINEELPTK
  PF-525	A. niger, 50	KFSDQIDKGQDALKDKLGDL	1063
  	S. pneumoniae, 50
  PF-529	A. niger, 50	LSEMERRRLRKRA-NH2	1064
  	S. pneumoniae, 50
  PF-148	A. niger, 50	RRGCTERLRRMARRNAWDLYAEHFY	1065
  	B. subtilis, 50
  PF-530	A. baumannii, 25	SKFKVLRKIIIKEYKGELMLSIQKQR	1066
  PF-522	C. difficile, 25	FELVDWLETNLGKILKSKSA-NH2	1067
  PF-497	B. subtilis, 50	LVLRICTDLFTFIKWTIKQRKS	1068
  PF-499	B. subtilis, 50	VYSFLYVLVIVRKLLSMKKRIERL	1069
  PF-322	B. subtilis, 50	GIVLIGLKLIPLLANVLR	1070
  PF-511	S. pneumoniae, 50	VMQSLYVKPPLILVTKLAQQN	1071
  PF-512	S. pneumoniae, 50	SFMPEIQKNTIPTQMK	1072
  PF-520	S. pneumoniae, 50	LGLTAGVAYAAQPTNQPTNQPTNQPTN	1073
  		QPTNQPTNQPRW-NH2
  PF-521	S. pneumoniae, 50	CGKLLEQKNFFLKTR	1074
  PF-523	S. pneumoniae, 50	ASKQASKQASKQASKQASKQASRSLKN	1075
  		HLL
  PF-524	S. pneumoniae, 50	PDAPRTCYHKPILAALSRIVVTDR	1076
  PF-209	MRSA, 50	NYAVVSHT	1077
  PF-437	S. pneumoniae, 50	FQKPFTGEEVEDFQDDDEIPTII	1078

  
  Where protecting groups are shown (e.g., —NH₂) they are optional. Conversely any peptide shown without protecting groups can bear one or more such groups.
• In certain embodiments peptides that induce alterations in phenotype or other biological activities can also be used as antimicrobial effector moieties. Illustrative alternative peptides are shown in Table 5.

• TABLE 5
  Illustrative list of novel morphology, biofilm and growth disrupting peptides.

  			SEQ ID
  ID	Organism, effect	Structure/sequence	NO
  G-1	S. mutans: Ca2	DSSQSDSDSDSNSSNTNSNSSITNG	1079
  	binding
  G-2	S. mutans: biofilm	LPGTLHIQAEFPVQLEAGSLIQIFD	1080
  	structure
  G-4	S. mutans:	EIPIQLANDLANYYDISLDSIFFW	1081
  	Biofilm structure
  G-5	M. xanthus:	RDMTVAGKRPNFLIITTDEE	1082
  	Altered cell
  	morphology
  G-6	M. xanthus:	NTSIVCAVTFAPIKEVPLLWRAGLTLRS	1083
  	Altered cell	RQS
  	morphology
  G-7	M. xanthus:	QAKVEREVERDLVYTLRRLCDPSGSER	1084
  	Altered cell	TK
  	morphology
  G-8	S. mutans:	PRMIDIISFHGCHGDHQVWTDPQATAL	1085
  	Altered biofilm	PR
  	structure
  PF-001	S. epidermidis (C)	MNNWIIVAQLSVTVINEIIDIMKEKQKG	1086
  	M. luteus (C)	GK
  	MRSA (R)
  	C. jeikeium (D)
  PF-002	B. subtilis (R)	NDDAQ	1087
  	S. pneumoniae (H)
  PF-003	S. epidermidis (D)	MNNWIKVAQISVTVINEVIDIMKEKQN	1088
  	M. luteus (A)	GGK
  	MRSA (R)
  	C. jeikeium (A)
  PF-004	S. epidermidis (A)	ARLSKAIIIAVIVVYHLDVRGLF	1089
  	M. luteus (A)
  	MRSA (R)
  	C. jeikeium (A)
  PF-005	B. subtilis (C)	MESIFKIKLMNGICRSENMNMKKKNK	1090
  	S. pneumoniae (H)	GEKI
  PF-006	S. epidermidis (D)	MGIIAGIIKFIKGLIEKFTGK	1091
  	M. luteus (A)
  	B. subtilis (I)
  	MRSA (I)
  	S. pneumoniae (R)
  	C. jejuni (D)
  PF-007	S. epidermidis (A)	MGIIAGIIKVIKSLIEQFTGK	1092
  	M. luteus (A)
  	E. coli (A)
  	MRSA (R)
  	E. faecalis (A)
  PF-008	B. subtilis (D)	MIEIGSIAYLNGGSKKYNHILNQENR	1093
  	C. jejuni (R)
  PF-009	S. epidermidis (S)	SKKYNHILNQENR	1094
  PF-010	S. epidermidis (S)	MDIDVNKLLQAFVYFKSFEKLRHNNS	1095
  	M. luteus (A)
  	MRSA (R)
  	C. jeikeium (A)
  PF-011	MRSA (R)	MFCYYKQHKGDNFSIEEVKNIIADNEM	1096
  	C. jeikeium (C)	KVN
  PF-012	S. epidermidis (S)	WRGPNTEAGGKSANNIVQVGGAPT	1097
  	M. luteus (C)
  	MRSA (R)
  	C. jeikeium (A)
  PF-013	S. epidermidis (C)	LIQKGLNQTFIVVIRLNNFIKKS	1098
  	M. luteus (D)
  	MRSA (R)
  	C. jeikeium (D)
  PF-015	MRSA (W)	SIDKRNLYNLKYYE	1099
  PF-017	MRSA (M)	ESIIE	1100
  PF-019	MRSA (M)	NDTNK	1101
  PF-020	S. mutans (F)	MKIILLLFLIFGFIVVVTLKSEHQLTLFSI	1102
  	S. epidermidis (C)
  	M. luteus (C)
  	MRSA (C)
  	S. pneumoniae (D)
  PF-021	S. epidermidis (A)	FSLNFSKQKYVTVN	1103
  	M. luteus (A)
  	MRSA (R)
  	C. jeikeium (R)
  PF-022	S. epidermidis (D)	MINELKNKNSGIMNNYVVTKESKL	1104
  	M. luteus (A)
  	MRSA (R)
  	C. jeikeium (A)
  PF-023	MRSA (S)	MTKNTIISLENEKTQINDSENESSDLRK	1105
  		AK
  PF-024	S. epidermidis (D)	DLRKAK	1106
  	MRSA (M)
  PF-025	S. epidermidis (S)	LLIIFRLWLELKWKNKK	1107
  	M. luteus (A)
  	MRSA (R)
  	C. jeikeium (A)
  PF-026	MRSA (M)	SIHFIN	1108
  PF-027	S. epidermidis (D)	HNARKYLEFISQKIDGDKLTKEDSL	1109
  	MRSA (M)
  PF-028	S. epidermidis (M)	ALDCSEQSVILWYETILDKIVGVIK	1110
  	MRSA (R)
  	C. jeikeium (M)
  PF-029	MRSA (M)	NSTNE	1111
  PF-030	S. epidermidis (D)	MTCHQAPTTTHQSNMA	1112
  	M. luteus (C)
  	MRSA (R)
  	C. jeikeium (C)
  PF-031	MRSA (M)	MPHHSTTSSRIVVPAHQSNMASTPNLSI	1113
  		TP
  PF-032	S. epidermidis (S)	RIVVPAHQSNMASTPNLSITP	1114
  	C. jeikeium (C)
  PF-033	S. epidermidis (M)	MFIFKTTSKSHFHNNVKSLECIKIPINK	1115
  	B. subtilis (C)	NR
  	MRSA (M)
  	S. pneumoniae (R)
  	C. jeikeium (D)
  	C. jejuni (R)
  PF-034	S. epidermidis (A)	EPKKKHFPKMESASSEP	1116
  PF-035	MRSA (M)	SFYESY	1117
  PF-036	S. epidermidis (S)	ILNRLSRIVSNEVTSLIYSLK	1118
  	M. luteus (A)
  	MRSA(R)
  	C. jeikeium (A)
  PF-037	S. epidermidis (D)	MTKKRRYDTTEFGLAHSMTAKITLHQ	1119
  	M. luteus (C)	ALYK
  	MRSA (R)
  	C. jeikeium (D)
  PF-040	S. mutans (F)	MIHLTKQNTMEALHFIKQFYDMFFILN	1120
  	S. epidermidis (D)	FNV
  	M. luteus (D)
  	B. subtilis (D)
  	P. mirabilis (C)
  	E. coli (C)
  	MRSA (D)
  	S. pneumoniae (D)
  	C. jeikeium (D)
  	C. jejuni (D)
  PF-041	S. epidermidis (R)	ELLVILPGFI	1121
  	MRSA (M)
  PF-042	S. epidermidis (D)	LLSYFRYTGALLQSLF	1122
  	M. luteus (C)
  	MRSA (R)
  	C. jeikeium (S)
  PF-043	S. epidermidis (D)	MIKNETAYQMNELLVIRSAYAK	1123
  	M. luteus (C)
  	MRSA (R)
  	C. jeikeium (A)
  PF-045	MRSA (S)	LDINDYRSTY	1124
  PF-046	S. epidermidis (C)	LDFYLTKHLTLML	1125
  	MRSA (R)
  	C. jeikeium (R)
  PF-048	S. epidermidis (D)	LYFAFKKYQERVNQAPNIEY	1126
  	MRSA (W)
  	C. jeikeium (S)
  PF-049	MRSA (S)	AYYLKRREEKGK	1127
  PF-051	S. mutans (D)	RFFNFEIKKSTKVDYVFAHVDLSDV	1128
  	S. epidermidis (D)
  	M. luteus (C)
  	MRSA (D)
  	S. pneumoniae (D)
  PF-052	S. epidermidis (S)	QELINEAVNLLVKSK	1129
  	M. luteus (A)
  	MRSA (R)
  	C. jeikeium (D)
  PF-053	S. epidermidis (C)	KLFGQWGPELGSIYILPALIGSIILIAIVT	1130
  	M. luteus (D)	LILRAMRK
  	B. subtilis (H)
  	E. coli (A)
  	P. aeruginosa (A)
  	C. albicans (A)
  	MRSA (D)
  	S. pneumoniae (S)
  	E. faecalis (A)
  	C. jeikeium (D)
  	C. jejuni (D)
  PF-056	S. epidermidis (D)	AEQLFGKQKQRGVDLFLNRLTIILSILF	1131
  	M. luteus (D)	FVLMICISYLGM
  	B. subtilis (C)
  	C. albicans (B)
  	MRSA (M)
  	S. pneumoniae (D)
  	C. jeikeium (S)
  	C. jejuni (D)
  PF-057	S. epidermidis (D)	TMIVISIPRFEEYMKARHKKWM	1132
  	M. luteus (C)
  	E. coli (M)
  	C. albicans (A)
  	MRSA (M)
  	S. pneumoniae (R)
  	E. faecalis (A)
  	C. jeikeium (A)
  	C. jejuni (D)
  PF-058	MRSA (M)	FADQSQDNA	1133
  PF-059	C. jejuni (C)	TITLKAGIERALHEEVPGVIEVEQVF	1134
  PF-061	S. epidermidis (R)	GYNSYKAVQDVKTHSEEQRVTAKK	1135
  	B. subtilis (R)
  	S. pneumoniae (R)
  	C. jejuni (R)
  PF-063	S. epidermidis (R)	IAAIIVLVLFQKGLLQIFNWILIQLQ	1136
  	M. luteus (R)
  	B. subtilis (C)
  	P. aeruginosa (A)
  	MRSA (M)
  	S. pneumoniae (D)
  	C. jeikeium (D)
  	C. jejuni (D)
  PF-064	S. epidermidis (D)	DYYGKE	1137
  	MRSA (M)
  PF-065	S. epidermidis (D)	LEKNTRDNYFIHAIDRIYINTSKGLFPES	1138
  	MRSA (R)	ELVAWG
  	C. jeikeium (A)
  PF-066	MRSA (S)	IKGTVKAVDETTVVITVNGHGTELTFE	1139
  		KPAIKQVDPS
  PF-067	S. epidermidis (D)	DLIVKVHICFVVKTASGYCYLNKREAQ	1140
  	M. luteus (R)	AAI
  	B. subtilis (C)
  	P. aeruginosa (A)
  	MRSA (M)
  	S. pneumoniae (D)
  	C. jeikeium (D)
  	C. jejuni (D)
  PF-068	S. epidermidis (M)	SHLINNFGLSVINPSTPICLNFSPVFNLL	1141
  	M. luteus (D)	TVYGITCN
  	B. subtilis (A)
  	E. coli (A)
  	MRSA (M)
  	S. pneumoniae (D)
  	E. faecalis (A)
  	C. jeikeium (R)
  	C. jejuni (D)
  PF-069	B. subtilis (D)	FDPVPLKKDKSASKHSHKHNH	1142
  	C. jejuni (R)
  PF-070	B. subtilis (D)	SMVKSEIVDLLNGEDNDD	1143
  PF-071	S. epidermidis (R)	HCVIGNVVDIANLLKRRAVYRDIADVI	1144
  	M. luteus (R)	KMR
  	B. subtilis (D)
  	C. albicans (B)
  	MRSA (C)
  	S. pneumoniae (A)
  	C. jejuni (A)
  PF-073	S. epidermidis (R)	CPSVTMDACALLQKFDFCNNISHFRHF	1145
  	M. luteus (R)	FAIKQPIER
  	MRSA (M)
  	S. pneumoniae (D)
  	C. jeikeium (D)
  	C. jejuni (D)
  PF-074	S. epidermidis (D)	RDIHPIYFMTKD	1146
  	MRSA (M)
  PF-075	S. epidermidis (D)	FVNSLIMKDLSDNDMRFKYEYYNREK	1147
  	M. luteus (A)	DT
  	MRSA (R)
  	C. jeikeium (D)
  PF-076	S. epidermidis (S)	LYQYELLSKEEYLKCTLIINQRRNEQK	1148
  	M. luteus (A)
  	MRSA (R)
  	C. jeikeium (A)
  PF-099	S. epidermidis (D)	EIIAYLEGRFANA	1149
  	C. jeikeium (C)
  PF-123	S. epidermidis (M)	TTRPQVAEDRQLDDALKETFPASDPISP	1150
  PF-124	S. epidermidis (C)	MADGQIAAIAKLHGVPVATRNIRHFQS	1151
  	C. jeikeium (R)	FGVELINPWSG
  PF-125	S. epidermidis (D)	YVVGALVILAVAGLIYSMLRKA	1152
  	M. luteus (C)
  PF-127	S. epidermidis (M)	MLRYLSLFAVGLATGYAWGWIDGLA	1153
  	M. luteus (A)	ASLAV
  	C. jeikeium (A)
  PF-128	S. epidermidis (D)	GIKVVAARFEEIQFSENFDSIILA	1154
  	P. aeruginosa (C)
  PF-129	S. epidermidis (M)	MKLLARDPWVCAWNDIW	1155
  	C. jeikeium (R)
  PF-133	C. jeikeium (R)	GDPTAGQKPVECP	1156
  PF-135	C. jeikeium (R)	PPARPARIPQTPTLHGASLFRQRS	1157
  PF-137	S. epidermidis (D)	VLGKGHDLLDVGKTALKSRVFAWLG	1158
  	M. luteus (D)	GS
  	C. jeikeium (A)
  PF-139	S. epidermidis (M)	ALSKPAIQARTLCRRQDPP	1159
  	M. luteus (C)
  	C. jeikeium (R)
  PF-140	S. epidermidis (D)	FHRRVIRASEWALTTRSFSTPLRSAAR	1160
  	M. luteus (R)
  	P. aeruginosa (A)
  	C. albicans (B)
  	MRSA (M)
  	S. pneumoniae (D)
  	C. jeikeium (D)
  	C. jejuni (D)
  PF-143	P. aeruginosa (C)	LSPRPIIVSRRSRADNNNDWSR	1161
  PF-144	S. pneumoniae (H)	RSGQPVGRPSRRAWLR	1162
  PF-145	S. epidermidis (D)	GIVLTGRAGLVSGACSMALGVGLG	1163
  	M. luteus (A)
  	B. subtilis (C)
  	MRSA (M)
  	S. pneumoniae (R)
  	C. jeikeium (R)
  	C. jejuni (R)
  PF-148	S. epidermidis (D)	RRGCTERLRRMARRNAWDLYAEHFY	1164
  	M. luteus (A)
  	B. subtilis (I)
  	C. albicans (B)
  	MRSA (C)
  	S. pneumoniae (R)
  	C. jeikeium (H)
  	C. jejuni (H)
  PF-149	MRSA (H)	GKVSVLTRVPRSLGGAPANQ	1165
  PF-153	S. epidermidis (M)	GILARADCSQIA	1166
  	C. jeikeium (C)
  PF-156	MRSA (H)	LITAEQPATAPIAGK	1167
  PF-157	S. epidermidis (M)	HTAVVWLAGVSGCVALSHCEPA	1168
  PF-164	C. jeikeium (R)	EEVSRALAGIGLGLGCRIG	1169
  PF-168	P. aeruginosa (H)	VLPFPAIPLSRRRACVAAPRPRSRQRAS	1170
  	MRSA (I)
  PF-171	S. epidermidis (R)	TQVTLCRTW	1171
  	M. luteus (R)
  	B. subtilis (D)
  	MRSA (M)
  	S. pneumoniae (D)
  	C. jejuni (R)
  PF-173	S. epidermidis (A)	AGRTAIVQGGG	1172
  	C. jeikeium (D)
  PF-175	M. luteus (S)	RRRPAGQRPEKASQAMIAA	1173
  	B. subtilis (D)
  	C. albicans (B)
  	S. pneumoniae (A)
  	C. jejuni (M)
  PF-176	S. epidermidis (C)	RLTSNQFLTRITPFVFAQH	1174
  	M. luteus (C)
  	C. jeikeium (D)
  PF-178	S. epidermidis (D)	EVYSSPTNNVAITVQNN	1175
  	E. coli (C)
  	MRSA (M)
  	S. pneumoniae (D)
  PF-180	S. epidermidis (C)	SGLGDLGFSSEAK	1176
  PF-186	S. epidermidis (C)	DADKNLSLERDRFAWRVAAP	1177
  	C. jeikeium (A)
  PF-188	C. jeikeium (H)	ARTFAGRLGTRYFGGLMRSTKA	1178
  PF-190	S. epidermidis (C)	HFILRKPLLFMIHSLKTGPLDRF	1179
  	C. jeikeium (R)
  PF-191	S. epidermidis (A)	QFCNFAWLFLASNNAQVSALA	1180
  	MRSA (H)
  	C. jeikeium (R)
  PF-192	S. epidermidis (D)	VEEDEAPPPHY	1181
  PF-196	S. epidermidis (C)	TTARYIRRQCHTSITPLSQG	1182
  	C. jeikeium (R)
  PF-199	S. epidermidis (C)	FPAFSFGAIAGSVSVAR	1183
  	M. luteus (A)
  	C. jeikeium (R)
  PF-203	S. epidermidis (A)	SWKCHHLAI	1184
  	C. jeikeium (R)
  PF-204	S. epidermidis (C)	ALQKQDMNLPSVKNQLVFLKSTG	1185
  	M. luteus (C)
  	P. aeruginosa (H)
  	C. jeikeium (D)
  PF-208	S. epidermidis (D)	DAYHCHLVRSPDAHDLSMRIGFV	1186
  	C. jeikeium (A)
  PF-209	S. epidermidis (C)	NYAVVSHT	1187
  	P. aeruginosa (H)
  	MRSA (I)
  PF-212	M. luteus (M)	NDSKASN	1188
  PF-215	M. luteus (T)	ELKITNYNVNTVLYRYYKWGNDLCE	1189
  PF-220	S. pneumoniae (H)	VDPADDGTRHIRPEDGDPIEIDE	1190
  PF-224	M. luteus (T)	DYFYITLSQKNTF	1191
  PF-226	S. epidermidis (C)	LMFFSENMDKRDTLSGKFRYFAGSKVI	1192
  	M. luteus (T)	KLMNWLSENGK
  PF-233	S. epidermidis (C)	DANAMARTTIAIVYILALIALTISYSL	1193
  PF-234	M. luteus (T)	RTPYILRS	1194
  PF-235	M. luteus (T)	GIPFSKPHKRQVNYMKSDVLAYIEQNK	1195
  		MAHTA
  PF-249	M. luteus (R)	INSRYKISF	1196
  PF-250	M. luteus (T)	SEDIFGRLANEKANGLEELRKIRLKQ	1197
  PF-255	M. luteus (M)	DHKINESQHNPFRSDSNKQNVDFF	1198
  PF-257	M. luteus (R)	VWENRKKYLENEIERHNVFLKLGQEVI	1199
  		KGLNALASRGR
  PF-264	M. luteus (H)	MQSLSNRQSLIASYILMGIFLSFGYPPA	1200
  		SLSKFFCRLSHL
  PF-270	M. luteus (H)	MYLTPYAWIAVGSIFAFSVTTIKIGDQN	1201
  		DEKQKSHKNDVHKR
  PF-271	M. luteus (T)	AAQPQTTSP	1202
  PF-273	S. epidermidis (C)	LVGALLIFVALIYMVLKGNADKN	1203
  PF-274	M. luteus (M)	SIQEAEKIIKNDPFYIHDVADYDFMWF	1204
  		EPSKSLEEIKEFV
  PF-276	M. luteus (M)	LDLALSTNSLNLEGFSF	1205
  PF-278	S. epidermidis (I)	LSLATFAKIFMTRSNWSLKRFNRL	1206
  	M. luteus (R)
  	C. albicans (B)
  PF-283	S. epidermidis (H)	MIRIRSPTKKKLNRNSISDWKSNTSGRF	1207
  	B. subtilis (H)	FY
  PF-289	B. subtilis (C)	MGRHLWNPSYFVATVSENTEEQIRKY	1208
  		RKNK
  PF-290	S. epidermidis (C)	MVHDMTNGTLIIVKH	1209
  PF-292	S. epidermidis (C)	SFVSTTVRLIFEESKRYKF	1210
  	B. subtilis (C)
  PF-293	S. epidermidis (C)	YDPLK	1211
  PF-294	S. epidermidis (C)	DFLVNFLWFKGELNWGKKRYK	1212
  PF-296	S. epidermidis (C)	GAFGMPSIKTNTICGEKGKFISACDAW	1213
  	B. subtilis (C)	LSNLK
  PF-297	S. epidermidis (C)	ISKGIDDIVYVINKILSIGNIFKIIKRK	1214
  	B. subtilis (C)
  PF-301	S. epidermidis (C)	GIVLIGLKLIPLLANVLN	1215
  	B. subtilis (C)
  PF-303	B. subtilis (C)	EYPWSWISEPWPWDKSFYK	1216
  PF-305	B. subtilis (C)	MREWICPSCNETHDRDINASINILKEGL	1217
  		RLITIQNK
  PF-306	B. subtilis (C)	GCILPHKKDNYNYIMSKFQDLVKITSK	1218
  		K
  PF-307	S. epidermidis (T)	MKRRRCNWCGKLFYLEEKSKEAYCC	1219
  	B. subtilis (H)	KECRKKAKKVKK
  	C. albicans (B)
  PF-310	S. epidermidis (C)	GVALIGTILVPLLSGLFG	1220
  PF-313	S. epidermidis (C)	YITSHKNARAIIKKFERDEILEEVITHYL	1221
  		NRK
  PF-318	S. epidermidis (C)	MGRHLWNPSYFVATVSENTEEQIRKYI	1222
  	B. subtilis (C)	NNQKKQVK
  PF-319	S. epidermidis (C)	SIGSMIGMYSFRHKTKHIKFTFGIPFILF	1223
  	B. subtilis (C)	LQFLLVYFYILK
  PF-322	S. epidermidis (C)	GIVLIGLKLIPLLANVLR	1224
  	B. subtilis (H)
  PF-335	S. epidermidis (C)	AAYPIEDWSDWYEDFFIMLSNI	1225
  	B. subtilis (C)
  PF-339	S. epidermidis (C)	KKIDILINKYMYLSK	1226
  	B. subtilis (C)
  PF-342	S. epidermidis (C)	AFSGVYKTLIVYTRRK	1227
  	B. subtilis (C)
  PF-344	E. coli (A)	DERLPEAKAIRNFNGSVMVLGR	1228
  PF-347	S. epidermidis (C)	GIFTGVTVVVSLKHC	1229
  	E. coli (C)
  	MRSA (C)
  	E. faecalis (C)
  PF-349	S. epidermidis (C)	MPKSCHVPVLCDFFFLVIIKFLALFKTI	1230
  	E. coli (C)	QS
  	MRSA (C)
  	E. faecalis (C)
  PF-350	S. epidermidis (C)	LAVILRAIVY	1231
  	E. coli (C)
  	MRSA (C)
  PF-354	MRSA (H)	FTFSKCRASNGRGFGTLWL	1232
  PF-355	S. epidermidis (C)	WIAIGLLLYFSLKNQ	1233
  	E. coli (C)
  	P. aeruginosa (A)
  	MRSA (A)
  	S. pneumoniae (D)
  	E. faecalis (D)
  	C. jejuni (D)
  PF-356	S. epidermidis (S)	VSIKIGAIVIGMIGLMELLTE	1234
  	P. aeruginosa (A)
  	MRSA (C)
  	S. pneumoniae (R)
  	E. faecalis (R)
  	C. jejuni (D)
  PF-357	S. epidermidis (M)	MLTIIIGFIFWTMTLMLGYLIGEREGRK	1235
  	M. luteus (C)	RE
  	MRSA (M)
  	S. pneumoniae (M)
  PF-360	S. epidermidis (S)	MEQKVKVIFVPRSKPDNQLKTFVSAVL	1236
  	E. coli (C)	FKA
  	MRSA (H)
  PF-362	E. coli (C)	NIERILKEKVWMIRCVE	1237
  	MRSA (C)
  PF-363	S. epidermidis (S)	SMLSVTVMCLMHASVAANQAMEKKV	1238
  	E. coli (C)
  	MRSA (H)
  	S. pneumoniae (R)
  	E. faecalis (D)
  	C. jejuni (D)
  PF-366	S. epidermidis (R)	ALCSVIKAIELGIINVHLQ	1239
  	E. coli (C)
  	P. aeruginosa (A)
  	MRSA (D)
  	S. pneumoniae (C)
  	E. faecalis (C)
  	C. jejuni (D)
  PF-369	S. epidermidis (S)	MSEAVNLLRGARYSQRYAKNQVPYEV	1240
  	E. coli (R)	IIEK
  	MRSA (H)
  	E. faecalis (C)
  PF-370	S. epidermidis (C)	VIFLHKESGNLKEIFY	1241
  	E. coli (R)
  	MRSA (C)
  PF-373	S. epidermidis (M)	HFYLLFER	1242
  	MRSA (M)
  PF-374	S. epidermidis (C)	HLFFVKGMFILCQKNQINDE	1243
  	E. coli (C)
  	MRSA (M)
  	E. faecalis (C)
  PF-375	S. epidermidis (C)	MDSAKAQTMRTDWLAVSCLVASAYL	1244
  	E. coli (C)	RSMLA
  	MRSA (C)
  	E. faecalis (C)
  PF-376	S. epidermidis (C)	MTVFEALMLAIAFATLIVKISNKNDKK	1245
  	E. coli (C)
  	MRSA (C)
  	E. faecalis (C)
  PF-378	S. epidermidis (M)	ESAKSNLNFLMQEEWALFLLL	1246
  	MRSA (M)
  PF-379	S. epidermidis (C)	VFVVLFIIYLASKLLTKLFPIKK	1247
  	E. coli (C)
  	MRSA (C)
  	E. faecalis (C)
  PF-380	S. epidermidis (C)	KKIIPLITLFVVTLVG	1248
  	E. coli (C)
  	P. aeruginosa (A)
  	MRSA (D)
  	S. pneumoniae (D)
  	E. faecalis (C)
  	C. jejuni (D)
  PF-381	S. epidermidis (C)	QGANPCQQVGFTVNDPDCRLAKTV	1249
  	E. coli (R)
  	MRSA (C)
  	E. faecalis (C)
  PF-382	MRSA (M)	KYKCSWCKRVYTLRKDHKTAR	1250
  PF-383	S. epidermidis (C)	WSEIEINTKQSN	1251
  	E. coli (R)
  PF-385	E. coli (A)	MIKKSILKIKYYVPVLISLTLILSA	1252
  PF-386	S. epidermidis (C)	FTLTLITTIVAILNYKDKKK	1253
  	E. coli (C)
  	MRSA (C)
  	E. faecalis (C)
  PF-387	S. epidermidis (C)	GAVGIAFFAGNMKQDKRIADRQNKKS	1254
  	E. coli (M)	EKK
  	MRSA (C)
  	E. faecalis (C)
  PF-389	S. epidermidis (R)	GLQFKEIAEEFHITTTALQQWHKDNGY	1255
  	MRSA (C)	PIYNKNNRK
  	S. pneumoniae (D)
  	E. faecalis (R)
  	C. jejuni (R)
  PF-390	S. epidermidis (D)	VVAYVITQVGAIRF	1256
  	E. coli (C)
  	MRSA (D)
  	S. pneumoniae (D)
  	E. faecalis (D)
  	C. jejuni (D)
  PF-392	MRSA (S)	DPAGCNDIVRKYCK	1257
  	E. faecalis (A)
  	C. jejuni (A)
  PF-393	S. epidermidis (R)	DLVQSILSEFKKSG	1258
  	MRSA (C)
  	S. pneumoniae (R)
  	E. faecalis (A)
  	C. jejuni (R)
  PF-394	MRSA (C)	VLKEECYQKN	1259
  	E. faecalis (A)
  PF-395	S. epidermidis (C)	YCVPLGNMGNMNNKIW	1260
  	E. coli (R)
  	MRSA (C)
  PF-396	S. epidermidis (S)	LIYTILASLGVLTVLQAILGREPKAVKA	1261
  	E. coli (C)
  	MRSA (C)
  	E. faecalis (C)
  PF-397	S. epidermidis (C)	VEDLMEDLNA	1262
  PF-398	S. epidermidis (C)	ILVVLAGILLVVLSYVGISKFKMNC	1263
  	E. coli (C)
  	MRSA (C)
  	E. faecalis (C)
  PF-399	S. epidermidis (C)	FPIISALLGAIICIAIYSFIVNRKA	1264
  	E. coli (C)
  	MRSA (C)
  	E. faecalis (C)
  PF-401	S. epidermidis (C)	YWLSRVTTGHSFAFEKPVPLSLTIK	1265
  	E. coli (R)
  	MRSA (C)
  	E. faecalis (C)
  PF-403	S. epidermidis (M)	LLSTEQLLKYYDGETFDGFQLPSNE	1266
  	E. coli (R)
  	MRSA (M)
  PF-404	S. epidermidis (M)	VLYFQATVV	1267
  	MRSA (M)
  PF-405	MRSA (M)	LVRIEVDDLEEWYERNFI	1268
  PF-406	S. epidermidis (C)	YLEMNADYLSNMDIFDELWEKYLENN	1269
  	MRSA (M)	K
  PF-407	S. epidermidis (M)	KPKNKKEKTVISYEKLLSMY	1270
  	MRSA (C)
  	S. pneumoniae (R)
  	E. faecalis (R)
  PF-408	S. epidermidis (M)	YCVPLGNMGNMNNKIW	1271
  	MRSA (M)
  PF-410	S. epidermidis (C)	FALELIALCRNLFIVYFP	1272
  	E. coli (S)
  	MRSA (M)
  	E. faecalis (C)
  PF-411	S. epidermidis (C)	WVAVAILLNIALQTQLT	1273
  	E. coli (C)
  	P. aeruginosa (A)
  	MRSA (D)
  	S. pneumoniae (D)
  	E. faecalis (D)
  	C. jejuni (D)
  PF-413	S. epidermidis (C)	TFAGSIKIGVPDLVHVTFNCKR	1274
  	E. coli (S)
  	MRSA (C)
  PF-414	S. pneumoniae (H)	LLNKKLE	1275
  PF-415	S. pneumoniae (D)	MIDVTIGQKSKTGAFNASYSICFSGENF	1276
  		SF
  PF-416	S. pneumoniae (H)	SKAGLYGKIERSDKRE	1277
  PF-417	S. epidermidis (M)	DSYFRS	1278
  	MRSA (M)
  	S. pneumoniae (M)
  PF-418	S. epidermidis (M)	FFLVHFYIRKRKGKVSIFLNYF	1279
  	E. coli (C)
  	MRSA (D)
  	S. pneumoniae (D)
  	E. faecalis (D)
  	C. jejuni (D)
  PF-419	S. pneumoniae (H)	VVTGKVGSLPQIK	1280
  PF-421	S. pneumoniae (H)	KHCFEITDKTDVV	1281
  PF-422	S. epidermidis (R)	MSRKKYENDEKSQKKLKIGRKSDVFY	1282
  	MRSA (C)	GIID
  	S. pneumoniae (C)
  	E. faecalis (R)
  	C. jejuni (R)
  PF-423	S. pneumoniae (H)	AGKKERLLSFREQFLNKNKKK	1283
  PF-424	S. pneumoniae (H)	IAAFVTSRAFSDTVSPI	1284
  PF-425	S. epidermidis (D)	MMELVLKTIIGPIVVGVVLRIVDKWLN	1285
  	E. coli (C)	KDK
  	P. aeruginosa (A)
  	C. albicans (A)
  	MRSA (D)
  	S. pneumoniae (D)
  	E. faecalis (D)
  	C. jejuni (D)
  PF-426	S. epidermidis (D)	MLQKYTQMISVTKCIITKNKKTQENVD	1286
  	E. coli (C)	AYN
  	C. albicans (A)
  	MRSA (D)
  	S. pneumoniae (D)
  	E. faecalis (D)
  	C. jejuni (D)
  PF-427	E. coli (C)	YVLEYHGLRATQDVDAFMAL	1287
  	MRSA (C)
  	S. pneumoniae (R)
  	E. faecalis (C)
  PF-428	S. pneumoniae (H)	ENEESIF	1288
  PF-429	S. epidermidis (C)	AATLICVGSGIMSSL	1289
  	MRSA (C)
  	S. pneumoniae (M)
  	E. faecalis (C)
  PF-430	S. epidermidis (M)	AVVCGYLAYTATS	1290
  	MRSA (M)
  	S. pneumoniae (M)
  PF-431	S. epidermidis (M)	VAYAAICWW	1291
  	MRSA (C)
  	S. pneumoniae (R)
  	E. faecalis (R)
  	C. jejuni (R)
  PF-432	S. epidermidis (M)	FNGDSEFFLCIAF	1292
  	E. coli (R)
  	P. aeruginosa (A)
  	MRSA (M)
  	S. pneumoniae (D)
  	E. faecalis (D)
  	C. jejuni (D)
  PF-433	S. pneumoniae (H)	MRKEFHNVLSSGQLLADKRPARDYNR	1293
  		K
  PF-434	S. pneumoniae (S)	GQLLADKRPARDYNRK	1294
  PF-437	S. pneumoniae (I)	FQKPFTGEEVEDFQDDDEIPTII	1295
  PF-439	S. epidermidis (C)	RVLVLKKFHGIMDGNRNVAVFFVGQ	1296
  	E. coli (R)
  	MRSA (M)
  	S. pneumoniae (R)
  	E. faecalis (C)
  PF-440	S. epidermidis (C)	MFIISPDLFNIAVILYILFFIHDILLLILS	1297
  	E. coli (R)
  	MRSA (C)
  	S. pneumoniae (R)
  	E. faecalis (C)
  PF-442	MRSA (M)	MQIFYIKTKIFLSFFLFLLIFSQCFYKIEE	1298
  	S. pneumoniae (C)
  PF-443	E. coli (R)	KLLYFFNYFENLQQVHLLVQL	1299
  	MRSA (C)
  	S. pneumoniae (C)
  PF-444	S. epidermidis (C)	MAAKLWEEGKMVYASSASMTKRLKL	1300
  	E. coli (R)	AMSKV
  	MRSA (C)
  	S. pneumoniae (R)
  	E. faecalis (C)
  PF-445	S. pneumoniae (M)	ASMTKRLKLAMSKV	1301
  PF-446	S. pneumoniae (H)	SGNEKV	1302
  PF-447	S. epidermidis (C)	IDKSRNKDQFSHIFGLYNICSG	1303
  	MRSA (C)
  	S. pneumoniae (C)
  	E. faecalis (C)
  PF-448	S. pneumoniae (I)	SLQSQLGPCLHDQRH	1304
  PF-449	S. pneumoniae (H)	MPTTKSKQKGWTNTKKASNTQ	1305
  PF-450	MRSA (C)	HRNLIILQRTIFI	1306
  	S. pneumoniae (C)
  	E. faecalis (C)
  PF-451	S. epidermidis (C)	MVNYIIGSYMLYREQNNNEALRKFDIT	1307
  	E. coli (R)	LAM
  	MRSA (C)
  	S. pneumoniae (C)
  	E. faecalis (C)
  PF-452	S. epidermidis (C)	MNNWIKVAQISVTVINEVIDIMKEKQN	1308
  	E. coli (C)	GGK
  	MRSA (C)
  	S. pneumoniae (R)
  	E. faecalis (C)
  PF-453	S. epidermidis (C)	IIQDIAHAFGY	1309
  	E. coli (C)
  	MRSA (C)
  	S. pneumoniae (C)
  PF-454	S. epidermidis (C)	MSVFVPVTNIFMFIMSPIFNVNLLHFKV	1310
  	E. coli (R)	YI
  	P. aeruginosa (H)
  	MRSA (C)
  	S. pneumoniae (R)
  	E. faecalis (C)
  PF-455	S. pneumoniae (A)	MARNDDDIKKIKGTLGQSPEVYGERK	1311
  		LPYT
  PF-456	E. faecalis (A)	TCVKPRTIN	1312
  	C. jejuni (A)
  PF-457	S. pneumoniae (M)	INKYHHIA	1313
  PF-458	P. aeruginosa (H)	ISLIIFIMLFVVALFKCITNYKHQS	1314
  	MRSA (M)
  	S. pneumoniae (M)
  PF-459	S. pneumoniae (H)	EKRMSFNENQSHRPLL	1315
  PF-460	S. epidermidis (C)	MEHVLPFQNTPPNIVIIYKDFTHLKSITF	1316
  	E. coli (H)	S
  	MRSA (C)
  	S. pneumoniae (R)
  	E. faecalis (C)
  PF-461	MRSA (R)	MTLAIKNCSVTKCLGFGDFVNDDSDS	1317
  	S. pneumoniae (R)	YFDA
  	E. faecalis (A)
  PF-462	S. pneumoniae (H)	KNKTDTL	1318
  PF-464	S. pneumoniae (S)	VDMVNRFLGN	1319
  PF-465	S. pneumoniae (H)	KPVGKALEEIADGKIEPVVPKEYLG	1320
  PF-466	S. pneumoniae (H)	VRKSDQ	1321
  PF-467	S. pneumoniae (H)	YYKDYFKEI	1322
  PF-468	S. pneumoniae (H)	EDNKDKKDKKDK	1323
  PF-469	S. epidermidis (D)	YKVNYNNIDNHFNTLRH	1324
  	E. coli (C)
  	MRSA (D)
  	S. pneumoniae (D)
  	E. faecalis (D)
  	C. jejuni (D)
  PF-470	E. faecalis (A)	PYSDSYATRPHWEQHRAR	1325
  	C. jejuni (A)
  PF-471	S. epidermidis (C)	MVGKIRGVTPRNDLLNANITGQLNLN	1326
  	E. coli (C)	YRLI
  	P. aeruginosa (A)
  	MRSA (D)
  	S. pneumoniae (D)
  	E. faecalis (C)
  	C. jejuni (D)
  PF-472	MRSA (C)	MHISHLLDEVEQTEREKAVNVLENMN	1327
  	S. pneumoniae (R)	GNVI
  	E. faecalis (A)
  	C. jejuni (R)
  PF-473	S. epidermidis (R)	MAADIISTIGDLVKWIIDTVNKFKK	1328
  	E. coli (C)
  	MRSA (C)
  	S. pneumoniae (H)
  	E. faecalis (R)
  	C. jejuni (R)
  PF-474	S. epidermidis (C)	MHRNLVLVKMEPIPHIMIIANQIGIIIEK	1329
  	E. coli (C)	A
  	P. aeruginosa (A)
  	C. albicans (B)
  	MRSA (D)
  	S. pneumoniae (D)
  	E. faecalis (C)
  	C. jejuni (D)
  PF-475	S. epidermidis (M)	MREKVRFTQAFKLFWTNYFNFKGRSR	1330
  	C. albicans (B)	RSEY
  	MRSA (S)
  	S. pneumoniae (R)
  	E. faecalis (R)
  	C. jejuni (R)
  PF-476	S. pneumoniae (H)	WADAQYKLCENCSE	1331
  PF-477	S. pneumoniae (H)	HKNKLNIPHIKS	1332
  PF-478	S. epidermidis (C)	HLFILKSHLKPFPPFRYTYD	1333
  	E. coli (C)
  	MRSA (H)
  	S. pneumoniae (C)
  PF-479	S. pneumoniae (C)	AYILKRREEKNK	1334
  PF-480	S. epidermidis (C)	MVEILVNTAISVYIVALYTQWLSTRDN	1335
  	E. coli (R)	LKA
  	MRSA (C)
  	S. pneumoniae (R)
  	E. faecalis (C)
  PF-482	S. pneumoniae (S)	LVGYVRTSGTVRSYKIN	1336
  PF-484	E. faecalis (A)	HKKDIRKQVFKN	1337
  PF-485	S. pneumoniae (A)	KNSMSRSIALID	1338
  PF-511	S. pneumoniae (H)	VMQ SLYVKPPLILVTKLAQQN	1339
  PF-512	S. pneumoniae (H)	SFMPEIQKNTIPTQMK	1340
  PF-513	S. pneumoniae (M)	SNGVGLGVGIGSGIRF-NH2	1341
  PF-514	S. epidermidis (C)	QRFYKLFYHIDLTNEQALKLFQVK	1342
  	E. coli (R)
  	S. pneumoniae (M)
  	E. faecalis (C)
  PF-515	S. pneumoniae (H)	DKSTQDKDIKQAKLLAQELGL-NH2	1343
  PF-516	S. pneumoniae (H)	ASKQASKQASKQASKQ	1344
  PF-517	S. pneumoniae (M)	VKPTMTASLISTVC	1345
  PF-518	S. epidermidis (C)	SFYSKYSRYIDNLAGAIFLFF	1346
  	E. coli (R)
  	MRSA (C)
  	S. pneumoniae (M)
  	E. faecalis (C)
  PF-519	E. coli (R)	YLVYSGVLATAAAF-NH2	1347
  	MRSA (C)
  	S. pneumoniae (S)
  	E. faecalis (C)
  PF-520	S. pneumoniae (M)	LGLTAGVAYAAQPTNQPTNQPTNQPT	1348
  		NQPTNQPTNQPRW-NH2
  PF-521	S. pneumoniae (H)	CGKLLEQKNFFLKTR	1349
  PF-522	S. pneumoniae (H)	FELVDWLETNLGKILKSKSA-NH2	1350
  PF-524	E. coli (M)	PDAPRTCYHKPILAALSRIVVTDR	1351
  	MRSA (C)
  	S. pneumoniae (M)
  	E. faecalis (C)
  PF-525	S. pneumoniae (H)	KFSDQIDKGQDALKDKLGDL	1352
  PF-526	S. epidermidis (C)	VLLLFIFQPFQKQLL-NH2	1353
  	E. coli (R)
  	C. albicans (C)
  	MRSA (C)
  	S. pneumoniae (R)
  PF-527	S. epidermidis (M)	GSVIKKRRKRMAKKKHRKLLKKTRIQ	1354
  	M. luteus (S)	RRRAGK
  	B. subtilis (I)
  	P. aeruginosa (I)
  	C. albicans (B)
  	MRSA (I)
  	S. pneumoniae (H)
  	C. jeikeium (I)
  	C. jejuni (M)
  PF-528	S. epidermidis (H)	LVDVVVLIRRHLPKSCS-NH2	1355
  	E. coli (H)
  	C. albicans (C)
  	MRSA (H)
  	S. pneumoniae (R)
  PF-529	S. pneumoniae (H)	LSEMERRRLRKRA-NH2	1356
  PF-530	S. epidermidis (H)	SKFKVLRKIIIKEYKGELMLSIQKQR	1357
  	E. coli (R)
  	MRSA (C)
  	S. pneumoniae (R)
  	E. faecalis (C)
  PF-531	S. epidermidis (I)	YIQFHLNQQPRPKVKKIKIFL-NH2	1358
  	E. coli (M)
  	P. aeruginosa (I)
  	S. pneumoniae (C)
  PF-532	E. coli (C)	KFIYKYKLSFIIYKILIQTLTMELNK	1359
  	MRSA (C)
  	S. pneumoniae (C)
  	E. faecalis (C)
  PF-533	S. epidermidis (H)	KTPNDKIHKTIIIKHIIL	1360
  	E. coli (R)
  	MRSA (H)
  	S. pneumoniae (C)
  	E. faecalis (C)
  PF-534	S. epidermidis (C)	KYFHLFYHNIIHYSKQHLSLKVDFKN-	1361
  	E. coli (R)	NH2
  	MRSA (C)
  	S. pneumoniae (R)
  	E. faecalis (C)
  PF-535	P. aeruginosa (H)	NIKTRKRALKIIKQHQRSK	1362
  	S. pneumoniae (H)
  PF-536	S. epidermidis (C)	MEPIPHIMIIANQIGIIIEKA	1363
  	E. coli (R)
  	P. aeruginosa (H)
  	MRSA (C)
  	S. pneumoniae (M)
  	E. faecalis (C)
  PF-537	S. pneumoniae (C)	LANDYYKKTKKSW	1364
  PF-538	S. pneumoniae (H)	KNKKQTDILEKVKEILDKKKKTKVG	1365
  		QKLY
  PF-539	MRSA (H)	SIITKKKRRKIPLSIDSQIYKYTFKQ	1366
  	S. pneumoniae (A)
  PF-540	S. epidermidis (H)	KSILILIKVIFIGQTTIIL	1367
  	E. coli (R)
  	MRSA (H)
  	S. pneumoniae (R)
  PF-541	E. coli (H)	RRNLNSPNIKTRKRALKIIKQHQRSK	1368
  	S. pneumoniae (H)
  PF-542	S. pneumoniae (H)	KKDNPSLNDQDKNAVLNLLALAK	1369
  PF-543	S. mutans (S)	NILFGIIGFVVAMTAAVIVTAISIAK	1370
  	S. epidermidis (D)
  	M. luteus (C)
  	E. coli (C)
  	MRSA (D)
  	S. pneumoniae (D)
  PF-544	S. epidermidis (D)	FGEKQMRSWWKVHWFHP	1371
  	MRSA (D)
  	S. pneumoniae (M)
  	E. faecalis (R)
  PF-545	B. subtilis (I)	RESKLIAMADMIRRRI-NH2	1372
  	C. albicans (B)
  	E. faecalis (H)
  	C. jeikeium (H)
  PF-546	S. epidermidis (D)	PIIAPTIKTQIQ	1373
  	E. coli (R)
  	MRSA (D)
  	S. pneumoniae (D)
  	E. faecalis (D)
  	C. jeikeium (D)
  PF-547	S. epidermidis (R)	WSRVPGHSDTGWKVWHRW-NH2	1374
  	B. subtilis (I)
  	MRSA (M)
  	E. faecalis (R)
  PF-548	S. epidermidis (M)	ARPIADLIHFNSTTVTASGDVYYGPG	1375
  	M. luteus (A)
  	B. subtilis (C)
  	MRSA (M)
  	S. pneumoniae (D)
  	C. jeikeium (R)
  	C. jejuni (D)
  PF-549	B. subtilis (D)	TGIGPIARPIEHGLDS	1376
  	MRSA (C)
  PF-550	B. subtilis (D)	STENGWQEFESYADVGVDPRRYVPL	1377
  PF-551	MRSA (C)	QVKEKRREIELQFRDAEKKLEASVQAE	1378
  PF-552	B. subtilis (D)	ELDKADAALGPAKNLAPLDVINRS	1379
  PF-553	B. subtilis (D)	LTIVGNALQQKNQKLLLNQKKITSLG	1380
  	MRSA (M)
  	S. pneumoniae (R)
  	C. jeikeium (R)
  PF-554	B. subtilis (D)	AKNFLTRTAEEIGEQAVREGNINGP	1381
  PF-555	MRSA (M)	EAYMRFLDREMEGLTAAYNVKLFTEA	1382
  	S. pneumoniae (R)	IS
  	C. jejuni (R)
  PF-556	S. epidermidis (A)	SLQIRMNTLTAAKASIEAA	1383
  	M. luteus (A)
  	B. subtilis (C)
  	MRSA (M)
  	S. pneumoniae (D)
  	E. faecalis (A)
  	C. jeikeium (D)
  	C. jejuni (R)
  PF-557	B. subtilis (D)	AANKAREQAAAEAKRKAEEQAR	1384
  PF-558	S. epidermidis (M)	ADAPPPLIVRYS	1385
  	B. subtilis (D)
  	MRSA (C)
  	S. pneumoniae (R)
  	C. jejuni (H)
  PF-559	B. subtilis (C)	SRPGKPGGVSIDVSRDRQDILSNYP	1386
  	C. jejuni (A)
  PF-560	B. subtilis (D)	FGNPFRGFTLAMEADFKKRK	1387
  	MRSA (C)
  	S. pneumoniae (R)
  	C. jejuni (A)
  PF-561	B. subtilis (D)	ESLEADVQAELDTEAAKYPALPASF	1388
  	MRSA (M)
  PF-562	S. epidermidis (A)	TPEQWLERSTVVVTGLLNRK	1389
  	M. luteus (R)
  	MRSA (M)
  	S. pneumoniae (D)
  	C. jejuni (R)
  PF-563	B. subtilis (D)	RPELDNELDVVQNSASLDKLQASYN	1390
  	S. pneumoniae (H)
  	C. jejuni (H)
  PF-564	B. subtilis (D)	TIILNDQINSLQERLNKLNAETDRR	1391
  	MRSA (C)
  	C. jeikeium (R)
  	C. jejuni (R)
  PF-565	B. subtilis (D)	RAEAEAQRQAEADAKRKAEEAARL	1392
  	MRSA (C)
  PF-566	M. luteus (D)	EAQQVTQQLGADFNAITTPTATKV	1393
  	B. subtilis (C)
  	MRSA (M)
  	S. pneumoniae (D)
  	C. jeikeium (C)
  	C. jejuni (D)
  PF-567	M. luteus (C)	QQRVKAVDASLSQVSTQVSGAVASA	1394
  	MRSA (D)
  	S. pneumoniae (D)
  	C. jeikeium (C)
  	C. jejuni (D)
  PF-569	B. subtilis (D)	KSKISEYTEKEFLEFVEDIYTNNK	1395
  PF-571	B. subtilis (D)	SDLLYYPNENREDSPAGVVKEVKE	1396
  PF-572	B. subtilis (D)	WRASKGLPGFKAG	1397
  	S. pneumoniae (R)
  PF-573	S. pneumoniae (C)	EKKLIVKLIDSIGKSHEEIVGAG	1398
  PF-574	B. subtilis (D)	LVKSGKLESPYEHSEHLTLSQEKGLE	1399
  PF-575	P. aeruginosa (A)	LNFRAENKILEKIHISLIDTVEGSA	1400
  	S. pneumoniae (A)
  	C. jeikeium (A)
  	C. jejuni (R)
  PF-576	S. epidermidis (A)	AYSGELPEPLVRKMSKEQVRSVMGK	1401
  	E. coli (A)
  	MRSA (R)
  	S. pneumoniae (C)
  	C. jejuni (C)
  PF-577	S. epidermidis (A)	PFETRESFRVPVIGILGGWDYFMHP	1402
  	E. coli (A)
  	P. aeruginosa (A)
  	MRSA (M)
  	S. pneumoniae (R)
  	E. faecalis (A)
  	C. jejuni (R)
  PF-578	S. mutans (D)	QKANLRIGFTYTSDSNVCNLTFALLGS	1403
  	S. epidermidis (D)	K
  	M. luteus (C)
  	P. mirabilis (C)
  	E. coli (C)
  	MRSA (C)
  	S. pneumoniae (D)
  PF-580	S. epidermidis (M)	EILNNNQVIKELTMKYKTQFESNLGG	1404
  	M. luteus (C)	WTARARR
  	MRSA (M)
  	S. pneumoniae (C)
  PF-581	MRSA (A)	WTARARR	1405
  	S. pneumoniae (A)
  	E. faecalis (A)
  	C. jejuni (A)
  PF-582	E. faecalis (A)	NLKTIEKECPFCNNKMDIKLKD	1406
  PF-583	S. mutans (F)	KFQGEFTNIGQSYIVSASHMSTSLNTG	1407
  	S. epidermidis (I)	K
  	MRSA (I)
  	S. pneumoniae (D)
  PF-584	S. epidermidis (C)	SYIKNLSNQKFLIAF	1408
  	E. coli (C)
  	MRSA (D)
  	S. pneumoniae (D)
  	E. faecalis (D)
  	C. jejuni (D)
  PF-585	S. epidermidis (S)	DYNHLLNVVQDWVNTN	1409
  	MRSA (S)
  	S. pneumoniae (R)
  	E. faecalis (A)
  	C. jejuni (R)
  PF-586	S. epidermidis (C)	FFNQANYFFKEF	1410
  	E. coli (C)
  	MRSA (D)
  	S. pneumoniae (D)
  	E. faecalis (D)
  	C. jejuni (D)
  PF-587	S. pneumoniae (C)	ASGKYQSYLLNVYVDSKKDRLDIFDK	1411
  		LKAKAKFVL
  PF-588	E. faecalis (A)	ESVEAIKAKAIK	1412
  PF-589	MRSA (M)	APLRIDEIRNSNVIDEVLDCAPKKQEHF	1413
  	S. pneumoniae (C)	FVVPKIIE
  PF-590	C. jejuni (R)	YYQAKLFPLL	1414
  PF-591	S. pneumoniae (R)	DLLKSLLGQDGAKNDEIIEFIKIIMEK	1415
  	E. faecalis (A)
  	C. jejuni (C)
  PF-592	S. epidermidis (M)	IMKNYKYFKLFIVKYALF	1416
  	E. coli (C)
  	MRSA (D)
  	S. pneumoniae (D)
  	E. faecalis (D)
  	C. jejuni (S)
  PF-593	E. faecalis (A)	MEISTLKKEKLHVKDELSQYLANYKK	1417
  PF-594	E. faecalis (C)	IVSAIV	1418
  PF-595	S. epidermidis (C)	LQNKIYELLYIKERSKLCS	1419
  	E. coli (C)
  	MRSA (D)
  	S. pneumoniae (R)
  	E. faecalis (D)
  	C. jejuni (D)
  PF-596	S. epidermidis (D)	SKMWDKILTILILILELIRELIKL	1420
  	E. coli (C)
  	MRSA (D)
  	S. pneumoniae (D)
  	E. faecalis (D)
  	C. jejuni (D)
  PF-597	E. faecalis (A)	DEIKVSDEEIEKFIKENNL	1421
  PF-598	S. epidermidis (R)	MKFMLEVRNKAISAYKEITRTQI	1422
  	E. coli (C)
  	MRSA (D)
  	S. pneumoniae (R)
  	E. faecalis (R)
  	C. jejuni (R)
  PF-599	S. epidermidis (M)	LFEIFKPKH	1423
  	MRSA (C)
  	S. pneumoniae (R)
  	E. faecalis (A)
  	C. jejuni (R)
  PF-600	S. mutans (S)	TKKIELKRFVDAFVKKSYENYILEREL	1424
  	S. epidermidis (C)	KKLIKAINEELPTK
  	M. luteus (C)
  	E. coli (H)
  	MRSA (M)
  	S. pneumoniae (R)
  PF-601	E. faecalis (A)	YRVTVKALE	1425
  	C. jejuni (A)
  PF-602	E. faecalis (A)	LEKEKKEYIEKLFKTK	1426
  PF-603	S. epidermidis (D)	IDKLKKMNLQKLSYEVRISQDGKSIYA	1427
  	M. luteus (A)	RIK
  	E. coli (M)
  	MRSA (M)
  	S. pneumoniae (C)
  PF-604	E. faecalis (A)	LMEQVEV	1428
  PF-605	S. epidermidis (R)	HYRWNTQWWKY	1429
  	E. coli (C)
  	P. aeruginosa (A)
  	C. albicans (B)
  	MRSA (C)
  	S. pneumoniae (D)
  	E. faecalis (R)
  	C. jejuni (R)
  PF-606	S. mutans (I)	FESKILNASKELDKEKKVNTALSFNSH	1430
  	S. epidermidis (I)	QDFAKAYQNGKI
  	C. albicans (B)
  	MRSA (I)
  	S. pneumoniae (H)
  PF-607	S. epidermidis (M)	YIESDPRKFDYIFGAIRDH	1431
  	MRSA (S)
  	S. pneumoniae (R)
  	E. faecalis (A)
  	C. jejuni (R)
  PF-609	MRSA (C)	TEIKLDNNEYLVLNLDDILGILK	1432
  	S. pneumoniae (R)
  	E. faecalis (A)
  	C. jejuni (R)
  PF-610	S. epidermidis (C)	VFLKLKTSKIDLASIIFYP	1433
  	E. coli (C)
  	MRSA (D)
  	S. pneumoniae (D)
  	E. faecalis (D)
  	C. jejuni (D)
  PF-612	S. mutans (F)	GTTLKYGLERQLKIDIHPEITIINLNGGA	1434
  	S. epidermidis (C)	DEFAKL
  	M. luteus (A)
  	P. mirabilis (C)
  	E. coli (C)
  	MRSA (C)
  	S. pneumoniae (C)
  PF-613	S. epidermidis (R)	ADEFAKL	1435
  	MRSA (C)
  	E. faecalis (A)
  PF-614	S. epidermidis (M)	GLDIYA	1436
  	S. pneumoniae (R)
  	E. faecalis (A)
  	C. jejuni (R)
  PF-615	S. epidermidis (D)	FLNRFIFYIFTVKTKSALIKNLFLD	1437
  	E. coli (C)
  	MRSA (D)
  	S. pneumoniae (D)
  	E. faecalis (D)
  	C. jejuni (D)
  PF-616	S. epidermidis (R)	IVFVVTKEKK	1438
  	E. faecalis (A)
  PF-617	C. albicans (H)	PMNAAEPE	1439
  	S. pneumoniae (I)
  	E. faecalis (H)
  PF-618	S. pneumoniae (I)	KLNTLNKKDNPSLNDQDKNAVLNLLA	1440
  	E. faecalis (H)	LAK
  PF-619	S. epidermidis (M)	WSRVPGHSDTGWKVWHRW	1441
  	E. coli (C)
  	MRSA (M)
  	S. pneumoniae (C)
  PF-621	S. pneumoniae (I)	PPSSFLV	1442
  	E. faecalis (H)
  PF-622	S. epidermidis (D)	TREDVFSVRLINNIVNKQA	1443
  	MRSA (D)
  	S. pneumoniae (M)
  	E. faecalis (D)
  	C. jeikeium (D)
  PF-623	S. epidermidis (M)	VLFAVYLGALDWLFSWLTQKM	1444
  	MRSA (D)
  	S. pneumoniae (D)
  	E. faecalis (D)
  	C. jeikeium (R)
  PF-624	S. mutans (D)	VFLLDSYCFVKINL	1445
  	S. epidermidis (D)
  	M. luteus (C)
  	P. mirabilis (C)
  	E. coli (C)
  	MRSA (C)
  	S. pneumoniae (D)
  PF-625	S. pneumoniae (H)	SDSTNNARTRKKARDVTTKDIDK	1446
  PF-626	S. pneumoniae (H)	KYDFDDFEPEEA	1447
  PF-627	S. epidermidis (H)	INDLLSYFTLHEK	1448
  	C. albicans (B)
  	MRSA (R)
  	S. pneumoniae (I)
  	E. faecalis (H)
  PF-629	S. epidermidis (C)	GLAAIATVFALY	1449
  	MRSA (D)
  	S. pneumoniae (M)
  	E. faecalis (R)
  	C. jeikeium (R)
  PF-630	MRSA (M)	IPATPIIHS	1450
  PF-631	S. pneumoniae (I)	LIIYFSKTGNTARATRQI	1451
  	E. faecalis (H)
  PF-632	S. epidermidis (D)	TTIQGVASLEKHGFRYTITYPTRI	1452
  	B. subtilis (H)
  	C. albicans (B)
  	MRSA (D)
  	S. pneumoniae (M)
  	E. faecalis (D)
  	C. jeikeium (D)
  PF-634	S. mutans (D)	MPKARPVNHNKKKSKITIKSNFTLFYM	1453
  	S. epidermidis (D)	FNP
  	M. luteus (C)
  	P. mirabilis (C)
  	E. coli (C)
  	MRSA (D)
  	S. pneumoniae (D)
  PF-635	S. epidermidis (M)	MNAHGHSLIFQKMIVHAFAFFSKQKN	1454
  	C. albicans (B)	YLYF
  	MRSA (D)
  	S. pneumoniae (D)
  	E. faecalis (D)
  	C. jeikeium (D)
  PF-636	B. subtilis (H)	LVRLA	1455
  	C. albicans (B)
  	S. pneumoniae (H)
  	E. faecalis (H)
  PF-637	S. epidermidis (M)	SRIKQDARSVRKYDRIGIFFYSFKSA	1456
  	MRSA (M)
  	S. pneumoniae (M)
  	E. faecalis (D)
  	C. jeikeium (D)
  PF-638	S. epidermidis (R)	TFILPK	1457
  	MRSA (M)
  	S. pneumoniae (I)
  	E. faecalis (H)
  PF-639	C. albicans (B)	QATQIKSWIDRLLVSED	1458
  	MRSA (R)
  	S. pneumoniae (I)
  	E. faecalis (H)
  PF-640	C. albicans (B)	MGDINRNF	1459
  	S. pneumoniae (I)
  	E. faecalis (H)
  PF-642	MRSA (M)	FTTPMIGIPAGLLGGSYYLKRREEKGK	1460
  PF-643	MRSA (C)	VRCRL	1461
  	S. pneumoniae (R)
  	E. faecalis (R)
  PF-644	S. pneumoniae (H)	TSGLIIGENGLNGL	1462
  PF-645	C. albicans (B)	SNSVQQG	1463
  	S. pneumoniae (I)
  PF-646	C. albicans (B)	APASPGRRPG	1464
  	S. pneumoniae (H)
  PF-647	C. albicans (B)	GTFLGQKCAAATAS	1465
  	S. pneumoniae (R)
  PF-649	E. faecalis (R)	CPRYPFVDVGPAGPWRARWRVGS	1466
  PF-651	S. pneumoniae (H)	PRWPTGAGRHR	1467
  PF-652	S. pneumoniae (A)	FLAPARPDLQAQRQALAQ	1468
  PF-653	S. pneumoniae (H)	QSVHPLPAETPVADVI	1469
  PF-654	C. albicans (B)	LSGRLAGRR	1470
  	MRSA (R)
  	S. pneumoniae (A)
  PF-655	S. epidermidis (R)	DAPCFDDQFGDLKCQMC	1471
  	B. subtilis (H)
  	MRSA (M)
  	S. pneumoniae (H)
  PF-656	MRSA (R)	RGMFVPFHDVDCVQ	1472
  PF-657	S. epidermidis (C)	YVANYTITQFGRDFDDRLAVAIHFA	1473
  	MRSA (D)
  	S. pneumoniae (H)
  	E. faecalis (D)
  	C. jeikeium (D)
  PF-658	MRSA (R)	PTTPPPTTPPEIPTGGTVIST	1474
  	S. pneumoniae (H)
  PF-659	S. epidermidis (M)	TVIST	1475
  	B. subtilis (H)
  	MRSA (R)
  	S. pneumoniae (C)
  PF-660	S. pneumoniae (H)	TDPQATAAPRRRTSPR	1476
  PF-661	MRSA (R)	PDEDIRRRAILPPAGPCRPMSPE	1477
  PF-662	S. pneumoniae (A)	GKQSRAHGPVASRREFRRKSG	1478
  PF-663	S. pneumoniae (A)	ATLIPRKA	1479
  PF-664	S. epidermidis (M)	DQLCVEYPARVSTG	1480
  	MRSA (R)
  	S. pneumoniae (M)
  	E. faecalis (R)
  PF-665	S. pneumoniae (H)	VLRVATAVGEVPTGL	1481
  PF-666	S. pneumoniae (A)	PNRRSRPR	1482
  PF-667	S. epidermidis (R)	PAHQRLRIDQRLVADRDMVQDYES	1483
  	MRSA (R)
  	S. pneumoniae (R)
  	E. faecalis (R)
  PF-668	S. epidermidis (M)	TNAESMALAFRGRVHMSVNIAGLT	1484
  	B. subtilis (A)
  	C. albicans (A)
  	MRSA (R)
  	S. pneumoniae (M)
  	E. faecalis (D)
  	C. jeikeium (D)
  PF-670	B. subtilis (H)	TVIVAPMHSGV	1485
  	S. pneumoniae (H)
  PF-672	S. epidermidis (I)	MRFGSLALVAYDSAIKHSWPRPSSVRR	1486
  	B. subtilis (I)	LRM
  	C. albicans (I)
  	MRSA (I)
  	S. pneumoniae (I)
  	E. faecalis (I)
  	C. jeikeium (R)
  PF-675	S. pneumoniae (C)	EIIPISPTRRCEMHTMSSAEYRGL	1487
  	E. faecalis (R)
  PF-677	S. epidermidis (R)	TCRGAGMH	1488
  	MRSA (D)
  	S. pneumoniae (D)
  	E. faecalis (R)
  PF-680	MRSA (R)	ADPHPTTGI	1489
  PF-681	S. epidermidis (M)	TALTTVGVSGARLITYCVGVEDI	1490
  	MRSA (M)
  	S. pneumoniae (M)
  	E. faecalis (R)
  	C. jeikeium (R)
  PF-682	S. pneumoniae (A)	RRGKSEQGLSRR	1491
  PF-683	S. epidermidis (R)	LWPVA	1492
  	MRSA (R)
  	S. pneumoniae (H)
  PF-684	C. albicans (B)	RKLSLASGFALWRRSLV	1493
  	S. pneumoniae (C)
  	E. faecalis (A)
  PF-685	S. epidermidis (M)	PTLWLACL	1494
  	MRSA (M)
  	S. pneumoniae (M)
  	E. faecalis (R)
  	C. jeikeium (R)
  PF-686	S. epidermidis (H)	LAVLMGYIGYRGWSGKRHINRQ	1495
  	B. subtilis (I)
  	C. albicans (B)
  	MRSA (M)
  	S. pneumoniae (A)
  	E. faecalis (R)
  PF-687	S. pneumoniae (A)	AKRVLSLAVAPHRRQPVQGT	1496
  PF-688	S. pneumoniae (A)	ARNHAVIPAG	1497
  PF-690	S. epidermidis (R)	MIPLAGDPVSSHRTVEFGVLGTYLVSG	1498
  	MRSA (R)	GSL
  	S. pneumoniae (M)
  	E. faecalis (R)
  PF-691	S. pneumoniae (R)	HRTVEFGVLGTYLVSGGSL	1499
  PF-692	MRSA (R)	GVAREDPLEPDPLAPIIDDSR	1500
  PF-693	S. pneumoniae (A)	PDPAR	1501
  PF-694	MRSA (R)	DLIRPLYSMSAPSVA	1502
  	S. pneumoniae (A)
  PF-695	MRSA (R)	ALSVMLGNIPLVVPNANQL	1503
  	S. pneumoniae (C)
  	E. faecalis (R)
  PF-696	S. pneumoniae (H)	IRSGISAAYARPLR	1504
  PF-697	C. albicans (H)	RADARAK	1505
  	S. pneumoniae (H)
  PF-698	C. albicans (H)	SSGRAGVKCRRPTGR	1506
  	S. pneumoniae (A)
  	E. faecalis (A)
  PF-699	S. pneumoniae (A)	GRAGVKCRRPTGR	1507
  PF-700	S. pneumoniae (C)	LNWPFTGR	1508
  PF-702	S. pneumoniae (H)	LSGRLAGRR	1509
  PF-704	S. pneumoniae (C)	APAARAAL	1510
  PF-737	S. pneumoniae (D)	KSSGSSASASSTAGGSSSK	1511
  PF-738	MRSA (M)	KSGATSAASGAKSGASS	1512
  PF-741	S. mutans (D)	AKREDTVAAQIGANILNLIQ	1513
  	S. epidermidis (C)
  	M. luteus (C)
  	P. mirabilis (C)
  	E. coli (C)
  	MRSA (C)
  	S. pneumoniae (D)
  PF-744	S. pneumoniae (H)	LGVGTFVGKVLIKNQQKQKSKKKAQ	1514
  PF-745	S. mutans (D)	ANSQNSLFSNRSSFKSIFDKKSNITTNA	1515
  	M. luteus (C)	TTPNSNIIIN
  	MRSA (C)
  	S. pneumoniae (C)
  PF-746	S. mutans (D)	FLGNSQYFTRK	1516
  	S. epidermidis (C)
  	M. luteus (C)
  	E. coli (C)
  	P. aeruginosa (A)
  	MRSA (C)
  	S. pneumoniae (C)
  PF-748	S. pneumoniae (H)	FQGFFDVAVNKWWEEHNKAKLWKN	1517
  		VKGKFLEGEGEEEDDE
  PF-749	S. pneumoniae (H)	GVNKWWEEHNKAKLWKNVKGKFLE	1518
  		GEGEEEDDE
  PF-752	S. pneumoniae (C)	LHVIRPRPELSELKFPITKILKVNKQGL	1519
  		KK
  PF-756	S. pneumoniae (A)	DALLRLA	1520
  PF-757	S. pneumoniae (H)	PQAISSVQQNA	1521
  PF-760	S. epidermidis (M)	DHITLDDYEIHDGFNFELYYG	1522
  	MRSA (M)
  	S. pneumoniae (C)
  PF-761	S. mutans (D)	SKFELVNYASGCSCGADCKCASETECK	1523
  	S. epidermidis (C)	CASKK
  	M. luteus (C)
  	E. coli (C)
  	P. aeruginosa (C)
  	MRSA (D)
  	S. pneumoniae (C)
  PF-762	S. pneumoniae (H)	PAPAPSAPAPAPEQPEQPA	1524
  PF-763	S. epidermidis (M)	GIWMARNYFHRSSIRKVYVESDKEYE	1525
  	M. luteus (C)	RVHPMQKIQYEGNYKSQ
  	MRSA (D)
  	S. pneumoniae (C)
  PF-764	MRSA (D)	GYFEPGKRD	1526
  	S. pneumoniae (H)
  PF-770	S. mutans (D)	GVGIGFIMMGVVGYAVKLVHIPIRYLI	1527
  	S. epidermidis (D)	V
  	M. luteus (C)
  	P. mirabilis (C)
  	E. coli (C)
  	MRSA (D)
  	S. pneumoniae (C)
  PF-776	S. mutans (D)	VSILLYLSATIILPNVLRLLVARAIIVRV	1528
  	S. epidermidis (D)
  	M. luteus (C)
  	E. coli (C)
  	MRSA (D)
  	S. pneumoniae (C)
  PF-C052	P. gingivalis (H)	SRFRNGV	1529
  PF-C055	F. nucleatum (T)	YNLSIYIYFLHTITIAGLITLPFII	1530
  	S. mutans (I)
  PF-C057	S. mutans (I)	YFWWYWVQDCIPYKNNEVWLELSNN	1531
  		MK
  PF-C058	S. mutans (F)	FETGFGDGYYMSLWGLNEKDEVCKV	1532
  		VIPFINPELID
  PF-C061	F. nucleatum (T)	TLNYKKMFFSVIFLLGLNYLICNSPLFF	1533
  	S. mutans (F)	KQIEF
  PF-C062	F. nucleatum (T)	PLARATEVVATLFIICSLLLYLTR	1534
  	S. mutans (I)
  PF-C064	F. nucleatum (T)	DEEALEMGANLYAQFAIDFLNSKK	1535
  PF-C065	F. nucleatum (T)	DEERYSDSYFLKEKVFYLILALFLILFH	1536
  		QKYLYFLEIITI
  PF-C069	F. nucleatum (T)	NALMLREMQLAKNIKVEVTDVLSNKK	1537
  		YC
  PF-C071	F. nucleatum (T)	QVIVKIL	1538
  PF-C072	F. nucleatum (T)	KKMFSLIRKVNWIFFILFIVLDLTNVFP	1539
  	P. gingivalis (T)	LIRTILFAILSRQ
  	S. mutans (F)
  PF-C075	F. nucleatum (T)	KALVISVFAIVFSIIFVKFFYWRDKK	1540
  	P. gingivalis (R)
  	S. mutans (F)
  PF-C084	F. nucleatum (T)	FFSVIFLFGLNYLICNSPLFNILR	1541
  	P. gingivalis (R)
  	S. mutans (F)
  PF-C085	S. mutans (F)	KKFKIFVIINWFYHKYIILNFEENF	1542
  PF-C086	F. nucleatum (T)	ELFFTILSDCNELFLLHLLQQPLFYIKK	1543
  		GK
  PF-C088	F. nucleatum (H)	DIANNILNSVSERLIIA	1544
  	P. gingivalis (R)
  	S. mutans (I)
  PF-C089	P. gingivalis (R)	MPKRHYYKLEAKALQFGLPFAYSPIQL	1545
  		LK
  PF-C091	F. nucleatum (T)	ASNTPRFVRLTLFNFYSKIWNVTHLFLF	1546
  		NNL
  PF-C095	F. nucleatum (T)	LLALNMNEDTYYFELFFIFDNQNKKW	1547
  		LIFDLKERG
  PF-C098	F. nucleatum (T)	PETKGKVSAFVFGIVVANVIAVVYILY	1548
  	S. mutans (F)	MLREIGIIQ
  PF-C120	F. nucleatum (T)	ASLSTMTFKVMELKELIILLCGLTMLMI	1549
  		QTEFV
  PF-C131	F. nucleatum (T)	QWIVAKREIRMHIYCHISVIHVIIFFG	1550
  	S. mutans (F)
  PF-C135	F. nucleatum (C)	KNTHAYLRVLRLSSLILSYQASVYPLF	1551
  	S. mutans (F)	AYLCQQKDY
  PF-C136	F. nucleatum (C)	LILSYQASVYPLFAYLCQQKDY	1552
  	P. gingivalis (R)
  PF-C 137	F. nucleatum (T)	QRMYWFKRGFETGDFSAGDTFAELK	1553
  PF-C 139	S. mutans (F)	LLASHPERLSLGVFFVYRVLHLLLENT	1554
  PF-C 142	S. mutans (I)	DFPPLSFFRRRFHAYTAPIDNFFGANPF	1555
  PF-C 143	F. nucleatum (C)	VVFGGGDRLV	1556
  PF-C 145	F. nucleatum (C)	YGKESDP	1557
  	S. mutans (I)
  PF-C180	P. gingivalis (R)	TVEELDKAFTWGAAAALAIGVIAINVG	1558
  	S. mutans (S)	LAAGYCYNNNDVF
  PF-C181	F. nucleatum (T)	KMRAGQVVFIYKLILVLLFYVLQKLFD	1559
  		LKKGCF
  PF-C194	F. nucleatum (T)	NTNDLLQAFELMGLGMAGVFIVLGILY	1560
  	P. gingivalis (T)	IVAELLIKIFPVNN
  	S. mutans (F)
  PF-C214	F. nucleatum (T)	GGHKQLVIEPLVSQ	1561
  PF-C281	S. mutans (F)	KKEKLLTAIRLQHRAEIRGYFTIFFLFFR	1562
  		I
  PF-C290	S. mutans (F)	GNVHPESDFHNLIQFIKTFLYFTIFFKYF	1563
  		L
  PF-C291	F. nucleatum (T)	HPFLTGTGCPLFLIFRLFFVKAYFSFTVF	1564
  	S. mutans (F)
  PF-C293	F. nucleatum (T)	IIIILPKIYLVCKTV	1565
  	P. gingivalis (R)
  	S. mutans (F)
  PF-S003	S. epidermidis (R)	ALALLKQDLLNFEGRGRIITSTYLQFNE	1566
  	M. luteus (R)	GCVP
  	B. subtilis (A)
  	P. aeruginosa (A)
  	C. albicans (A)
  	MRSA (M)
  	S. pneumoniae (D)
  	C. jeikeium (D)
  	C. jejuni (D)
  Key to Abbreviations: (A) Peptide aggregates; (B) Less hyphal formation; (C) Clumps; (D) Diffuse clumps and small polyps; (F) Diffuse growth; (H) Thin; (I) Growth inhibition; (M) Microcolony formation; (R) Rippled; (S) Small polyps; (T) Thick; (W) Halo formation on top, microlonies on bottom. These data thus indicate peptide-mediated interruption of bacterial biofilm formation processes, cellular metabolism, cellular import/export, nutrient acquisition, quorum sensing and communication, motility, chemotaxis, replication, translation, and/or transcription. Accordingly, without being bound to a particular theory, it is believed that the alteration of one or more of these basic pathways is important to pathogenesis, or the stopping thereof

• In certain embodiments, the amino acid sequence of the antimicrobial peptides comprises or consists of a single amino acid sequence, e.g., as listed above in Tables 4 and/or 5, and/or Table 15, and/or below in Table 14. In certain embodiments the amino acid sequence of the antimicrobial peptides comprises two copies, three copies, four copies, five copies six copies or more of one or more of the amino acid sequences listed in Tables 4, and/or 5, and/or Table 15, and/or Table 14. Thus, compound antimicrobial constructs are contemplated where the construct comprises multiple domains each having antimicrobial activity. The AMP domains comprising such a construct can be the same or different. In certain embodiments the construct comprises at least 2, at least 3, at least 4, at least 5, at least 6, at least 7, or at least 8 different AMP domains each domain comprising a different AMP sequence.
• Various AMP domains comprising such a construct can be joined directly to each other or two or more of such domains can be attached to each other via a linker. An illustrative, but non-limiting, list of suitable linkers is provided in Table 16. Thus, in certain embodiments, two or more AMP domains comprising a compound AMP construct are chemically conjugated together.
• In certain embodiments the two or more AMP domains comprising the AMP construct are joined by a peptide linker. Where all the AMP domains are attached directly to each other or are joined by peptide linkers, the entire construct can be provided as a single-chain peptide (fusion protein).
• In various embodiments, the antimicrobial peptides described herein comprise one or more of the amino acid sequences shown in Tables 4, and/or 5, and/or 15 and/or 14 (and/or the retro, inverso, retroinverso, etc. forms of such sequences). In certain embodiments the peptides range in length up to about 100 amino acids in length, preferably up to about 80, about 70, about 60, or about 51 amino acids in length. In certain embodiments the peptides range in length from about 8 amino acids up to about 100 amino acids 80 amino acids, 60 amino acids or about 51 amino acids in length. In certain embodiments the peptides range in length from about 8 up to about 50, 40, 30, 20, 15, 15, 13, or 12 amino acids in length.
• As shown in Tables 4, and/or 5, and/or 15 and/or 14, the various amino acid sequences described herein are effective against particular microorganisms. The range of activity of the peptides or compositions comprising such peptides can be increased by including amino acid sequences effective against different microorganisms either as separate components and/or as multiple domains within a single construct.

• TABLE 6
  Illustrative target microorganisms and peptides effective against that target.
  Gram Positive Bacteria:

  A. naeslundii	PF-531, PF-527, PF-672, PF-545, PF-168, PF-448, PF-525, PF-529, PF-
  	148
  B. subtilis	PF-002, PF-005, PF-006, PF-040, PF-053, PF-056, PF-061, PF-063, PF-
  	067, PF-068, PF-069, PF-070, PF-071, PF-145, PF-148, PF-171, PF-175,
  	PF-283, PF-289, PF-292, PF-296, PF-297, PF-301, PF-303, PF-305, PF-
  	306, PF-307, PF-318, PF-319, PF-322, PF-335, PF-339, PF-342, PF-497,
  	PF-499, PF-527, PF-531, PF-545, PF-547, PF-548, PF-549, PF-550, PF-
  	552, PF-553, PF-554, PF-556, PF-557, PF-558, PF-559, PF-560, PF-561,
  	PF-563, PF-564, PF-565, PF-566, PF-569, PF-571, PF-572, PF-574, PF-
  	632, PF-636, PF-655, PF-659, PF-668, PF-670, PF-672, PF-686, PF-998,
  	PF-2003
  C. difficile	PF-522, PF-531, PF-538
  C. jeikeium	PF-001, PF-003, PF-004, PF-101, PF-011, PF-012, PF-013, PF-021, PF-
  	022, PF-025, PF-028, PF-030, PF-032, PF-033, PF-036, PF-037, PF-040,
  	PF-042, PF-043, PF-046, PF-048, PF-052, PF-053, PF-056, PF-057, PF-
  	063, PF-065, PF-067, PF-068, PF-073, PF-075, PF-076, PF-099, PF-124,
  	PF-127, PF-129, PF-133, PF-135, PF-137, PF-139, PF-140, PF-145, PF-
  	148, PF-164, PF-173, PF-176, PF-186, PF-188, PF-190, PF-191, PF-196,
  	PF-199, PF-203, PF-204, PF-208, PF-527, PF-531, PF-545, PF-546, PF-
  	548, PF-553, PF-556, PF-564, PF-566, PF-567, PF-575, PF-622, PF-523,
  	PF-629, PF-632, PF-635, PF-637, PF-657, PF-668, PF-672, PF-681, PF-
  	685, PF-S003
  E. faecalis	PF-007, PF-053, PF-057, PF-068, PF-347, PF-349, PF-355, PF-356, PF-
  	363, PF-366, PF-369, PF-374, PF-375, PF-376, PF-379, PF-380, PF-381,
  	PF-386, PF-387, PF-389, PF-390, PF-392, PF-393, PF-394, PF-396, PF-
  	398, PF-399, PF-401, PF-407, PF-410, PF-411, PF-418, PF-422, PF-425,
  	PF-426, PF-427, PF-429, PF-431, PF-432, PF-439, PF-440, PF-444, PF-
  	447, PF-450, PF-451, PF-452, PF-454, PF-456, PF-460, PF-461, PF-469,
  	PF-470, PF-471, PF-472, PF-473, PF-474, PF-475, PF-480, PF-484, PF-
  	514, PF-518, PF-519, PF-524, PF-530, PF-532, PF-533, PF-534, PF-536,
  	PF-544, PF-545, PF-546, PF-547, PF-556, PF-577, PF-581, PF-582, PF-
  	584, PF-585, PF-586, PF-588, PF-591, PF-592, PF-593, PF-594, PF-595,
  	PF-596, PF-597, PF-598, PF-599, PF-601, PF-602, PF-604, PF-605, PF-
  	607, PF-609, PF-610, PF-613, PF-614, PF-615, PF-616, PF-617, PF-618,
  	PF-621, PF-622, PF-623, PF-627, PF-629, PF-631, PF-632, PF-635, PF-
  	636, PF-637, PF-638, PF-639, PF-640, PF-643, PF-649, PF-657, PF-664,
  	PF-667, PF-668, PF-672, PF-675, PF-677, PF-681, PF-684, PF-685, PF-
  	686, PF-690, PF-695, PF-698
  M. luteus	PF-001, PF-003, PF-004, PF-006, PF-007, PF-010, PF-012, PF-013, PF-
  	020, PF-021, PF-022, PF-025, PF-030, PF-036, PF-037, PF-040, PF-042,
  	PF-043, PF-051, PF-052, PF-053, PF-056, PF-057, PF-063, PF-067, PF-
  	068, PF-071, PF-073, PF-075, PF-076, PF-125, PF-127, PF-137, PF-139,
  	PF-140, PF-145, PF-148, PF-171, PF-175, PF-176, PF-199, PF-204, PF-
  	212, PF-215, PF-224, PF-226, PF-234, PF-235, PF-249, PF-250, PF-255,
  	PF-257, PF-264, PF-270, PF-271, PF-274, PF-276, PF-278, PF-357, PF-
  	527, PF-543, PF-548, PF-556, PF-562, PF-566, PF-567, PF-578, PF-580,
  	PF-600, PF-603, PF-612, PF-624, PF-634, PF-741, PF-745, PF-746, PF-
  	761, PF-763, PF-770, PF-776, PF-S003
  MRSA	PF-001, PF-003, PF-004, PF-006, PF-007, PF-010, PF-011, PF-012, PF-
  	013, PF-015, PF-017, PF-019, PF-020, PF-021, PF-022, PF-023, PF-024,
  	PF-025, PF-026, PF-027, PF-028, PF-029, PF-030, PF-031, PF-033, PF-
  	035, PF-036, PF-037, PF-040, PF-041, PF-042, PF-043, PF-045, PF-046,
  	PF-048, PF-049, PF-051, PF-052, PF-053, PF-056, PF-057, PF-058, PF-
  	063, PF-064, PF-065, PF-066, PF-067, PF-068, PF-071, PF-073, PF-074,
  	PF-075, PF-076, PF-140, PF-145, PF-148, PF-149, PF-156, PF-168, PF-
  	171, PF-178, PF-191, PF-209, PF-347, PF-349, PF-350, PF-354, PF-355,
  	PF-356, PF-357, PF-360, PF-362, PF-366, PF-369, PF-370, PF-373, PF-
  	374, PF-375, PF-376, PF-378, PF-379, PF-380, PF-381, PF-382, PF-386,
  	PF-387, PF-389, PF-390, PF-392, PF-393, PF-394, PF-395, PF-396, PF-
  	398, PF-399, PF-401, PF-403, PF-404, PF-405, PF-406, PF-407, PF-408,
  	PF-410, PF-411, PF-413, PF-417, PF-418, PF-422, PF-425, PF-426, PF-
  	427, PF-429, PF-430, PF-431, PF-432, PF-439, PF-440, PF-442, PF-443,
  	PF-444, PF-447, PF-450, PF-451, PF-452, PF-453, PF-454, PF-458, PF-
  	460, PF-461, PF-469, PF-471, PF-472, PF-473, PF-474, PF-475, PF-478,
  	PF-480, PF-518, PF-519, PF-524, PF-526, PF-527, PF-528, PF-530, PF-
  	532, PF-533, PF-534, PF-536, PF-539, PF-540, PF-543, PF-544, PF-545,
  	PF-546, PF-547, PF-548, PF-549, PF-551, PF-553, PF-555, PF-556, PF-
  	558, PF-560, PF-561, PF-562, PF-564, PF-565, PF-566, PF-567, PF-576,
  	PF-577, PF-578, PF-580, PF-581, PF-583, PF-584, PF-585, PF-586, PF-
  	589, PF-592, PF-595, PF-596, PF-598, PF-599, PF-600, PF-603, PF-605,
  	PF-606, PF-607, PF-609, PF-610, PF-612, PF-613, PF-615, PF-619, PF-
  	622, PF-623, PF-624, PF-627, PF-629, PF-630, PF-632, PF-634, PF-635,
  	PF-637, PF-638, PF-639, PF-652, PF-643, PF-654, PF-655, PF-656, PF-
  	657, PF-658, PF-659, PF-661, PF-664, PF-667, PF-778, PF-672, PF-677,
  	PF-680, PF-683, PF-685, PF-686, PF-690, PF-692, PF-694, PF-695, PF-
  	738, PF-741, PF-745, PF-746, PF-760, PF-761, PF-763, PF-764, PF-770,
  	PF-776, PF-S003
  S. epidermidis	PF-001, PF-003, PF-004, PF-006, PF-007, PF-009, PF-010, PF-012, PF-
  	013, PF-020, PF-021, PF-022, PF-024, PF-025, PF-027, PF-028, PF-030,
  	PF-032, PF-033, PF-034, PF-036, PF-037, PF-040, PF-041, PF-042, PF-
  	043, PF-046, PF-048, PF-051, PF-052, PF-953, PF-956, PF-957, PF-961,
  	PF-963, PF-964, PF-965, PF-967, PF-968, PF-971, PF-073, PF-074, PF-
  	075, PF-076, PF-099, PF-123, PF-124, PF-125, PF-127, PF-128, PF-129,
  	PF-137, PF-139, PF-140, PF-145, PF-148, PF-153, PF-157, PF-171, PF-
  	173, PF-176, PF-178, PF-180, PF-186, PF-190, PF-191, PF-192, PF-196,
  	PF-199, PF-203, PF-204, PF-208, PF-209, PF-226, PF-233, PF-273, PF-
  	278, PF-283, PF-290, PF-292, PF-293, PF-294, PF-296, PF-297, PF-301,
  	PF-307, PF-310, PF-313, PF-318, PF-319, PF-322, PF-335, PF-339, PF-
  	342, PF-347, PF-349, PF-350, PF-355, PF-356, PF-357, PF-360, PF-363,
  	PF-366, PF-369, PF-370, PF-373, PF-374, PF-375, PF-376, PF-378, PF-
  	379, PF-380, PF-381, PF-383, PF-386, PF-387, PF-389, PF-390, PF-393,
  	PF-395, PF-396, PF-397, PF-398, PF-399, PF-401, PF-403, PF-404, PF-
  	406, PF-407, PF-408, PF-410, PF-411, PF-413, PF-417, PF-418, PF-422,
  	PF-425, PF-246, PF-249, PF-430, PF-431, PF-432, PF-439, PF-440, PF-
  	444, PF-447, PF-451, PF-452, PF-453, PF-454, PF-460, PF-469, PF-471,
  	PF-473, PF-474, PF-475, PF-478, PF-480, PF-514, PF-518, PF-526, PF-
  	527, PF-528, PF-530, PF-531, PF-533, PF-534, PF-536, PF-540, PF-543,
  	PF-544, PF-546, PF-547, PF-548, PF-556, PF-558, PF-562, PF-576, PF-
  	577, PF-578, PF-580, PF-583, PF-584, PF-585, PF-586, PF-592, PF-595,
  	PF-596, PF-598, PF-599, PF-600, PF-603, PF-605, PF-606, PF-607, PF-
  	610, PF-612, PF-613, PF-614, PF-615, PF-616, PF-619, PF-622, PF-623,
  	PF-624, PF-627, PF-632, PF-634, PF-635, PF-637, PF-638, PF-655, PF-
  	657, PF-659, PF-664, PF-667, PF-778, PF-672, PF-677, PF-681, PF-683,
  	PF-685, PF-686, PF-690, PF-741, PF-746, PF-760, PF-761, PF-763, PF-
  	770, PF-776, PF-S003
  S. mutans	G-1, G-2, G-4, G-8, PF-020, PF-040, PF-051, PF-531, PF-543, PF-547,
  	PF-578, PF-583, PF-600, PF-606, PF-612, PF-624, PF-634, PF-741, PF-
  	745, PF-746, PF-761, PF-770, PF-776, PF-C055, PF-C057, PF-C058, PF-
  	C061, PF-C062, PF-C072, PF-C075, PF-C084, PF-C085, PF-C088, PF-
  	C098, PF-C131, PF-C135, PF-C139, PF-C142, PF-C146, PF-C180, PF-
  	C194, PF-C281, PF-C290, PF-C291, PF-C293
  S. pneumoniae	PF-002, PF-005, PF-006, PF-020, PF-033, PF-040, PF-051, PF-053, PF-
  	056, PF-057, PF-061, PF-063, PF-068, PF-071, PF-073, PF-140, PF-144,
  	PF-145, PF-148, PF-171, PF-175, PF-178, PF-220, PF-355, PF-356, PF-
  	357, PF-363, PF-366, PF-380, PF-389, PF-390, PF-393, PF-407, PF-411,
  	PF-414, PF-415, PF-416, PF-417, PF-418, PF-419, PF-421, PF-422, PF-
  	423, PF-424, PF-425, PF-426, PF-427, PF-428, PF-429, PF-430, PF-431,
  	PF-432, PF-433, PF-434, PF-437, PF-439, PF-440, PF-442, PF-443, PF-
  	444, PF-445, PF-446, PF-447, PF-448, PF-449, PF-450, PF-451, PF-452,
  	PF-453, PF-454, PF-455, PF-457, PF-458, PF-469, PF-460, PF-461, PF-
  	462, PF-464, PF-465, PF-466, PF-467, PF-468, PF-469, PF-471, PF-472,
  	PF-473, PF-474, PF-475, PF-476, PF-477, PF-478, PF-479, PF-480, PF-
  	482, PF-485, PF-511, PF-512, PF-513, PF-514, PF-515, PF-516, PF-517,
  	PF-518, PF-519, PF-520, PF-521, PF-522, PF-523, PF-524, PF-525, PF-
  	526, PF-527, PF-528, PF-529, PF-530, PF-531, PF-532, PF-533, PF-534,
  	PF-535, PF-536, PF-537, PF-538, PF-539, PF-540, PF-541, PF-542, PF-
  	543, PF-544, PF-546, PF-548, PF-553, PF-555, PF-556, PF-558, PF-560,
  	PF-562, PF-563, PF-566, PF-567, PF-572, PF-573, PF-575, PF-576, PF-
  	577, PF-578, PF-580, PF-581, PF-583, PF-585, PF-585, PF-586, PF-587,
  	PF-589, PF-591, PF-592, PF-595, PF-596, PF-598, PF-599, PF-600, PF-
  	603, PF-605, PF-606, PF-607, PF-609, PF-610, PF-612, PF-614, PF-615,
  	PF-617, PF-618, PF-619, PF-621, PF-622, PF-623, PF-624, PF-625, PF-
  	626, PF-627, PF-629, PF-631, PF-632, PF-634, PF-635, PF-636, PF-637,
  	PF-638, PF-639, PF-640, PF-643, PF-644, PF-645, PF-646, PF-647, PF-
  	651, PF-652, PF-653, PF-654, PF-655, PF-657, PF-658, PF-659, PF-660,
  	PF-662, PF-663, PF-664, PF-665, PF-666, PF-667, PF-668, PF-670, PF-
  	672, PF-675, PF-677, PF-681, PF-682, PF-683, PF-684, PF-685, PF-686,
  	PF-687, PF-688, PF-690, PF-691, PF-693, PF-694, PF-695, PF-696, PF-
  	697, PF-698, PF-699, PF-700, PF-702, PF-704, PF-737, PF-741, PF-744,
  	PF-745, PF-746, PF-748, PF-749, PF-752, PF-756, PF-757, PF-760, PF-
  	761, PF-762, PF-763, PF-764, PF-770, PF-776, PF-S003

  Gram Negative Bacteria:

  A. baumannii	PF-531, PF-006, PF-538, PF-530
  C. jejuni	PF-006, PF-008, PF-033, PF-040, PF-053, PF-056, PF-057, PF-059, PF-
  	061, PF-063, PF-067, PF-068, PF-069, PF-071, PF-073, PF-140, PF-145,
  	PF-148, PF-171, PF-175, PF-355, PF-356, PF-363, PF-366, PF-380, PF-
  	389, PF-390, PF-392, PF-393, PF-411, PF-418, PF-422, PF-425, PF-426,
  	PF-431, PF-432, PF-456, PF-469, PF-470, PF-471, PF-472, PF-473, PF-
  	474, PF-475, PF-527, PF-548, PF-555, PF-556, PF-558, PF-559, PF-560,
  	PF-562, PF-563, PF-564, PF-566, PF-567, PF-575, PF-576, PF-577, PF-
  	581, PF-584, PF-585, PF-586, PF-590, PF-591, PF-592, PF-595, PF-596,
  	PF-598, PF-599, PF-601, PF-605, PF-607, PF-609, PF-610, PF-614, PF-
  	615, PF-S003
  E. coli	PF-007, PF-040, PF-053, PF-057, PF-068, PF-178, PF-344, PF-347, PF-
  	349, PF-350, PF-355, PF-360, PF-362, PF-363, PF-366, PF-369, PF-370,
  	PF-374, PF-375, PF-376, PF-379, PF-380, PF-381, PF-383, PF-385, PF-
  	386, PF-387, PF-390, PF-395, PF-396, PF-398, PF-399, PF-401, PF-403,
  	PF-410, PF-411, PF-413, PF-418, PF-425, PF-426, PF-427, PF-432, PF-
  	439, PF-440, PF-443, PF-444, PF-451, PF-452, PF-453, PF-454, PF-460,
  	PF-469, PF-471, PF-473, PF-474, PF-478, PF-480, PF-514, PF-518, PF-
  	519, PF-524, PF-526, PF-528, PF-530, PF-531, PF-532, PF-533, PF-534,
  	PF-536, PF-540, PF-541, PF-543, PF-546, PF-576, PF-577, PF-578, PF-
  	584, PF-586, PF-592, PF-595, PF-596, PF-598, PF-600, PF-603, PF-605,
  	PF-606, PF-610, PF-612, PF-615, PF-619, PF-624, PF-634, PF-741, PF-
  	746, PF-761, PF-770, PF-776
  F. nucleatum	PF-C055, PF-C061, PF-C062, PF-C064, PF-C065, PF-C069, PF-C071,
  	PF-C072, PF-C075, PF-C084, PF-C086, PF-C088, PF-C091, PF-C095,
  	PF-C098, PF-C120, PF-C131, PF-C135, PF-C136, PF-C137, PF-C143,
  	PF-C145, PF-C181, PF-C194, PF-C214, PF-C291, PF-C293
  M. xanthus	G-5, G-6, G-7
  P. aeruginosa	PF-053, PF-063, PF-067, PF-128, PF-140, PF-143, PF-168, PF-204, PF-
  	209, PF-355, PF-356, PF-366, PF-380, PF-411, PF-425, PF-432, PF-454,
  	PF-458, PF-471, PF-474, PF-527, PF-531, PF-535, PF-536, PF-575, PF-
  	577, PF-605, PF-746, PF-761, PF-S003
  P. gingivalis	PF-C052, PF-C072, PF-C075, PF-C084, PF-C088, PF-C089, PF-C136,
  	PF-C180, PF-C194, C293
  P. mirabilis	PF-040, PF-578, PF-612, PF-624, PF-634, PF-741, PF-770

  Yeast Fungi:

  A. niger	PF-531, PF-527, PF-672, PF-545, PF-168, PF-448, PF-525, PF-529, PF-
  	148
  C. albicans	PF-053, PF-056, PF-057, PF-071, PF-140, PF-148, PF-175, PF-278, PF-
  	307, PF-425, PF-426, PF-474, PF-475, PF-526, PF-527, PF-528, PF-545,
  	PF-605, PF-606, PF-617, PF-627, PF-632, PF-635, PF-636, PF-639, PF-
  	640, PF-645, PF-646, PF-647, PF-654, PF-668, PF-672, PF-684, PF-686,
  	PF-697, PF-698, PF-S003
  T. rubrum	PF-283, PF-307, PF-527, PF-531, PF-547, PF-672

• In certain embodiments the activity against a particular microorganism or group of microorganisms can be increased by increasing the number of peptides or peptide domains with activity against that microorganism or group of microorganisms.
• Thus, for example, in certain embodiments, a peptide or composition effective to kill or inhibit the growth and/or proliferation of a yeast or fungus can comprise or more peptides and/or one or more peptide domains having sequences selected from the sequences shown in Tables 4, 5, or 6 (e.g., PF-S003, PF-053, PF-056, PF-057, PF-071, PF-140, PF-148, PF-168, PF-175, PF-278, PF-283, PF-307, PF-425, PF-426, PF-448, PF-474, PF-475, PF-525, PF-526, PF-527, PF-528, PF-529, PF-531, PF-545, PF-547, PF-606, PF-617, PF-627, PF-632, PF-635, PF-636, PF-639, PF-640, PF-645, PF-646, PF-647, PF-654, PF-668, PF-672, PF-684, PF-686, PF-697, and PF-69)8. A peptide or composition effective to kill or inhibit the growth and/or proliferation of Aspergillus niger can comprise one or more peptides and/or one or more peptide domains having sequences selected from the group consisting of PF-531, PF-527, PF-672, PF-545, PF-168, PF-448, PF-525, PF-529, and PF-148. A peptide or composition effective to kill or inhibit the growth and/or proliferation of Candida albicans can comprise one or more peptides and/or one or more peptide domains having sequences selected from the group consisting of PF-053, PF-056, PF-057, PF-071, PF-140, PF-148, PF-175, PF-278, PF-307, PF-425, PF-426, PF-474, PF-475, PF-526, PF-527, PF-528, PF-545, PF-605, PF-606, PF-617, PF-627, PF-632, PF-635, PF-636, PF-639, PF-640, PF-645, PF-646, PF-647, PF-654, PF-668, PF-672, PF-684, PF-686, PF-697, PF-698, and PF-S003. A peptide or composition effective to kill or inhibit the growth and/or proliferation of Trichophyton rubrum can comprise one or more peptides and/or one or more peptide domains having sequences selected from the group consisting of PF-283, PF-307, PF-527, PF-531, PF-547, and PF-672.
• In certain embodiments a peptide or composition effective to kill or inhibit the growth and/or proliferation of a bacterium can comprise one or more peptides and/or one or more peptide domains comprising or consisting of sequences identified as having activity against a bacterium in Tables 4, 5, or 6.
• In certain embodiments a peptide or composition effective to kill or inhibit the growth and/or proliferation of a gram positive bacterium can comprise one or more peptides and/or one or more peptide domains comprising or consisting of sequences identified as having activity against a gram positive bacterium in Tables 4, 5, or 6. In certain embodiments a peptide or composition effective to kill or inhibit the growth and/or proliferation of a gram negative bacterium can comprise one or more peptides and/or one or more peptide domains comprising or consisting of sequences identified as having activity against a gram negative bacterium in Tables 4, 5, or 6.
• In certain embodiments a peptide or composition effective to kill or inhibit the growth and/or proliferation of A. naeslundii can comprise one or more peptides and/or one or more peptide domains comprising or consisting of sequences identified as having activity against A. Naeslundii in Tables 4, 5, or 6 (e.g., from the group consisting of PF-531, PF-527, PF-672, PF-545, PF-168, PF-448, PF-525, PF-529, and PF-148).
• In certain embodiments a peptide or composition effective to kill or inhibit the growth and/or proliferation of B. subtilis can comprise one or more peptides and/or one or more peptide domains comprising or consisting of sequences identified as having activity against B. subtilis in Tables 4, 5, or 6 (e.g., from the group consisting of PF-002, PF-005, PF-006, PF-040, PF-053, PF-056, PF-061, PF-063, PF-067, PF-068, PF-069, PF-070, PF-071, PF-145, PF-148, PF-171, PF-175, PF-283, PF-289, PF-292, PF-296, PF-297, PF-301, PF-303, PF-305, PF-306, PF-307, PF-318, PF-319, PF-322, PF-335, PF-339, PF-342, PF-497, PF-499, PF-527, PF-531, PF-545, PF-547, PF-548, PF-549, PF-550, PF-552, PF-553, PF-554, PF-556, PF-557, PF-558, PF-559, PF-560, PF-561, PF-563, PF-564, PF-565, PF-566, PF-569, PF-571, PF-572, PF-574, PF-632, PF-636, PF-655, PF-659, PF-668, PF-670, PF-672, PF-686, PF-998, and PF-2003).
• In certain embodiments a peptide or composition effective to kill or inhibit the growth and/or proliferation of C. difficile can comprise one or more peptides and/or one or more peptide domains comprising or consisting of sequences identified as having activity against C. difficile in Tables 4, 5, or 6 (e.g., from the group consisting of PF-522, PF-531, and PF-538).
• In certain embodiments a peptide or composition effective to kill or inhibit the growth and/or proliferation of C. jeikeium can comprise one or more peptides and/or one or more peptide domains comprising or consisting of sequences identified as having activity against C. jeikeium in Tables 4, 5, or 6 (e.g., from the group consisting of PF-001, PF-003, PF-004, PF-101, PF-011, PF-012, PF-013, PF-021, PF-022, PF-025, PF-028, PF-030, PF-032, PF-033, PF-036, PF-037, PF-040, PF-042, PF-043, PF-046, PF-048, PF-052, PF-053, PF-056, PF-057, PF-063, PF-065, PF-067, PF-068, PF-073, PF-075, PF-076, PF-099, PF-124, PF-127, PF-129, PF-133, PF-135, PF-137, PF-139, PF-140, PF-145, PF-148, PF-164, PF-173, PF-176, PF-186, PF-188, PF-190, PF-191, PF-196, PF-199, PF-203, PF-204, PF-208, PF-527, PF-531, PF-545, PF-546, PF-548, PF-553, PF-556, PF-564, PF-566, PF-567, PF-575, PF-622, PF-523, PF-629, PF-632, PF-635, PF-637, PF-657, PF-668, PF-672, PF-681, PF-685, and PF-S003).
• In certain embodiments a peptide or composition effective to kill or inhibit the growth and/or proliferation of E. faecalis can comprise one or more peptides and/or one or more peptide domains comprising or consisting of sequences identified as having activity against E. faecalis in Tables 4, 5, or 6 (e.g., from the group consisting of PF-007, PF-053, PF-057, PF-068, PF-347, PF-349, PF-355, PF-356, PF-363, PF-366, PF-369, PF-374, PF-375, PF-376, PF-379, PF-380, PF-381, PF-386, PF-387, PF-389, PF-390, PF-392, PF-393, PF-394, PF-396, PF-398, PF-399, PF-401, PF-407, PF-410, PF-411, PF-418, PF-422, PF-425, PF-426, PF-427, PF-429, PF-431, PF-432, PF-439, PF-440, PF-444, PF-447, PF-450, PF-451, PF-452, PF-454, PF-456, PF-460, PF-461, PF-469, PF-470, PF-471, PF-472, PF-473, PF-474, PF-475, PF-480, PF-484, PF-514, PF-518, PF-519, PF-524, PF-530, PF-532, PF-533, PF-534, PF-536, PF-544, PF-545, PF-546, PF-547, PF-556, PF-577, PF-581, PF-582, PF-584, PF-585, PF-586, PF-588, PF-591, PF-592, PF-593, PF-594, PF-595, PF-596, PF-597, PF-598, PF-599, PF-601, PF-602, PF-604, PF-605, PF-607, PF-609, PF-610, PF-613, PF-614, PF-615, PF-616, PF-617, PF-618, PF-621, PF-622, PF-623, PF-627, PF-629, PF-631, PF-632, PF-635, PF-636, PF-637, PF-638, PF-639, PF-640, PF-643, PF-649, PF-657, PF-664, PF-667, PF-668, PF-672, PF-675, PF-677, PF-681, PF-684, PF-685, PF-686, PF-690, PF-695, and PF-698).
• In certain embodiments a peptide or composition effective to kill or inhibit the growth and/or proliferation of M. luteus can comprise one or more peptides and/or one or more peptide domains comprising or consisting of sequences identified as having activity against M. luteus in Tables 4, 5, or 6 (e.g., from the group consisting of PF-001, PF-003, PF-004, PF-006, PF-007, PF-010, PF-012, PF-013, PF-020, PF-021, PF-022, PF-025, PF-030, PF-036, PF-037, PF-040, PF-042, PF-043, PF-051, PF-052, PF-053, PF-056, PF-057, PF-063, PF-067, PF-068, PF-071, PF-073, PF-075, PF-076, PF-125, PF-127, PF-137, PF-139, PF-140, PF-145, PF-148, PF-171, PF-175, PF-176, PF-199, PF-204, PF-212, PF-215, PF-224, PF-226, PF-234, PF-235, PF-249, PF-250, PF-255, PF-257, PF-264, PF-270, PF-271, PF-274, PF-276, PF-278, PF-357, PF-527, PF-543, PF-548, PF-556, PF-562, PF-566, PF-567, PF-578, PF-580, PF-600, PF-603, PF-612, PF-624, PF-634, PF-741, PF-745, PF-746, PF-761, PF-763, PF-770, PF-776, and PF-S003).
• In certain embodiments a peptide or composition effective to kill or inhibit the growth and/or proliferation of MRSA can comprise one or more peptides and/or one or more peptide domains comprising or consisting of sequences identified as having activity against MRSA in Tables 4, 5, or 6 (e.g., from the group consisting of PF-001, PF-003, PF-004, PF-006, PF-007, PF-010, PF-011, PF-012, PF-013, PF-015, PF-017, PF-019, PF-020, PF-021, PF-022, PF-023, PF-024, PF-025, PF-026, PF-027, PF-028, PF-029, PF-030, PF-031, PF-033, PF-035, PF-036, PF-037, PF-040, PF-041, PF-042, PF-043, PF-045, PF-046, PF-048, PF-049, PF-051, PF-052, PF-053, PF-056, PF-057, PF-058, PF-063, PF-064, PF-065, PF-066, PF-067, PF-068, PF-071, PF-073, PF-074, PF-075, PF-076, PF-140, PF-145, PF-148, PF-149, PF-156, PF-168, PF-171, PF-178, PF-191, PF-209, PF-347, PF-349, PF-350, PF-354, PF-355, PF-356, PF-357, PF-360, PF-362, PF-366, PF-369, PF-370, PF-373, PF-374, PF-375, PF-376, PF-378, PF-379, PF-380, PF-381, PF-382, PF-386, PF-387, PF-389, PF-390, PF-392, PF-393, PF-394, PF-395, PF-396, PF-398, PF-399, PF-401, PF-403, PF-404, PF-405, PF-406, PF-407, PF-408, PF-410, PF-411, PF-413, PF-417, PF-418, PF-422, PF-425, PF-426, PF-427, PF-429, PF-430, PF-431, PF-432, PF-439, PF-440, PF-442, PF-443, PF-444, PF-447, PF-450, PF-451, PF-452, PF-453, PF-454, PF-458, PF-460, PF-461, PF-469, PF-471, PF-472, PF-473, PF-474, PF-475, PF-478, PF-480, PF-518, PF-519, PF-524, PF-526, PF-527, PF-528, PF-530, PF-532, PF-533, PF-534, PF-536, PF-539, PF-540, PF-543, PF-544, PF-545, PF-546, PF-547, PF-548, PF-549, PF-551, PF-553, PF-555, PF-556, PF-558, PF-560, PF-561, PF-562, PF-564, PF-565, PF-566, PF-567, PF-576, PF-577, PF-578, PF-580, PF-581, PF-583, PF-584, PF-585, PF-586, PF-589, PF-592, PF-595, PF-596, PF-598, PF-599, PF-600, PF-603, PF-605, PF-606, PF-607, PF-609, PF-610, PF-612, PF-613, PF-615, PF-619, PF-622, PF-623, PF-624, PF-627, PF-629, PF-630, PF-632, PF-634, PF-635, PF-637, PF-638, PF-639, PF-652, PF-643, PF-654, PF-655, PF-656, PF-657, PF-658, PF-659, PF-661, PF-664, PF-667, PF-778, PF-672, PF-677, PF-680, PF-683, PF-685, PF-686, PF-690, PF-692, PF-694, PF-695, PF-738, PF-741, PF-745, PF-746, PF-760, PF-761, PF-763, PF-764, PF-770, PF-776, and PF-5003).
• In certain embodiments a peptide or composition effective to kill or inhibit the growth and/or proliferation of S. epidermidis can comprise one or more peptides and/or one or more peptide domains comprising or consisting of sequences identified as having activity against of S. epidermidis in Tables 4, 5, or 6 (e.g., from the group consisting of PF-001, PF-003, PF-004, PF-006, PF-007, PF-009, PF-010, PF-012, PF-013, PF-020, PF-021, PF-022, PF-024, PF-025, PF-027, PF-028, PF-030, PF-032, PF-033, PF-034, PF-036, PF-037, PF-040, PF-041, PF-042, PF-043, PF-046, PF-048, PF-051, PF-052, PF-953, PF-956, PF-957, PF-961, PF-963, PF-964, PF-965, PF-967, PF-968, PF-971, PF-073, PF-074, PF-075, PF-076, PF-099, PF-123, PF-124, PF-125, PF-127, PF-128, PF-129, PF-137, PF-139, PF-140, PF-145, PF-148, PF-153, PF-157, PF-171, PF-173, PF-176, PF-178, PF-180, PF-186, PF-190, PF-191, PF-192, PF-196, PF-199, PF-203, PF-204, PF-208, PF-209, PF-226, PF-233, PF-273, PF-278, PF-283, PF-290, PF-292, PF-293, PF-294, PF-296, PF-297, PF-301, PF-307, PF-310, PF-313, PF-318, PF-319, PF-322, PF-335, PF-339, PF-342, PF-347, PF-349, PF-350, PF-355, PF-356, PF-357, PF-360, PF-363, PF-366, PF-369, PF-370, PF-373, PF-374, PF-375, PF-376, PF-378, PF-379, PF-380, PF-381, PF-383, PF-386, PF-387, PF-389, PF-390, PF-393, PF-395, PF-396, PF-397, PF-398, PF-399, PF-401, PF-403, PF-404, PF-406, PF-407, PF-408, PF-410, PF-411, PF-413, PF-417, PF-418, PF-422, PF-425, PF-246, PF-249, PF-430, PF-431, PF-432, PF-439, PF-440, PF-444, PF-447, PF-451, PF-452, PF-453, PF-454, PF-460, PF-469, PF-471, PF-473, PF-474, PF-475, PF-478, PF-480, PF-514, PF-518, PF-526, PF-527, PF-528, PF-530, PF-531, PF-533, PF-534, PF-536, PF-540, PF-543, PF-544, PF-546, PF-547, PF-548, PF-556, PF-558, PF-562, PF-576, PF-577, PF-578, PF-580, PF-583, PF-584, PF-585, PF-586, PF-592, PF-595, PF-596, PF-598, PF-599, PF-600, PF-603, PF-605, PF-606, PF-607, PF-610, PF-612, PF-613, PF-614, PF-615, PF-616, PF-619, PF-622, PF-623, PF-624, PF-627, PF-632, PF-634, PF-635, PF-637, PF-638, PF-655, PF-657, PF-659, PF-664, PF-667, PF-778, PF-672, PF-677, PF-681, PF-683, PF-685, PF-686, PF-690, PF-741, PF-746, PF-760, PF-761, PF-763, PF-770, PF-776, and PF-S003).
• In certain embodiments a peptide or composition effective to kill or inhibit the growth and/or proliferation of S. mutans can comprise one or more peptides and/or one or more peptide domains comprising or consisting of sequences identified as having activity against S. mutans in Tables 4, 5, or 6 (e.g., from the group consisting of G-1, G-2, G-4, G-8, PF-020, PF-040, PF-051, PF-531, PF-543, PF-547, PF-578, PF-583, PF-600, PF-606, PF-612, PF-624, PF-634, PF-741, PF-745, PF-746, PF-761, PF-770, PF-776, PF-0055, PF-0057, PF-0058, PF-0061, PF-0062, PF-0072, PF-0075, PF-0084, PF-0085, PF-0088, PF-0098, PF-C131, PF-C135, PF-C139, PF-C142, PF-C146, PF-C180, PF-C194, PF-C281, PF-C290, PF-C291, PF-C293
• In certain embodiments a peptide or composition effective to kill or inhibit the growth and/or proliferation of S. pneumoniae can comprise one or more peptides and/or one or more peptide domains comprising or consisting of sequences identified as having activity against S. pneumoniae in Tables 4, 5, or 6 (e.g., from the group consisting of PF-002, PF-005, PF-006, PF-020, PF-033, PF-040, PF-051, PF-053, PF-056, PF-057, PF-061, PF-063, PF-068, PF-071, PF-073, PF-140, PF-144, PF-145, PF-148, PF-171, PF-175, PF-178, PF-220, PF-355, PF-356, PF-357, PF-363, PF-366, PF-380, PF-389, PF-390, PF-393, PF-407, PF-411, PF-414, PF-415, PF-416, PF-417, PF-418, PF-419, PF-421, PF-422, PF-423, PF-424, PF-425, PF-426, PF-427, PF-428, PF-429, PF-430, PF-431, PF-432, PF-433, PF-434, PF-437, PF-439, PF-440, PF-442, PF-443, PF-444, PF-445, PF-446, PF-447, PF-448, PF-449, PF-450, PF-451, PF-452, PF-453, PF-454, PF-455, PF-457, PF-458, PF-469, PF-460, PF-461, PF-462, PF-464, PF-465, PF-466, PF-467, PF-468, PF-469, PF-471, PF-472, PF-473, PF-474, PF-475, PF-476, PF-477, PF-478, PF-479, PF-480, PF-482, PF-485, PF-511, PF-512, PF-513, PF-514, PF-515, PF-516, PF-517, PF-518, PF-519, PF-520, PF-521, PF-522, PF-523, PF-524, PF-525, PF-526, PF-527, PF-528, PF-529, PF-530, PF-531, PF-532, PF-533, PF-534, PF-535, PF-536, PF-537, PF-538, PF-539, PF-540, PF-541, PF-542, PF-543, PF-544, PF-546, PF-548, PF-553, PF-555, PF-556, PF-558, PF-560, PF-562, PF-563, PF-566, PF-567, PF-572, PF-573, PF-575, PF-576, PF-577, PF-578, PF-580, PF-581, PF-583, PF-585, PF-585, PF-586, PF-587, PF-589, PF-591, PF-592, PF-595, PF-596, PF-598, PF-599, PF-600, PF-603, PF-605, PF-606, PF-607, PF-609, PF-610, PF-612, PF-614, PF-615, PF-617, PF-618, PF-619, PF-621, PF-622, PF-623, PF-624, PF-625, PF-626, PF-627, PF-629, PF-631, PF-632, PF-634, PF-635, PF-636, PF-637, PF-638, PF-639, PF-640, PF-643, PF-644, PF-645, PF-646, PF-647, PF-651, PF-652, PF-653, PF-654, PF-655, PF-657, PF-658, PF-659, PF-660, PF-662, PF-663, PF-664, PF-665, PF-666, PF-667, PF-668, PF-670, PF-672, PF-675, PF-677, PF-681, PF-682, PF-683, PF-684, PF-685, PF-686, PF-687, PF-688, PF-690, PF-691, PF-693, PF-694, PF-695, PF-696, PF-697, PF-698, PF-699, PF-700, PF-702, PF-704, PF-737, PF-741, PF-744, PF-745, PF-746, PF-748, PF-749, PF-752, PF-756, PF-757, PF-760, PF-761, PF-762, PF-763, PF-764, PF-770, PF-776, and PF-S003).
• In certain embodiments a peptide or composition effective to kill or inhibit the growth and/or proliferation of A. baumannii can comprise one or more peptides and/or one or more peptide domains comprising or consisting of sequences identified as having activity against A. baumannii in Tables 4, 5, or 6 (e.g., from the group consisting of PF-531, PF-006, PF-538, and PF-530).
• In certain embodiments a peptide or composition effective to kill or inhibit the growth and/or proliferation of C. jejuni can comprise one or more peptides and/or one or more peptide domains comprising or consisting of sequences identified as having activity against C. jejuni in Tables 4, 5, or 6 (e.g., from the group consisting of PF-006, PF-008, PF-033, PF-040, PF-053, PF-056, PF-057, PF-059, PF-061, PF-063, PF-067, PF-068, PF-069, PF-071, PF-073, PF-140, PF-145, PF-148, PF-171, PF-175, PF-355, PF-356, PF-363, PF-366, PF-380, PF-389, PF-390, PF-392, PF-393, PF-411, PF-418, PF-422, PF-425, PF-426, PF-431, PF-432, PF-456, PF-469, PF-470, PF-471, PF-472, PF-473, PF-474, PF-475, PF-527, PF-548, PF-555, PF-556, PF-558, PF-559, PF-560, PF-562, PF-563, PF-564, PF-566, PF-567, PF-575, PF-576, PF-577, PF-581, PF-584, PF-585, PF-586, PF-590, PF-591, PF-592, PF-595, PF-596, PF-598, PF-599, PF-601, PF-605, PF-607, PF-609, PF-610, PF-614, PF-615, and PF-S003).
• In certain embodiments a peptide or composition effective to kill or inhibit the growth and/or proliferation of E. coli can comprise one or more peptides and/or one or more peptide domains comprising or consisting of sequences identified as having activity against E. coli in Tables 4, 5, or 6 (e.g., from the group consisting of PF-007, PF-040, PF-053, PF-057, PF-068, PF-178, PF-344, PF-347, PF-349, PF-350, PF-355, PF-360, PF-362, PF-363, PF-366, PF-369, PF-370, PF-374, PF-375, PF-376, PF-379, PF-380, PF-381, PF-383, PF-385, PF-386, PF-387, PF-390, PF-395, PF-396, PF-398, PF-399, PF-401, PF-403, PF-410, PF-411, PF-413, PF-418, PF-425, PF-426, PF-427, PF-432, PF-439, PF-440, PF-443, PF-444, PF-451, PF-452, PF-453, PF-454, PF-460, PF-469, PF-471, PF-473, PF-474, PF-478, PF-480, PF-514, PF-518, PF-519, PF-524, PF-526, PF-528, PF-530, PF-531, PF-532, PF-533, PF-534, PF-536, PF-540, PF-541, PF-543, PF-546, PF-576, PF-577, PF-578, PF-584, PF-586, PF-592, PF-595, PF-596, PF-598, PF-600, PF-603, PF-605, PF-606, PF-610, PF-612, PF-615, PF-619, PF-624, PF-634, PF-741, PF-746, PF-761, PF-770, and PF-776).
• In certain embodiments a peptide or composition effective to kill or inhibit the growth and/or proliferation of F. nucleatum can comprise one or more peptides and/or one or more peptide domains comprising or consisting of sequences identified as having activity against F. nucleatum in Tables 4, 5, or 6 (e.g., from the group consisting of PF-0055, PF-0061, PF-0062, PF-0064, PF-0065, PF-0069, PF-0071, PF-0072, PF-0075, PF-C084, PF-0086, PF-0088, PF-0091, PF-0095, PF-0098, PF-C120, PF-C131, PF-C135, PF-C136, PF-C137, PF-C143, PF-C145, PF-C181, PF-C194, PF-C214, PF-C291, and PF-C293).
• In certain embodiments a peptide or composition effective to kill or inhibit the growth and/or proliferation of M. Xanthus can comprise one or more peptides and/or one or more peptide domains comprising or consisting of sequences identified as having activity against M. Xanthus in Tables 4, 5, or 6 (e.g., from the group consisting of G-5, G-6, and G-7).
• In certain embodiments a peptide or composition effective to kill or inhibit the growth and/or proliferation of P. aeruginosa can comprise one or more peptides and/or one or more peptide domains comprising or consisting of sequences identified as having activity against P. aeruginosa in Tables 4, 5, or 6 (e.g., from the group consisting of PF-053, PF-063, PF-067, PF-128, PF-140, PF-143, PF-168, PF-204, PF-209, PF-355, PF-356, PF-366, PF-380, PF-411, PF-425, PF-432, PF-454, PF-458, PF-471, PF-474, PF-527, PF-531, PF-535, PF-536, PF-575, PF-577, PF-605, PF-746, PF-761, and PF-S003).
• In certain embodiments a peptide or composition effective to kill or inhibit the growth and/or proliferation of P. gingivalis can comprise one or more peptides and/or one or more peptide domains comprising or consisting of sequences identified as having activity against P. gingivalis in Tables 4, 5, or 6 (e.g., from the group consisting of PF-C052, PF-0072, PF-0075, PF-0084, PF-0088, PF-0089, PF-C136, PF-C180, PF-C194, and C293).
• In certain embodiments a peptide or composition effective to kill or inhibit the growth and/or proliferation of P. mirabilis can comprise one or more peptides and/or one or more peptide domains comprising or consisting of sequences identified as having activity against P. mirabilis in Tables 4, 5, or 6 (e.g., from the group consisting of PF-040, PF-578, PF-612, PF-624, PF-634, PF-741, and PF-770).
• It was also a surprising discovery that a number of novel antimicrobial peptides are characterized by the presence of particular amino acid motifs. Such motifs include KIF, FIK, KIH, HIK, and KIV, as illustrated in Table 7.

• TABLE 7
  Antimicrobial peptides characterized by particular motifs.

  	Omnibus		SEQ ID
  Motif	#	Sequence	NO
  KIF	PF-278	LSLATFA KIF MTRSNWSLKRFNRL	1567
  	PF-C059	QKIIDMSKFLFSLILFIMIVVIYIGKSIGGYSAIVSS	1568
  		IMLELDTVLYNK KIF FIYK
  	PF-C073	FESLLPQATKKIVNNKGSKIN KIF	1569
  	PF-C085	KKF KIF VIINWFYHKYIILNFEENF	1570
  	PF-531	YIQFHLNQQPRPKVKKI KIF L	1571
  	PF-C194	NTNDLLQAFELMGLGMAGVFIVLGILYIVAELLI	1572
  		KIF PVNN
  	PF-C201	IFKLFEEHLLYLLDAFYYS KIF RRLKQGLYRRKE	1573
  		QPYTQDLFRM
  	PF-442	MQIFYIKT KIF LSFFLFLLIFSQCFYKIEE	1574
  	PF-C252	NYRLVNAIFS KIF KKKFIKF	1575
  FIK	PF-251	MAWK FIK LDKVVSQKECNNFLEKEENKKLLKL	1576
  		LRIQKNMR
  	PF-261	MDIWK FIK SFNTVNTYLLLSCVLLIILVLYFYVI	1577
  		NPA
  	PF-497	LVLRICTDLFT FIK WTIKQRKS	1578
  	PF-775	DLCGQE FIK FKTCVTNQLAKK	1579
  	PF-591	DLLKSLLGQDGAKNDEIIE FIK IIMEK	1580
  	PF-597	DEIKVSDEEIEK FIK ENNL	1581
  	PF-608	LICEVVKPEED FIK VKLNEDNVTAKISREFIAKKI	1582
  		DA
  	IT-133	Y FIK DDNEALSKDWEVIGNDLKGTIDKYGKEFK	1583
  		VR
  	PF-C252	NYRLVNAIFSKIFKKK FIK F	1584
  	PF-C278	DMKIIKLYIKILSFL FIK YCNKKLNSVKLKA	1585
  	PF-C290	GNVHPESDFHNLIQ FIK TFLYFTIFFKYFL	1586
  	PF-006	MGIIAGIIK FIK GLIEKFTGK	1587
  	PF-013	LIQKGLNQTFIVVIRLNN FIK KS	1588
  	PF-040	MIHLTKQNTMEALH FIK QFYDMFFILNFNV	1589
  KIH	PF-252	MKKLVAALAVIVILTGCVYDPVNYD KIH DQEF	1590
  		QDHLRQNG
  	PF-575	LNFRAENKILE KIH ISLIDTVEGSA	1591
  	PF-533	KTPND KIH KTIIIKHIIL	1592
  HIK	PF-222	HIK ETR	1593
  	PF-319	SIGSMIGMYSFRHKTK HIK FTFGIPFILFLQFLLV	1594
  		YFYILK
  	PF-477	HKNKLNIP HIK S	1595
  KIV	PF-272	MTLTIKIKHRS KIV PLNLISLVYAFFTYNFVANRI	1596
  		MFLTND
  	PF-758	PEII KIV SGLL	1597
  	PF-336	MLTSRKKRLK KIV EEQNKKDESI	1598
  	PF-C073	FESLLPQATK KIV NNKGSKINKIF	1599
  	PF-721	TEQAK KIV DILNNWLE	1600
  	PF-730	FEDIEQIIKYHLIDG KIV APLLLDR	1601
  	PF-095	KRGS KIV IAIAVVLIVLAGVWVW	1602
  	PF-028	ALDCSEQSVILWYETILD KIV GVIK	1603
  VIK	PF-257	VWENRKKYLENEIERHNVFLKLGQE VIK GLNA	1604
  		LASRGR
  	PF-226	LMFFSENMDKRDTLSGKFRYFAGSK VIK LMNW	1605
  		LSENGK
  	PF-580	EILNNNQ VIK ELTMKYKTQFESNLGGWTARAR	1606
  		R
  	PF-366	ALCS VIK AIELGIINVHLQ	1607
  	PF-C092	NGDKKAKEELDKWDE VIK ELNIQF	1608
  	PF-S028	GS VIK KRRKRMSKKKHRKMLRRTRVQRRKLG	1609
  		K
  	PF-103	VIK ISVPGQVQMLIP	1610
  	PF-527	GS VIK KRRKRMAKKKHRKLLKKTRIQRRRAGK	1611
  	PF-167	AIEG VIK KGACFKLLRHEMF	1612
  	PF-C166	KRKHENVIVAEEMR VIK N	1613
  	PF-007	MGIIAGIIK VIK SLIEQFTGK	1614
  	PF-071	HCVIGNVVDIANLLKRRAVYRDIAD VIK MR	1615
  	PF-028	ALDCSEQSVILWYETILDKIVG VIK	1616
  PRP	PF-C031	WSESQPPTAT PRP HAEVARAGLVTPPTL	1617
  	PF-752	LHVIR PRP ELSELKFPITKILKVNKQGLKK	1618
  	PF-672	MRFGSLALVAYDSAIKHSW PRP SSVRRLRM	1619
  	PF-088	VMFVLTRGRS PRP MIPAY	1620
  	PF-143	LS PRP IIVSRRSRADNNNDWSR	1621
  	PF-168	VLPFPAIPLSRRRACVAA PRP RSRQRAS	1622
  	PF-531	YIQFHLNQQ PRP KVKKIKIFL	1623

  
  All groups are associated with antimicrobial activity
• In certain embodiments, peptides described herein can have multiple activities. Thus for example, a peptide can have both binding/targeting activity and antimicrobial activity. Illustrative peptides having multiple activities are shown in Table 8. Such peptides can be used, e.g., in a chimeric construct, for any or all of these properties. Thus, for example, a peptide designated “B” in Table 8 can be used as a targeting peptide. If it is also designated G or M it can also be used for antimicrobial activity.

• TABLE 8
  Peptides having multiple activities. B: targeting/binding activity;
  M: antimicrobial activity; G: Growth or phenotype altering.

  	Peptide	Activities
  	PF-001	G B
  	PF-002	G B
  	PF-003	G B
  	PF-004	G B
  	PF-005	G B
  	PF-006	G B M
  	PF-007	G B
  	PF-008	G B
  	PF-009	G B
  	PF-010	G B
  	PF-011	G B
  	PF-012	G B
  	PF-013	G B
  	PF-015	G B
  	PF-017	G B
  	PF-020	G B
  	PF-021	G B
  	PF-022	G B
  	PF-023	G B
  	PF-024	G B
  	PF-025	G B
  	PF-026	G B
  	PF-027	G B
  	PF-028	G B
  	PF-029	G B
  	PF-030	G B
  	PF-031	G B
  	PF-033	G B
  	PF-034	G B
  	PF-035	G B
  	PF-036	G B
  	PF-037	G B
  	PF-040	G B
  	PF-041	G B
  	PF-042	G B
  	PF-043	G B
  	PF-045	G B
  	PF-046	G B
  	PF-048	G B
  	PF-049	G B
  	PF-051	G B
  	PF-052	G B
  	PF-053	G B
  	PF-056	G B
  	PF-057	G B
  	PF-058	G B
  	PF-061	G B
  	PF-063	G B
  	PF-064	G B
  	PF-065	G B
  	PF-066	G B
  	PF-067	G B
  	PF-068	G B
  	PF-069	G B
  	PF-070	G B
  	PF-071	G B
  	PF-073	G B
  	PF-074	G B
  	PF-075	G B
  	PF-076	G B
  	PF-099	G B
  	PF-123	G B
  	PF-124	G B
  	PF-125	G B
  	PF-127	G B
  	PF-128	G B
  	PF-129	G B
  	PF-133	G B
  	PF-135	G B
  	PF-137	G B
  	PF-139	G B
  	PF-140	G B
  	PF-143	G B
  	PF-144	G B
  	PF-145	G B
  	PF-148	G B M
  	PF-149	G B
  	PF-153	G B
  	PF-156	G B
  	PF-157	G B
  	PF-164	G B
  	PF-168	G B M
  	PF-171	G B
  	PF-173	G B
  	PF-175	G B
  	PF-176	G B
  	PF-178	G B
  	PF-180	G B
  	PF-186	G B
  	PF-188	G B
  	PF-190	G B
  	PF-191	G B
  	PF-192	G B
  	PF-196	G B
  	PF-203	G B
  	PF-204	G B
  	PF-208	G B
  	PF-209	G B M
  	PF-212	G B
  	PF-215	G B
  	PF-224	G B
  	PF-226	G B
  	PF-233	G B
  	PF-234	G B
  	PF-235	G B
  	PF-249	G B
  	PF-255	G B
  	PF-257	G B
  	PF-270	G B
  	PF-271	G B
  	PF-273	G B
  	PF-276	G B
  	PF-278	G B M
  	PF-283	G B M
  	PF-289	G B
  	PF-292	G B
  	PF-294	G B
  	PF-297	G B
  	PF-301	G B
  	PF-305	G B
  	PF-306	G B
  	PF-307	G B M
  	PF-313	G B
  	PF-319	G B
  	PF-322	G M
  	PF-344	G B
  	PF-347	G B
  	PF-349	G B
  	PF-350	G B
  	PF-354	G B
  	PF-355	G B
  	PF-356	G B
  	PF-357	G B
  	PF-360	G B
  	PF-362	G B
  	PF-363	G B
  	PF-366	G B
  	PF-369	G B
  	PF-370	G B
  	PF-373	G B
  	PF-374	G B
  	PF-375	G B
  	PF-376	G B
  	PF-378	G B
  	PF-379	G B
  	PF-380	G B
  	PF-381	G B
  	PF-382	G B
  	PF-383	G B
  	PF-385	G B
  	PF-386	G B
  	PF-387	G B
  	PF-389	G B
  	PF-390	G B
  	PF-392	G B
  	PF-393	G B
  	PF-394	G B
  	PF-395	G B
  	PF-396	G B
  	PF-397	G B
  	PF-398	G B
  	PF-399	G B
  	PF-401	G B
  	PF-403	G B
  	PF-404	G B
  	PF-405	G B
  	PF-406	G B
  	PF-407	G B
  	PF-408	G B
  	PF-410	G B
  	PF-411	G B
  	PF-413	G B
  	PF-414	G B
  	PF-416	G B
  	PF-417	G B
  	PF-418	G B
  	PF-421	G B
  	PF-422	G B
  	PF-423	G B
  	PF-424	G B
  	PF-425	G B
  	PF-426	G B
  	PF-427	G B
  	PF-428	G B
  	PF-429	G B
  	PF-430	G B
  	PF-431	G B
  	PF-432	G B
  	PF-433	G B
  	PF-434	G B
  	PF-437	G M
  	PF-439	G B
  	PF-440	G B
  	PF-442	G B
  	PF-443	G B
  	PF-444	G B
  	PF-445	G B
  	PF-446	G B
  	PF-447	G B
  	PF-S003	G B
  	PF-448	G B M
  	PF-450	G B
  	PF-451	G B
  	PF-452	G B
  	PF-453	G B
  	PF-454	G B
  	PF-456	G B
  	PF-457	G B
  	PF-458	G B
  	PF-459	G B
  	PF-460	G B
  	PF-461	G B
  	PF-462	G B
  	PF-464	G B
  	PF-465	G B
  	PF-466	G B
  	PF-467	G B
  	PF-469	G B
  	PF-470	G B
  	PF-471	G B
  	PF-472	G B
  	PF-473	G B
  	PF-474	G B
  	PF-475	G B
  	PF-476	G B
  	PF-477	G B
  	PF-478	G B
  	PF-479	G B
  	PF-480	G B
  	PF-482	G B
  	PF-484	G B
  	PF-497	B M
  	PF-499	B M
  	PF-511	G B M
  	PF-512	G B M
  	PF-513	G B
  	PF-514	G B
  	PF-515	G B
  	PF-516	G
  	PF-517	G B
  	PF-518	G B
  	PF-519	G B
  	PF-520	G B M
  	PF-521	G B M
  	PF-522	G B M
  	PF-523	B M
  	PF-524	G B M
  	PF-525	G M
  	PF-526	G B
  	PF-527	G B M
  	PF-528	G B
  	PF-529	G B M
  	PF-530	G M
  	PF-531	G M
  	PF-537	G B
  	PF-538	G M
  	PF-539	G B
  	PF-540	G B
  	PF-542	G B
  	PF-543	G B
  	PF-544	G B
  	PF-545	G B M
  	PF-546	G B
  	PF-547	G B M
  	PF-548	G B
  	PF-549	G B
  	PF-550	G B
  	PF-551	G B
  	PF-552	G B
  	PF-553	G B
  	PF-554	G B
  	PF-555	G B
  	PF-556	G B
  	PF-557	G B
  	PF-558	G B
  	PF-559	G B
  	PF-560	G B
  	PF-562	G B
  	PF-563	G B
  	PF-564	G B
  	PF-566	G B
  	PF-567	G B
  	PF-569	G B
  	PF-572	G B
  	PF-573	G B
  	PF-575	G B
  	PF-576	G B
  	PF-577	G B
  	PF-578	G B
  	PF-580	G B
  	PF-581	G B
  	PF-583	G B M
  	PF-584	G B
  	PF-585	G B
  	PF-586	G B
  	PF-587	G B
  	PF-588	G B
  	PF-589	G B
  	PF-590	G B
  	PF-592	G B
  	PF-593	G B
  	PF-594	G B
  	PF-595	G B
  	PF-596	G B
  	PF-597	G B
  	PF-598	G B
  	PF-599	G B
  	PF-600	G B M
  	PF-601	G B
  	PF-602	G B
  	PF-603	G B
  	PF-604	G B
  	PF-605	G B
  	PF-606	G M
  	PF-607	G B
  	PF-609	G B
  	PF-610	G B
  	PF-612	G B
  	PF-613	G B
  	PF-614	G B
  	PF-615	G B
  	PF-616	G B
  	PF-617	G B
  	PF-619	G B
  	PF-621	G B
  	PF-622	G B
  	PF-623	G B
  	PF-625	G B
  	PF-626	G B
  	PF-627	G B
  	PF-629	G B
  	PF-630	G B
  	PF-631	G B
  	PF-632	G B
  	PF-634	G B
  	PF-635	G B
  	PF-636	G B
  	PF-637	G B
  	PF-638	G B
  	PF-639	G B
  	PF-640	G B
  	PF-642	G B
  	PF-655	G B
  	PF-664	G B
  	PF-672	G B M
  	PF-681	G B
  	PF-686	G B
  	PF-737	G B
  	PF-738	G B
  	PF-741	G B
  	PF-744	G B
  	PF-745	G B
  	PF-746	G B
  	PF-748	G B
  	PF-749	G B
  	PF-752	G B
  	PF-756	G B
  	PF-757	G B
  	PF-760	G B
  	PF-761	G B
  	PF-762	G B
  	PF-763	G B
  	PF-764	G B
  	PF-770	G B
  	PF-776	G B
  	PF-C052	G B
  	PF-C055	G B
  	PF-C057	G B
  	PF-C058	G B
  	PF-C061	G B
  	PF-C062	G B
  	PF-C064	G B
  	PF-C065	G B
  	PF-C069	G B
  	PF-C071	G B
  	PF-C072	G B
  	PF-C075	G B
  	PF-C084	G B
  	PF-C085	G B
  	PF-C086	G B
  	PF-C088	G B
  	PF-C091	G B
  	PF-C095	G B
  	PF-C098	G B
  	PF-C120	G B
  	PF-C131	G B
  	PF-C135	G B
  	PF-C136	G B
  	PF-C137	G B
  	PF-C139	G B
  	PF-C142	G B
  	PF-C143	G B
  	PF-C145	G B
  	PF-C180	G B
  	PF-C181	G B
  	PF-C194	G B
  	PF-C281	G B
  	PF-C290	G B
  	PF-C291	G B

• Other peptides believed to show binding, growth altering, and/or antimicrobial activity are shown in Table 9.

• TABLE 9
  Additional peptides believed to have binding, growth
  altering,mand/or antimicrobial activity.

  		SEQ
  ID	Sequence	ID No.
  PF-198	RRLASRRSLVVST	1624
  PF-227	RLLGLYGENSAAGFIASVIGAVIILFIYNLIARKS	1625
  PF-260	GHLRVCWILWLQSANPLSFRHHYLAVMW	1626
  PF-261	MDIWKFIKSFNTVNTYLLLSCVLLIILVLYFYVINPA	1627
  PF-277	MIIQNKKIEKIYKYQTKEIFLNKTSLRAGFVFRMVRVLI	1628
  PF-280	MLIDWQEPDIEKSFCAAFLKISVSVLVYRTPLGYGNQLRE	1629
  PF-286	FFDGEVGCGC	1630
  PF-287	ILEQNIEEVFFIQS	1631
  PF-312	MDKIRIWNNFHISNEYIKQRYGIISIPLFYVYLF	1632
  PF-321	FAKKNPCRMRVPNTGTWYLVVNQDGNSGIVNFSINTIQN	1633
  PF-327	MLVFQMRYQMRYVDKTSTVLKQTKNSDYADK	1634
  PF-330	MLMNFEVYQQRILIIYNKCYHLKAVGKNLQLFIIVD	1635
  PF-331	MGRHLWNPSYFVATVSENTEEQIRKYINNQKKQVK	1636
  PF-341	DDKNEGKIAQGEY	1637
  PF-391	EASVYRE	1638
  PF-420	MVKHNFDVTDKTGKISSKHCFEITDKTDVV	1639
  PF-708	DRPSQTTHHTLSSSRITGPS	1640
  PF-710	EALLPPDPPDEDSQRIIPQ	1641
  PF-713	DRPSQTTHHTLSSSRITGPS	1642
  PF-715	LEDTKALFPCFVPI	1643
  PF-718	KKYSSFKSMIDDLEYDA	1644
  PF-719	FKSMIDDLEYDA	1645
  PF-721	TEQAKKIVDILNNWLE	1646
  PF-722	STSPSVTSVYAEALGLK	1647
  PF-723	VGAMAIFLNVVAMLAGV	1648
  PF-725	ARTIQNNGCLIHNSRYP	1649
  PF-726	CDDLYALEAQGTLNELLKK	1650
  PF-729	TPEPVVIVKP	1651
  PF-730	FEDIEQIIKYHLIDGKIVAPLLLDR	1652
  PF-734	SDIIAENIFQQGELEPMLRDAVAA	1653
  PF-736	KGSASGSASGSGSAK	1654
  PF-739	KSGASSVASAAKSG	1655
  PF-742	AAATTATTAK	1656
  PF-743	TKGTTTGTAKTTGVTTGTAK	1657
  PF-769	GSRGGAKRGGARG	1658
  PF-C031	WSESQPPTATPRPHAEVARAGLVTPPTL	1659
  PF-C038	QPIGFPTDSVHGTDLVHRLRGTTSSR	1660
  PF-C077	LENLDIEGLTEMKEHIEDLIAEKSAAESIEEVIVEAE	1661
  PF-C205	AYSLTFQNPNDNLTDEEVAKYMEKITKALTEKIGAEVR	1662
  PF-S016	PLTRETFAERGIRKARVARTFSEEEPPF	1663

III. Design and Construction of STAMPs and Other Chimeric Constructs.
• In various embodiments this invention provides chimeric moieties comprising one or more targeting moieties attached to one or more effectors. The targeting moieties can be selected to preferentially bind to a target microorganism (e.g., bacteria, virus, fungi, yeast, alga, protozoan, etc.) or group of microorganisms (e.g., gram-negative or gram-positive bacteria, particular genus, species, etc.) In certain embodiments the targeting moiety comprises one or more novel microorganism-binding peptides as described herein (see, e.g., Table 3, and/or Table 10, and/or Table 12). In certain embodiments the targeting moiety comprises non-peptide moieties (e.g., antibodies, receptor, receptor ligand, lectin, and the like).
• In various embodiments the effector comprises a moiety whose activity is to be delivered to the target microorganism(s), to a biofilm comprising the target microorganism(s), to a cell or tissue comprising the target microorganism(s), and the like. In certain embodiments the targeting moiety comprises one or more antimicrobial peptide(s) as described herein (see, e.g., Tables 4, 5 and/or 14), an antibiotic (including, but not limited to a steroid antibiotic), a detectable label, a porphyrin, a photosensitizing agent, an epitope tag, a lipid or liposome, a nanoparticle, a dendrimer, and the like.
• In certain embodiments one or more targeting moieties are attached to a single effector. In certain embodiments one or more effectors are attached to a single targeting moiety. In certain embodiments multiple targeting moieties are attached to multiple effectors. The targeting moieties(s) can be attached directly to the effector(s) or through a linker. Where the targeting moiety and the effector comprise peptides the chimeric moiety can be a fusion protein.
• A) Targeting Moieties.
• In various embodiments this invention provides targeting moieties that preferentially and/or specifically bind to a microorganism (e.g., a bacterium, a fungus, a yeast, etc.). One or more such targeting moieties can be attached to one or more effectors to provide chimeric moieties that are capable of delivering the effector(s) to a target (e.g., a bacterium, a fungus, a yeast, a biofilm comprising the bacterium or fungus or yeast, etc.).
• In various embodiments, targeting moieties include, but are not limited to peptides that preferentially bind particular microorganisms (e.g., bacteria, fungi, yeasts, protozoa, algae, viruses, etc.) or groups of such microorganisms, e.g., as described above, antibodies that bind particular microorganisms or groups of microorganisms, receptor ligands that bind particular microorganisms or groups of microorganisms, porphyrins (e.g., metalloporphyrins), lectins that bind particular microorganisms or groups of microorganisms, and the like. As indicated it will be appreciated that references to microorganisms or groups of microorganism include bacteria or groups of bacteria, viruses or groups of viruses, yeasts or groups of yeasts, protozoa or groups of protozoa, viruses or groups of viruses, and the like.
• i. Targeting Peptides.
• In certain embodiments, the targeting moiety comprises one or more targeting peptides that bind particular bacteria, fungi, and/or yeasts, and/or algae, and/or viruses and/or that bind particular groups of bacteria, and/or groups of fungi, and/or groups of yeasts, and/or groups of algae.
• In certain embodiments the targeting peptide can comprise one or more domains capable of binding, specifically binding, or preferentially binding to a microorganism, e.g., a target microbial organism (see, e.g., Table 3). In certain embodiment, the targeting peptide be identified via screening peptide libraries. For example, a phage display peptide library can be screened against a target microbial organism or a desired antigen or epitope thereof. Any peptide identified through such screening can be used as a targeting peptide for the target microbial organism. Illustrative additional targeting peptides are shown in Table 10.

• TABLE 10
  Additional illustrative targeting moieties.

  Targeting Moiety/		SEQ ID
  Organism	Structure/sequence	NO
  LPSB-1	RGLRRLGRRGLRRLGR	1664
  Phob-1	KPVLPVLPVLPVL	1665
  LPSB-2	VLRIIRIAVLRIIRIA	1666
  LPTG-1	LPETGGSGGSLPETG	1667
  α-1	RAHIRRAHIRR	1668
  ANION-1	DEDEDDEEDDDEEE	1669
  PHILIC-1	STMCGSTMCGSTMCG	1670
  SA5.1/S. aureus	VRLPLWLPSLNE	1671
  SA5.3/S. aureus	ANYFLPPVLSSS	1672
  SA5.4/S. aureus	SHPWNAQRELSV	1673
  SA5.5/S. aureus	SVSVGMRPMPRP	1674
  SA5.6/S. aureus	WTPLHPSTNRPP	1675
  SA5.7/S. aureus	SVSVGMKPSPRP	1676
  SA5.8/S. aureus	SVSVGMKPSPRP	1677
  SA5.9/S. aureus	SVPVGPYNESQP	1678
  SA5.10/S. aureus	WAPPLFRSSLFY	1679
  SA2.2/S. aureus	WAPPXPXSSLFY	1680
  SA2.4/S. aureus	HHGWTHHWPPPP	1681
  SA2.5/S. aureus	SYYSLPPIFHIP	1682
  SA2.6/S. aureus	HFQENPLSRGGEL	1683
  SA2.7/S. aureus	FSYSPTRAPLNM	1684
  SA2.8/S. aureus	SXPXXMKXSXXX	1685
  SA2.9/S. aureus	VSRHQSWHPHDL	1686
  SA2.10/S. aureus	DYXYRGLPRXET	1687
  SA2.11/S. aureus	SVSVGMKPSPRP	1688
  S. aureus/	V/Q/H-P/H-H-E-F/Y-K/H-H/A-L/H-X-X-K/R-P/L	1689
  Consensus
  DH5.1/E coli.	KHLQNRSTGYET	1690
  DH5.2/E coli.	HIHSLSPSKTWP	1691
  DH5.3/E coli.	TITPTDAEMPFL	1692
  DH5.4/E coli.	HLLESGVLERGM	1693
  DH5.5/E coli.	HDRYHIPPLQLH	1694
  DH5.6/E coli.	VNTLQNVRHMAA	1695
  DH5.7/E coli.	SNYMKLRAVSPF	1696
  DH5.8/E coli.	NLQMPYAWRTEF	1697
  DH5.9/E coli.	QKPLTGPHFSLI	1698
  CSP/S. mutans	SGSLSTFFRLFNRSFTQALGK	1699
  CSPC18/ S.  mutans	LSTFFRLFNRSFTQALGK		1700
  CSPC16/S. mutans	TFFRLFNRSFTQALGK	1701
  CSPM8/S. mutans	TFFRLFNR	1702
  KH/Pseudomonas spp	KKHRKHRKHRKH	1703
  (US 2004/0137482)
  cCF10	LVTLVFV	1704
  AgrD1	YSTCDFIM	1705
  AgrD2	GVNACSSLF	1706
  AgrD3	YINCDFLL	1707
  NisinA	ITSISLCTPGCKTGALMGCNMRTATCIICSIIIVSK	1708
  PlnA	KSSAYSLQMGATAIKQVKKLFKKWGW	1709
  S3L1-5	WWYNWWQDW	1710
  Penetratin	RQIKIWFWNRRMKWKK*	1711
  Tat	EHWSYCDLRPG	1712
  Pep-1N	KETWWETWWTEW	1713
  Pep27	MRKEFHNVLS SGQLLADKRPARDYNRK	1714
  HABP35	LKQKIKHVVKLKVVVKLRSQLVKRKQN	1715
  HABP42 (all D)	STMMSRSHKTRSHHV	1716
  HABP52	GAHWQFNALTVRGGGS	1717
  Hi3/17	KQRTSIRATEGCLPS	1718
  α-E.coli peptide	QEKIRVRLSA	1719
  Salivary Receptor	QLKTADLPAGRDETTSFVLV*	1720
  Adhesion Fragment
  S1 (Sushi frag.)	GFKLKGMARISCLPNGQWSNFPPKCIRECAMVSS	1721
  (LPS binding)
  S3 (Sushi frag.)	HAEHKVKIGVEQKYGQFPQGTEVTYTC SGNYFL	1722
  (LPS binding)	M
  MArg.1	AMDMYSIEDRYFGGYAPEVG	1723
  (Mycoplasma infected
  cell line binding
  peptide
  BPI fragment
  1	ASQQGTAALQKELKRIKPDYSDSFKIKH	1724
  (LPS binding)
  6,376,462
  BPI fragment 2	SSQISMVPNVGLKFSISNANIKISGKWKAQKRFL	1725
  (LPS binding)	K
  6,376,462
  BPI fragment 3	VHVHISKSKVGWLIQLFHKKIESALRNK	1726
  (LPS binding)
  6,376,462
  LBP fragment 1	AAQEGLLALQSELLRITLPDFTGDLRIPH	1727
  (LPS binding)
  6,376,462
  LBP fragment 2	HSALRPVPGQGLSLSISDSSIRVQGRWKVRKSFF	1728
  (LPS binding)	K
  6,376,462
  LBP fragment 3	VEVDMSGDLGWLLNLFHNQIESKFQKV	1729
  (LPS binding)
  6,376,462
  B. anthracis spore	ATYPLPIR	1730
  binding
  (WO/1999/036081)
  Bacillus	peptides of 5-12 amino acids containing the	1731
  sporebinding	sequence
  (WO/1999/036081)	Asn-His-Phe-Leu
  	peptides of 5-12 amino acids containing the	1732
  	sequence
  	Asn-His-Phe-Leu-Pro
  	Thr-Ser-Glu-Asn-Val-Arg-Thr (TSQNVRT)	1733
  	A peptide of formula Thr-Tyr-Pro-X-Pro-X-Arg	1734
  	(TYPXPXR) where X is a Ile, Val or Leu.
  	A peptide having the sequence TSQNVRT.	1735
  	A peptide having the sequence TYPLPIR	1736
  LPS binding peptide	TFRRLKWK	1737
  1 (6,384,188)
  LPS BP 2 (6,384,188)	RWKVRKSFFKLQ	1738
  LPS BP 3 (6,384,188)	KWKAQKRFLKMS	1739
  Pseudomonas pilin	KCTSDQDEQFIPKGCSK	1740
  binding peptide
  (5,494,672)
  RNAII inhibiting	YSPWTNF	1741
  peptide (S. Aureus)

  
  Patents and patent publications disclosing the referenced antibodies are identified in the table.
• In certain embodiments the targeting moieties can comprise other entities, particularly when utilized with an antimicrobial peptide as described, for example, in Table 4. Illustrative targeting moieties can include a polypeptide, a peptide, a small molecule, a ligand, a receptor, an antibody, a protein, or portions thereof that specifically interact with a target microbial organism, e.g., the cell surface appendages such as flagella and pili, and surface exposed proteins, lipids and polysaccharides of a target microbial organism.
• ii. Targeting Antibodies.
• In certain embodiments the targeting moieties can comprise one or more antibodies that bind specifically or preferentially a microorganism or group of microorganisms (e.g., bacteria, fungi, yeasts, protozoa, viruses, algae, etc.). The antibodies are selected to bind an epitope characteristic or the particular target microorganism(s). In various embodiments such epitopes or antigens are typically is gram-positive or gram-negative specific, or genus-specific, or species-specific, or strain specific and located on the surface of a target microbial organism. The antibody that binds the epitope or antigen can direct an anti-microbial peptide moiety or other effector to the site. Furthermore, in certain embodiments the antibody itself can provide anti-microbial activity in addition to the activity provided by effector moiety since the antibody may engage an immune system effector (e.g., a T-cell) and thereby elicit an antibody-associated immune response, e.g., a humoral immune response.
• Antibodies that bind particular target microorganisms can be made using any methods readily available to one skilled in the art. For example, as described in U.S. Pat. No. 6,231,857 (incorporated herein by reference) three monoclonal antibodies, i.e., SWLA1, SWLA2, and SWLA3 have been made against S. mutans. Monoclonal antibodies obtained from non-human animals to be used in a targeting moiety can also be humanized by any means available in the art to decrease their immunogenicity and increase their ability to elicit anti-microbial immune response of a human. Illustrative microorganisms and/or targets to which antibodies may be directed are shown, for example, in Tables 3 and 11.
• Various forms of antibody include, without limitation, whole antibodies, antibody fragments (e.g., (Fab′)₂ Fab′, etc.), single chain antibodies (e.g., scFv), minibodies, Di-miniantibody, Tetra-miniantibody, (scFv)₂, Diabody, scDiabody, Triabody, Tetrabody, Tandem diabody, VHH, nanobodies, affibodies, unibodies, and the like.
• Methods of making such antibodies are well known to those of skill in the art. In various embodiments, such methods typically involve providing the microorganism, or a component thereof for use as an antigen to raise an immune response in an organism or for use in a screening protocol (e.g., phage or yeast display).
• For example, polyclonal antibodies are typically raised by one or more injections (e.g. subcutaneous or intramuscular injections) of the target microorganism(s) or components thereof into a suitable non-human mammal (e.g., mouse, rabbit, rat, etc.).
• If desired, the immunizing microorganism or antigen derived therefrom can be administered with or coupled to a carrier protein by conjugation using techniques that are well-known in the art. Such commonly used carriers which are chemically coupled to the peptide include keyhole limpet hemocyanin (KLH), thyroglobulin, bovine serum albumin (BSA), and tetanus toxoid. The coupled peptide is then used to immunize the animal (e.g. a mouse or a rabbit).
• The antibodies are then obtained from blood samples taken from the mammal. The techniques used to develop polyclonal antibodies are known in the art (see, e.g., Methods of Enzymology, “Production of Antisera With Small Doses of Immunogen: Multiple Intradermal Injections”, Langone, et al. eds. (Acad. Press, 1981)). Polyclonal antibodies produced by the animals can be further purified, for example, by binding to and elution from a matrix to which the peptide to which the antibodies were raised is bound. Those of skill in the art will know of various techniques common in the immunology arts for purification and/or concentration of polyclonal antibodies, as well as monoclonal antibodies see, for example, Coligan, et al. (1991) Unit 9, Current Protocols in Immunology, Wiley Interscience).
• In certain embodiments the antibodies produced will be monoclonal antibodies (“mAb's”). The general method used for production of hybridomas secreting mAbs is well known (Kohler and Milstein (1975) Nature, 256:495
• Antibody fragments, e.g. single chain antibodies (scFv or others), can also be produced/selected using phage display and/or yeast display technology. The ability to express antibody fragments on the surface of viruses that infect bacteria (bacteriophage or phage) or yeasts makes it possible to isolate a single binding antibody fragment, e.g., from a library of greater than 10¹⁰ nonbinding clones. To express antibody fragments on the surface of phage (phage display) or yeast, an antibody fragment gene is inserted into the gene encoding a phage surface protein (e.g., pIII) and the antibody fragment-pIII fusion protein is displayed on the phage surface (McCafferty et al. (1990) Nature, 348: 552-554; Hoogenboom et al. (1991) Nucleic Acids Res. 19: 4133-4137).
• Since the antibody fragments on the surface of the phage or yeast are functional, phage bearing antigen binding antibody fragments can be separated from non-binding phage by antigen affinity chromatography (McCafferty et al. (1990) Nature, 348: 552-554). Depending on the affinity of the antibody fragment, enrichment factors of 20 fold-1,000,000 fold are obtained for a single round of affinity selection.
• Human antibodies can be produced without prior immunization by displaying very large and diverse V-gene repertoires on phage (Marks et al. (1991) J. Mol. Biol. 222: 581-597.
• In certain embodiments, nanobodies can be used as targeting moieties. Methods of making V_hH (nanobodies) are also well known to those of skill in the art. The Camelidae heavy chain antibodies are found as homodimers of a single heavy chain, dimerized via their constant regions. The variable domains of these camelidae heavy chain antibodies are referred to as V_HH domains or V_HH, and can be either used per se as nanobodies and/or as a starting point for obtaining nanobodies. Isolated V_HH retain the ability to bind antigen with high specificity (see, e.g., Hamers-Casterman et al. (1993) Nature 363: 446-448). In certain embodiments such V_HH domains, or nucleotide sequences encoding them, can be derived from antibodies raised in Camelidae species, for example in camel, dromedary, llama, alpaca and guanaco. Other species besides Camelidae (e.g. shark, pufferfish) can produce functional antigen-binding heavy chain antibodies, from which (nucleotide sequences encoding) such naturally occurring V_HH can be obtained, e.g. using the methods described in U.S. Patent Publication US 2006/0211088.
• In various embodiments, for use in therapy, human proteins are preferred, primarily because they are not as likely to provoke an immune response when administered to a patient. Comparisons of camelid V_HH with the V_H domains of human antibodies reveals several key differences in the framework regions of the camelid V_HH domain corresponding to the V_H/V_L interface of the human V_H domains. Mutation of these human residues to V_HH resembling residues has been performed to produce “camelized” human V_H domains that retain antigen binding activity, yet have improved expression and solubility.
• Libraries of single V_H domains have also been derived for example from V_H genes amplified from genomic DNA or from mRNA from the spleens of immunized mice and expressed in E. coli (Ward et al. (1989) Nature 341: 544-546) and similar approaches can be performed using the V_H domains and/or the V_L domains described herein. The isolated single VH domains are called “dAbs” or domain antibodies. A “dAb” is an antibody single variable domain (V_H or V_L) polypeptide that specifically binds antigen. A “dAb” binds antigen independently of other V domains; however, as the term is used herein, a “dAb” can be present in a homo- or heteromultimer with other V_H or V_L domains where the other domains are not required for antigen binding by the dAb, i.e., where the dAb binds antigen independently of the additional V_H or V_L domains.
• As described in U.S. Patent Publication US 2006/0211088 methods are known for the cloning and direct screening of immunoglobulin sequences (including but not limited to multivalent polypeptides comprising: two or more variable domains—or antigen binding domains—and in particular V_H domains or V_HH domains; fragments of V_L, V_H or V_HH domains, such as CDR regions, for example CDR3 regions; antigen-binding fragments of conventional 4-chain antibodies such as Fab fragments and scFv's, heavy chain antibodies and domain antibodies; and in particular of V_H sequences, and more in particular of V_HH sequences) that can be used as part of and/or to construct such nanobodies.
• Methods and procedures for the production of VHH/nanobodies can also be found for example in WO 94/04678, WO 96/34103, WO 97/49805, WO 97/49805 WO 94/25591, WO 00/43507 WO 01/90190, WO 03/025020, WO 04/062551, WO 04/041863, WO 04/041865, WO 04/041862, WO 04/041867, PCT/BE2004/000159, Hamers-Casterman et al. (1993) Nature 363: 446; Riechmann and Muyldermans (1999) J. Immunological Meth., 231: 25-38; Vu et al. (1997) Molecular Immunology, 34(16-17): 1121-1131; Nguyen et al. (2000) EMBO J., 19(5): 921-930; Arbabi Ghahroudi et al. (19997) FEBS Letters 414: 521-526; van der Linden et al. (2000) J. Immunological Meth., 240: 185-195; Muyldermans (2001) Rev. Molecular Biotechnology 74: 277-302; Nguyen et al. (2001) Adv. Immunol. 79: 261, and the like.
• In certain embodiments the antibody targeting moiety is a unibody. Unibodies provide an antibody technology that produces a stable, smaller antibody format with an anticipated longer therapeutic window than certain small antibody formats. In certain embodiments unibodies are produced from IgG4 antibodies by eliminating the hinge region of the antibody. Unlike the full size IgG4 antibody, the half molecule fragment is very stable and is termed a uniBody. Halving the IgG4 molecule left only one area on the UniBody that can bind to a target. Methods of producing unibodies are described in detail in PCT Publication WO2007/059782, which is incorporated herein by reference in its entirety (see, also, Kolfschoten et al. (2007) Science 317: 1554-1557).
• Affibody molecules are class of affinity proteins based on a 58-amino acid residue protein domain, derived from one of the IgG-binding domains of staphylococcal protein A. This three helix bundle domain has been used as a scaffold for the construction of combinatorial phagemid libraries, from which Affibody variants that target the desired molecules can be selected using phage display technology (see, e.g., Nord et al. (1997) Nat. Biotechnol. 15: 772-777; Ronmark et al. (2002) Eur. J Biochem., 269: 2647-2655.). Details of Affibodies and methods of production are known to those of skill (see, e.g., U.S. Pat. No. 5,831,012 which is incorporated herein by reference in its entirety).
• It will also be recognized that antibodies can be prepared by any of a number of commercial services (e.g., Berkeley antibody laboratories, Bethyl Laboratories, Anawa, Eurogenetec, etc.).
• Illustrative antibodies that bind various microorganisms are shown in Table 11.

• TABLE 11
  Illustrative antibodies that bind target microorganisms.

  Source	Antibody
  U.S. Pat. No. 7,195,763	Polyclonal/monoclonal binds specific
  	Gram(+) cell wall repeats
  U.S. Pat. No. 6,939,543	Antibodies against G(+) LTA
  U.S. Pat. No. 7,169,903	Antibodies against G(+) peptidoglycan
  U.S. Pat. No. 6,231,857	Antibody against S. mutans (Shi)
  U.S. Pat. No. 5,484,591	Gram(−) binding antibodies
  US 2007/0231321	Diabody binding to Streptococcus surface
  	antigen I/II
  US 2003/0124635	Antibody against S. mutans
  US 2006/0127372	Antibodies to Actinomyces naeslundii,
  	Lactobacillus casei
  US 2003/0092086	Antibody to S. sobrinus
  U.S. Pat. No. 7,364,738	Monoclonal antibodies to the ClfA protein
  	in S. aureus
  U.S. Pat. No. 7,632,502	Antibodies against C. albicans
  U.S. Pat. No. 7,608,265	Monoclonal against C. difficile
  U.S. Pat. No. 4,777,136	Monoclonal Antibodies against
  	Pseudomonas aeruginosa
  see, e.g., ab20429, ab20560,	Antibody against S. pneumoniae
  ab79522, ab35165, ab65602
  from AbCAMm Cambridge
  Science Park, U.K.

• In addition, antibodies (targeting moieties) that bind other microorganisms can readily be produced using, for example, the methods described above.
• iii. Porphyrins.
• In certain embodiments porphyrins, or other photosensitizing agents, can be used as targeting moieties in the constructs described herein. In particular, metalloporphyrins, particularly a number of non-iron metalloporphyrins mimic heme in their molecular structure and are actively accumulated by bacteria via high affinity heme-uptake systems. The same uptake systems can be used to deliver antibiotic-porphyrin and antibacterial-porphyrin conjugates. Illustrative targeting porphyrins suitable for this purpose are described in U.S. Pat. No. 6,066,628 and shown herein, for example, in FIGS. 1 and 2.
• For example, certain artificial (non-iron) metalloporphyrins (MPs) (Ga-IX, Mn-IX,) are active against Gram-negative and Gram-positive bacteria and acid-fast bacilli (e.g., Y. enterocolitica, N. meningitides, S. marcescens, E. coli, P. mirabilis, K pneumoniae, K. oxytoca, Ps. aeruginosa, C. freundii, E. aerogenes, F. menigosepticum, S. aureus, B. subtilis, S. pyogenes A, E. faecalis, M. smegmatis, M. bovis, M. tuber., S. crevisiae) as described in Tables 1-5 of U.S. Pat. No. 6,066,628. These MPs can be used as targeting moieties against these microorganisms.
• Similarly, some MPs are also growth-inhibitory against yeasts, indicating their usefulness targeting moieties to target Candida species (e.g., Candida albicans, C. krusei, C. pillosus, C. glabrata, etc.) and other mycoses including but not limited to those caused by as Trichophyton, Epidermophyton, Histoplasma, Aspergillus, Cryptococcus, and the like.
• Porphyrins, and other photosensitizers, also have antimicrobial activity. Accordingly, in certain embodiments, the porphyrins, or other photosensitizers, can be used as effectors (e.g., attached to targeting peptides as described herein). In various embodiments the porphyrins or other photosensitizers can provide a dual functionality, e.g., as a targeting moiety and an antimicrobial and can be attached to a targeting peptide and/or to an antimicrobial peptide as described herein.
• Illustrative porphyrins and other photosensitizers are shown in FIGS. 1-11 and described in more detail in the discussion of effectors below.
• iv. Pheromones.
• In certain embodiments, pheromones from microorganisms can be used as targeting moieties. Illustrative pheromones from bacteria and fungi are shown in Table 12.

• TABLE 12
  Illustrative bacterial and fungal pheromones utilizable as targeting moieties.

  Locus tag	Product	Sequence	SEQ ID
  Bacterial Pheromones
  gi|1041118|dbj|BAA11198.1|	iPD1 [Enterococcus faecalis]	MKQQKKHIAALLF	1742
  		ALILTLVS
  gi|l113947|gb|AAB35253.1|	iAM373sex pheromone	SIFTLVA	1743
  	inhibito [Enterococcus
  	faecalis, Peptide, 7 aa]
  gi|115412|sp|1313268.1|CAD1_	Sex pheromone CAD1	LFSLVLAG	1744
  ENTFA
  gi|116406|sp|P11932.1|CIA_	Sex pheromone cAM373	AIFILAS	1745
  ENTFA	(Clumping-inducing
  	agent) (CIA)
  gi|117240|sp|P13269.1|CPD1_	Sex pheromone cPD1	FLVMFLSG	1746
  ENTFA
  gi|12056953|gb|AAG48144.1|	putative peptide	DSIRDVSPTFNKIRR	1747
  AF322594_1	pheromone PrcA	WFDGLFK
  	[Lactobacillus paracasei]
  gi|123988|sp|P24803.1|IAD1_	Sex pheromone inhibitor	MSKRAMKKIIPLIT	1748
  ENTFA	determinant precursor	LFVVTLVG
  	(iAD1)
  gi|126362994|emb|CAM35812 .1|	precursor of pheromone	KDEIYWKPS	1749
  	peptide ComX [Bacillus
  	amyloliquefaciens FZB42]
  gi|1587088|prf|2205353A	pheromone	YSTCDFIM	1750
  gi|15900442|ref|NP_345046.1|	peptide pheromone BlpC	GLWEDLLYNINRY	1751
  	[Streptococcus	AHYIT
  	pneumoniae TIGR4]
  gi|1617436|emb|CAA66791.1|	competence pheromone	DIRHRINNSIWRDIF	1752
  	[Streptococcus gordonii]	LKRK
  gi|1617440|emb|CAA66786.1|	competence pheromone	DVRSNKIRLWWEN	1753
  	[Streptococcus gordonii]	IFFNKK
  gi|18307870|gb|AAL67728.1|	ComX pheromone	PTTREWDG	1754
  AF456134_2	precursor [Bacillus
  	mojavensis]
  gi|18307874|gb|AAL67731.1|_	ComX pheromone	LQIYTNGNWVPS	1755
  AF456135_2	precursor [Bacillus
  	mojavensis]
  gi|29377808|ref|NP_816936.1|	sex pheromone inhibitor	MSKRAMKKIIPLIT	1756
  	determinant [Enterococcus	LFVVTLVG
  	faecalis V583]
  gi|3342125|gb|AAC27522.1|	putative pheromone	GAGKNLIYGMGYG	1757
  	[Enterococcus faecium]	YLRSCNRL
  gi|41018893|sp|P60242.1|CSP1_	Competence-stimulating	EMRLSKFFRDFILQ	1758
  STRPN	peptide type 1 precursor	RKK
  	(CSP-1)
  gi|57489126|gb|AAW51333.1|	PcfP [Enterococcus	WSEIEINTKQSN	1759
  	faecalis]
  gi|57489152|gb|AAW51349.1|	PrgT [Enterococcus	HISKERFEAY	1760
  	faecalis]
  gi|58616083|ref|YP_195761.1|	UvaF [Enterococcus	KYKCSWCKRVYTL	1761
  	faecalis]	RKDHRTAR
  gi|58616111|ref|YP_195802.1|	PcfP [Enterococcus	WSEIEINTKQSN	1762
  	faecalis]
  gi|58616132|ref|YP_195769.1|	PrgQ [Enterococcus	MKTTLKKLSRYIA	1763
  	faecalis]	VVIAITLIFI
  gi|58616137|ref|YP_195772.1|	PrgT [Enterococcus	HISKERFEAY	1764
  	faecalis]
  gi|6919848|sp|O33689.1|CSP_	Competence-stimulating	DKRLPYFFKHLFSN	1765
  STROR	peptide precursor (CSP)	RTK
  gi|6919849|sp|O33666.1|CSP2_	Competence-stimulating	EMRKPDGALFNLF	1766
  STRMT	peptide precursor (CSP)	RRR
  gi|6919850|sp|O33668.1|CSP3_	Competence-stimulating	EMRKSNNNFFHFL	1767
  STRMT	peptide precursor (CSP)	RRI
  gi|6919851|sp|O33672.1|CSP1_	Competence-stimulating	ESRLPKIRFDFIFPR	1768
  STRMT	peptide precursor (CSP)	KK
  gi|6919852|sp|O33675.1|CSP4_	Competence-stimulating	EIRQTHNIFFNFFKR	1769
  STRMT	peptide precursor (CSP)	R
  gi|6919853|sp|O33690.1|CSP2_	Competence-stimulating	DWRISETIRNLIFPR	1770
  STROR	peptide precursor (CSP)	RK
  gi|999344|gb|AAB34501.1|	cOB1 bacterial sex	VAVLVLGA	1771
  	pheromone [Enterococcus
  	faecalis, Peptide, 8 aa]
  gi|18307878|gb|AAL67734.1|	ComX pheromone	FFEDDKRKSFI	1772
  AF456136_2	precursor [Bacillus
  	subtilis]
  gi|18307882|gb|AAL67737.1|	ComX pheromone	FFEDDKRKSFI	1773
  AF456137_2	precursor [Bacillus
  	subtilis]
  gi|28272731|emb|CAD65660.1|	accessory gene regulator	MKQKMYEAIAHLF	1774
  	protein D, peptide	KYVGAKQLVMCC
  	pheromone precursor	VGIWFETKIPDELR
  	[Lactobacillus plantarum	K
  	WCFS1]
  gi|28379890|ref|NP_786782.1|	accessory gene regulator	MKQKMYEAIAHLF	1775
  	protein D, peptide	KYVGAKQLVMCC
  	pheromone precursor	VGIWFETKIPDELR
  	[Lactobacillus plantarum	K
  	WCFS1]
  gi|57489105|gb|AAW51312.1|	PrgF [Enterococcus	VVAYVITQVGAIRF	1776
  	faecalis]
  gi|58616090|ref|YP_195779.1|	PrgF [Enterococcus	VVAYVITQVGAIRF	1777
  	faecalis]
  gi|58616138|ref|YP_195762.1|	PrgN [Enterococcus	LLKLQDDYLLHLE	1778
  	faecalis]	RHRRTKKIIDEN
  gi|57489117|gb|AAW51324.1|	Pcff [Enterococcus	EDIKDLTDKVQSLN	1779
  	faecalis]	ALVQSELNKLIKRK
  		DQS
  gi|57489119|gb|AAW51326.1|	PcfH [Enterococcus	WFLDFSDWLSKVP	1780
  	faecalis]	SKLWAE
  gi|58616102|ref|YP_195792.1|	Pcff [Enterococcus	EDIKDLTDKVQSLN	1781
  	faecalis]	ALVQSELNKLIKRK
  		DQS
  gi1586161041ref1YP_195794.11	PcfH [Enterococcus	WFLDFSDWLSKVP	1782
  	faecalis]	SKLWAE

  Fungi

  gi|1127585|gb|AAA99765.1|	mfa1 gene product	MLSIFAQTTQTSAS	1783
  		EPQQSPTAPQGRDN
  		GSPIGYSSCVVA
  gi|1127592|gbIAAA99771.1|	mfa2 gene product	MLSIFETVAAAAPV	1784
  		TVAETQQASNNEN
  		RGQPGYYCLIA
  gi|11907715|gb|AAG41298.1|	pheromone precursor	PSLPSSPPSLLPPLPL	1785
  	MFalpha1D	LKLLATRRPTLVG
  	[Cryptococcus neoformans	MTLCV
  	var. neoformans]
  gi|13810235|emb|CAC37424.1|	M-factor precursor Mfm1	MDSMANSVSSSSV	1786
  	[Schizosaccharomyces	VNAGNKPAETLNK
  	pombe]	TVKNYTPKVPYMC
  		VIA
  gi|14269436|gb|AAK58071.1|	peptide mating pheromone	MDTFTYVDLAAVA	1787
  AF378295_1	precursor Bbp2-3	AAAVADEVPRDFE
  	[Schizophyllum	DQITDYQSYCIIC
  	commune]
  gi|14269440|gb|AAK58073.1|	peptide mating pheromone	SNVHGWCVVA	1788
  AF378297_1	precursor Bbp2-1
  	[Schizophyllum
  	commune]
  gi|1813600|gb|AAB41859.1|	pheromone precursor	NTTAHGWCVVA	1789
  	Bbp1(1) [Schizophyllum
  	commune]
  gi|24940428|emb|CAD56313.1|	a-pheromone	MQPSTVTAAPKDK	1790
  	[Saccharomyces	TSAEKKDNYIIKGV
  	paradoxus]	FWDPAC VIA
  gi|27549492|gb|AA017258.1|	pheromone phb3.1	GPTWWCVNA	1791
  	[Coprinopsis cinerea]
  gi|27549494|gb|AA017259.1|	pheromone phb3.2	SGPTWFCIIQ	1792
  	[Coprinopsis cinerea]
  gi|27752314|gb|AA019469.1|	pheromone protein a	FTAIFSTLSSSVASK	1793
  	pecursor [Cryptococcus	TDAPRNEEAYSSG
  	neoformans var. grubii] NSP
  gi|2865510|gb|AACO2682.1|	MAT-1 pheromone	MFSIFAQPAQTSVS	1794
  	[Ustilago hordei]	ETQESPANHGANP
  		GKSGSGLGYSTCV
  		VA
  gi|3023372|sp|P78742.1|BB11_	RecName: Full = Mating-	NTTAHGWCVVA	1795
  SCHCO	type pheromone BBP1(1);
  	Flags: Precursor
  gi|3025079|sp|P56508.1|SNA2	RecName: Full = Protein	SDDNYGSLA	1796
  	YEAST SNA2
  gi|37626077|gb|AAQ96360.1|	pheromone precursor Phb3	NGLTFWCVIA	1797
  	B5 [Coprinopsis cinerea]
  gi|37626081|gb|AAQ96362.1|	pheromone precursor	PSWFCVIA	1798
  	Phb3.2 B45 [Coprinopsis
  	cinerea]
  gi|37626083|gb|AAQ96363.1|	pheromone precursor	ASWFCTIA	1799
  	Phb3.1 B47 [Coprinopsis
  	cinerea]
  gi|37961432|gb|AAP57503.1|	5te3-like pheromone	PHHKIANASDKRR	1800
  	receptor [Thanatephorus	RMYFEIFMCAVL
  	cucumeris]
  gi|400250|sp|P31962.1|MFA1_	RecName: Full = A1-	MLSIFAQTTQTSAS	1801
  USTMA	specific pheromone;	EPQQSPTAPQGRDN
  	AltName: Full = Mating	GSPIGYSSCVVA
  	factor A1
  gi|400251|sp|P31963.1|MFA2_	RecName: Full = A2-	MLSIFETVAAAAPV	1802
  USTMA	specific pheromone;	TVAETQQASNNEN
  	AltName: Full = Mating	RGQPGYYCLIA
  	factor A2
  gi|41209131|gb|AAR99617.1|	lipopeptide mating	SLTYAWCVVA	1803
  	pheromone precursor
  	Bap2(3) [Schizophyllum
  	commune]
  gi|41209146|gb|AAR99650.1|	lipopeptide mating	TSMAHAWCVVA	1804
  	pheromone precursor
  	Bap3(2) [Schizophyllum
  	commune]
  gi|41209149|gb|AAR99653.1|	lipopeptide mating	GYCVVA	1805
  	pheromone precursor
  	Bbp2(8) [Schizophyllum
  	commune]
  gi|46098187|gb|EAK83420.1|	MFA1_USTMA A1-	MLSIFAQTTQTSAS	1806
  	SPECIFIC PHEROMONE	EPQQSPTAPQGRDN
  	(MATING FACTOR A1)	GSPIGYSSCVVA
  	[Ustilago maydis 521]
  gi|546861|gb|AAB30833.1|	M-factor mating	MDSMANTVSSSVV	1807
  	pheromone	NTGNKPSETLNKT
  	[Schizosaccharomyces	VKNYTPKVPYMCV
  	pombe]	IA
  gi|5917793|gb|AAD56043.1|	pheromone Mfa2	MFSLFETVAAAVK	1808
  AF184069_1	[Ustilago hordei]	VVSAAEPEHAPTNE
  		GKGEPAPYCIIA
  gi|6014618|gb|AAF01424.1|	Phb3.2.42 [Coprinus	LTWFCVIA	1809
  AF186389_1	cinereus]
  gi|68266363|gb|AAY88882.1|	putative pheromone	LREKRRRRWFEAF	1810
  	receptor STE3.4	MGFGL
  	[Coprinellus disseminatus]
  gi|71012805|ref|XP_758529.1|	A1-specific pheromone	MLSIFAQTTQTSAS	1811
  	[Ustilago maydis 521]	EPQQSPTAPQGRDN
  		GSPIGYSSCVVA
  gi|72414834|emb|CAI59748.1|	mating factor a1.3	MDALTLFAPVSLG	1812
  	[Sporisorium reilianum]	AVATEQAPVDEER
  		PNRQTFPWIGCVV
  		A
  gi|72414854|emb|CAI59758.1|	mating factor a2.1	MFIFESVVASVQAV	1813
  	[Sporisorium reilianum]	SVAEQDQTPVSEG
  		RGKPAVYCTIA
  gi|11275871gbIAAA99767.1|	rba1 gene product	PWMSLLFSFLALLA	1814
  		LILPKLSKDDPLGL
  		TRQPR
  gi|151941959|gb|EDN60315.1|	pheromone-regulated	ASISLIMEGSANIEA	1815
  	membraneprotein	VGKLVWLAAALPL
  	AFI
  	[Saccharomyces cerevisiae
  	YJM789]
  gi|3025095|sp907549.1|SNA4_	Protein SNA4	ARNVYPSVETPLLQ	1816
  YEAST		GAAPHDNKQSLVE
  		SPPPYVP
  gi|73921293|sp|Q08245.3|ZEO1_	RecName: Full = Protein	FLKKLNRKIASIFN	1817
  YEAST	ZEO1; AltName:
  	Ful1 = Zeocin resistance
  	protein 1
  gi|74644573|sp|Q9P305.3|IGO2_	RecName: Full = Protein	DSISRQGSISSGPPP	1818
  YEAST	IGO2	RSPNK
  	EDF (E. coli)	NNWNN	1819

• v. Targeting Enhancers/Opsonins
• In certain embodiments compositions are contemplated that incorporate a targeting enhancer (e.g., an opsonin) along with one or more targeting moieties (e.g., targeting peptides). Targeting enhancers include moieties that increase binding affinity, and/or binding specificity, and/or internalization of a moiety by the target cell/microorganism.
• Accordingly, in certain embodiments, a targeting moiety and/or a targeted antimicrobial molecule comprise a peptide, with the desired level of binding specificity and/or avidity, attached (e.g., conjugated) to an opsonin. When bound to a target cell through the targeting peptide, the opsonin component encourages phagocytosis and destruction by resident macrophages, dendritic cells, monocytes, or PMNs. Opsonins contemplated for conjugation can be of a direct or indirect type.
• Direct opsonins include, fore example, any bacterial surface antigen, PAMP (pathogen-associated molecular pattern), or other molecule recognized by host PRRs (pathogen recognizing receptors). Opsonins can include, but are not limited to, bacterial protein, lipid, nucleic acid, charbohydrate and/or oligosaccharide moieties.
• In certain embodiments opsonins include, but are not limited to, N-acetyl-D-glucosamine (GlcNAc), N-acetyl-D-galactosamine (GlaNAc), N-acetylglucosamine-containing muramyl peptides, NAG-muramyl peptides, NAG-NAM, peptidoglycan, teichoic acid, lipoteichoic acid, LPS, o-antigen, mannose, fucose, ManNAc, galactose, maltose, glucose, glucosamine, sucrose, mannosamine, galactose-alpha-1,3-galactosyl-beta-1,4-N-acetyl glucosamine, or alpha-1,3-gal-gal, or other sugars.
• In certain embodiments, opsonins include indirect opsonins. Indirect opsonins function through binding to a direct opsonin already present. For example an Fc portion of an antibody, a sugar-binding lectin protein (example MBL), or host complement factors (example C3b, C4b, iC3b).
• In certain embodiments the opsonin is to galactose-alpha-1,3-galactosyl-beta-1,4-N-acetyl glucosamine, or alpha-1,3-gal-gal.
• Other examples of opsonin molecules include, but are not limited to antibodies (e.g., IgG and IgA), components of the complement system (e.g., C3b, C4b, and iC3b), mannose-binding lectin (MBL) (initiates the formation of C3b), and the like.
• Methods of coupling an opsonin to a targeting moiety are well known to those of skill in the art (see, e.g., discussion below regarding attachment of effectors to targeting moieties).
• B) Effectors.
• Any of a wide number of effectors can be coupled to targeting moieties as described herein to preferentially deliver the effector to a target organism and/or tissue. Illustrative effectors include, but are not limited to detectable labels, small molecule antibiotics, antimicrobial peptides, porphyrins or other photosensitizers, epitope tags/antibodies for use in a pretargeting protocol, agents that physically disrupt the extracellular matrix within a community of microorganisms, microparticles and/or microcapsules, nanoparticles and/or nanocapsules, “carrier” vehicles including, but not limited to lipids, liposomes, dendrimers, cholic acid-based peptide mimics or other peptide mimics, steroid antibiotics, and the like.
• i. Detectable Labels.
• In certain embodiments chimeric moieties are provided comprising a targeting moiety (e.g., as described in Table 3) attached directly or through a linker to a detectable label. Such chimeric moieties are effective for detecting the presence and/or quantity, and/or location of the microorganism(s) to which the targeting moiety is directed. Similarly these chimeric moieties are useful to identify cells and/or tissues and/or food stuffs and/or other compositions that are infected with the targeted microorganism(s).
• Detectable labels suitable for use in such chimeric moieties include any composition detectable by spectroscopic, photochemical, biochemical, immunochemical, electrical, optical, or chemical means. Illustrative useful labels include, but are not limited to, biotin for staining with labeled streptavidin conjugates, avidin or streptavidin for labeling with biotin conjugates fluorescent dyes (e.g., fluorescein, texas red, rhodamine, green fluorescent protein, and the like, see, e.g., Molecular Probes, Eugene, Oreg., USA), radiolabels (e.g., ³H, ¹²⁵I, ³⁵S, ¹⁴C, ³²P, ⁹⁹Tc, ²⁰³Pb, ⁶⁷Ga, ⁶⁸Ga, ⁷²As, ¹¹¹In, ^113mIn, ⁹⁷Ru, ⁶²Cu, ⁶⁴¹Cu, ⁵²Fe, ^52mMn, ⁵¹Cr, ¹⁸⁶Re, ¹⁸⁸Re, ⁷⁷As, ⁹⁰Y, ⁶⁷Cu, ¹⁶⁹Er, ¹²¹Sn, ¹²⁷Te, ¹⁴²Pr, ¹⁴³Pr, ¹⁹⁸Au, ¹⁹⁹Au, ¹⁶¹Tb, ¹⁰⁹Pd, ¹⁶⁵Dy, ¹⁴⁹Pm, ¹⁵¹Pm, ¹⁵³Sm, ¹⁵⁷Gd, ¹⁵⁹Gd, ¹⁶⁶Ho, ¹⁷²Tm, ¹⁶⁹Yb, ¹⁷⁵Yb, ¹⁷⁷Lu, ¹⁰⁵Rh, ¹¹¹Ag, and the like), enzymes (e.g., horse radish peroxidase, alkaline phosphatase and others commonly used in an ELISA), various colorimetric labels, magnetic or paramagnetic labels (e.g., magnetic and/or paramagnetic nanoparticles), spin labels, radio-opaque labels, and the like. Patents teaching the use of such labels include, for example, U.S. Pat. Nos. 3,817,837; 3,850,752; 3,939,350; 3,996,345; 4,277,437; 4,275,149; and 4,366,241.
• It will be recognized that fluorescent labels are not to be limited to single species organic molecules, but include inorganic molecules, multi-molecular mixtures of organic and/or inorganic molecules, crystals, heteropolymers, and the like. Thus, for example, CdSe—CdS core-shell nanocrystals enclosed in a silica shell can be easily derivatized for coupling to a biological molecule (Bruchez et al. (1998) Science, 281: 2013-2016). Similarly, highly fluorescent quantum dots (zinc sulfide-capped cadmium selenide) have been covalently coupled to biomolecules for use in ultrasensitive biological detection (Warren and Nie (1998) Science, 281: 2016-2018).
• In various embodiments spin labels are provided by reporter molecules with an unpaired electron spin which can be detected by electron spin resonance (ESR) spectroscopy. Illustrative spin labels include organic free radicals, transitional metal complexes, particularly vanadium, copper, iron, and manganese, and the like. Exemplary spin labels include, for example, nitroxide free radicals.
• Means of detecting such labels are well known to those of skill in the art. Thus, for example, where the label is a radioactive label, means for detection include a scintillation counter or photographic film as in autoradiography. Where the label is a fluorescent label, it may be detected by exciting the fluorochrome with the appropriate wavelength of light and detecting the resulting fluorescence, e.g., by microscopy, visual inspection, via photographic film, by the use of electronic detectors such as charge coupled devices (CCDs) or photomultipliers and the like. Similarly, enzymatic labels may be detected by providing appropriate substrates for the enzyme and detecting the resulting reaction product. Finally, simple colorimetric labels may be detected simply by observing the color associated with the label.
• ii. Antibiotics.
• In certain embodiments chimeric moieties are provided comprising a targeting moiety (e.g. as described in Table 3) attached directly or through a linker to a small molecule antibiotic and/or to a carrier (e.g., a lipid or liposome, a polymer, etc.) comprising a small molecule antibiotic. Illustrative antibiotics are shown in Table 13.

• TABLE 13
  Illustrative antibiotics for use in the chimeric moieties described herein.

  Class	Generic Name	BRAND NAME
  Aminoglycosides	Amikacin	AMIKIN ®
  	Gentamicin	GARAMYCIN ®
  	Kanamycin	KANTREX ®
  	Neomycin
  	Netilmicin	NETROMYCIN ®
  	Streptomycin
  	Tobramycin	NEBCIN ®
  	Paromomycin	HUMATIN ®
  Carbacephem	Loracarbef	LORABID ®
  Carbapenems	Ertapenem	INVANZ ®
  	Doripenem	FINIBAX ®
  	Imipenem/Cilastatin	PRIMAXIN ®
  	Meropenem	MERREM ®
  Cephalosporins	Cefadroxil	DURICEF ®
  (First generation)	Cefazolin	ANCEF ®
  	Cefalotin or Cefalothin	KEFLIN ®
  	Cefalexin	KEFLEX ®
  Cephalosporins	Cefaclor	CECLOR ®
  (Second	Cefamandole	MANDOLE ®
  generation)	Cefoxitin	MEFOXIN ®
  	Cefprozil	CEFZIL ®
  	Cefuroxime	CEFTIN, ZINNAT ®
  Cephalosporins	Cefixime	SUPRAX ®
  (Third	Cefdinir	OMNICEF ®
  generation)	Cefditoren	SPECTRACEF ®
  	Cefoperazone	CEFOBID ®
  	Cefotaxime	CLAFORAN ®
  	Cefpodoxime
  	Ceftazidime	FORTAZ ®
  	Ceftibuten	CEDAX ®
  	Ceftizoxime
  	Ceftriaxone	ROCEPHIN ®
  Cephalosporins	Cefepime	MAXIPIME ®
  (Fourth
  generation)
  Cephalosporins	Ceftobiprole
  (Fifth generation)
  Glycopeptides	Teicoplanin
  	Vancomycin	VANCOCIN ®
  Macrolides
  Azithromycin	Zithromax
  Clarithromycin	Biaxin
  Dirithromycin
  Erythromycin	Erythocin, Erythroped
  Roxithromycin
  Troleandomycin
  Telithromycin	Ketek
  Monobactams	Aztreonam
  Penicillins	Amoxicillin	NOVAMOX ®, AMOXIL ®
  	Ampicillin
  	Azlocillin
  	Carbenicillin
  	Cloxacillin
  	Dicloxacillin
  	Flucloxacillin	FLOXAPEN ®
  	Mezlocillin
  	Meticillin
  	Nafcillin
  	Oxacillin
  	Penicillin
  	Piperacillin
  	Ticarcillin
  Polypeptides	Bacitracin
  	Colistin
  	Polymyxin B
  Quinolones	Mafenide
  	Prontosil (archaic)
  	Sulfacetamide
  	Sulfamethizole
  	Sulfanilimide (archaic)
  	Sulfasalazine
  	Sulfisoxazole
  	Trimethoprim	BACTRIM ®
  	Trimethoprim-
  	Sulfamethoxazole (Co-
  	trimoxazole)
  	(TMP-SMX)
  Tetracyclines	Demeclocycline
  	Doxycycline	VIBRAMYCIN ®
  	Minocycline	MINOCIN ®
  	Oxytetracycline	TERRACIN ®
  	Tetracycline	SUMYCIN ®
  Natural products	Antimicrobial herbal
  	extracts
  	Essential oils
  	Farnesol
  	Licorice root extracts
  	Glycyrrhizol A
  	Glycyrrhizol B
  	6,8-diisoprenyl-5,7,4′-
  	trihydroxyisoflavone
  Others	Arsphenamine	SALVARSAN ®
  	Chloramphenicol	CHLOROMYCETIN ®
  	Clindamycin	CLEOCIN ®
  	Lincomycin
  	Ethambutol
  	Fosfomycin
  	Fusidic acid	FUCIDIN ®
  	Furazolidone
  	Isoniazid
  	Linezolid	ZYVOX ®
  	Metronidazole	FLAGYL ®
  	Mupirocin	BACTROBAN ®
  	Nitrofurantoin	MACRODANTIN ®,
  		MACROBID ®
  	Platensimycin
  	Pyrazinamide
  	Quinupristin/	SYNCERCID ®
  	Dalfopristin
  	Rifampin or
  	Rifampicin
  	Tinidazole
  	Artemisinin
  Antifungals	Amphotericin B
  	Anidulafungin
  	Caspofungin acetate
  	Clotrimazole
  	Fluconazole
  	Flucytosine
  	Griseofulvin
  	Itraconazole
  	Ketoconazole
  	Micafungin
  	Miconazole
  	Nystatin
  	Pentamidine
  	Posaconazole
  	Terbinafine
  	Voriconazole
  Antimycobiotics	Aminosalicylic Acid
  	Capreomycin
  	Clofazimine
  	Cycloserine
  	Ethionamide
  	Rifabutin
  	Rifapentine
  Antivirals	Abacavir
  	Acyclovir
  	Adefovir
  	Amantadine
  	Atazanavir
  	Cidofovir
  	Darunavir
  	Didanosine
  	Docosanol
  	Efavirenz
  	Emtricitabine
  	Enfuvirtide
  	Entecavir
  	Etravirine
  	Famciclovir
  	Fomivirsen
  	Fosamprenavir
  	Foscarnet
  	Ganciclovir
  	Idoxuridine
  	Indinavir
  	Interferon alpha
  	Lamivudine
  	Lopinavir/ritonavir
  	Maraviroc
  	Nelfinavir
  	Nevirapine
  	Oseltamivir
  	Penciclovir
  	Peramivir
  	Raltegravir
  	Ribavirin
  	Rimantadine
  	Ritonavir
  	Saquinavir
  	Stavudine
  	Telbivudine
  	Tenofovir
  	Tipranavir
  	Trifluridine
  	Valacyclovir
  	Valganciclovir
  	Zanamivir
  	Zidovudine
  Anti-parasitics	Albendazole
  	Artesunate
  	Atovaquone
  	Bephenium
  	hydroxynaphthoate
  	Chloroquine
  	Dapsone
  	Diethyl-carbamazine
  	Diloxanide furoate
  	Eflornithine
  	Emetine HCl
  	Furazolidone
  	Ivermectin
  	Lindane
  	Mebendazole
  	Mefloquine
  	Melarsoprol
  	Miltefosine
  	Niclosamide
  	Nifurtimox
  	Nitazoxanide
  	Oxamniquine
  	Paromomycin
  	Permethrin
  	Piperazine
  	Praziquantel
  	Primaquine
  	Pyrantel pamoate
  	Pyrimethamine
  	Proguanil
  	Quinacrine HCl
  	Quinidine
  	Quinine
  	Sodium Stibogluconate
  	Spiramycin
  	Thiabendazole
  	Tinidazole

• iii. Porphyrins and Non-Porphyrin Photosensitizers.
• In certain embodiments, porphyrins and other photosensitizers can be used as targeting moieties and/or as effectors in the methods and compositions of this invention. A photosensitizer is a drug or other chemical that increases photosensitivity of the organism (e.g., bacterium, yeast, fungus, etc.). As targeting moieties the photosensitizers (e.g., porphyrins) are preferentially uptaken by the target microorganisms and thereby facilitate delivery of the chimeric moiety to the target microorganism.
• As effectors, photosensitizers can be useful in photodynamic antimicrobial chemotherapy (PACT). In various embodiments PACT utilizes photosensitizers and light (e.g., visible, ultraviolet, infrared, etc.) in order to give a phototoxic response in the target organism(s), often via oxidative damage.
• Currently, the major use of PACT is in the disinfection of blood products, particularly for viral inactivation, although more clinically-based protocols are used, e.g. in the treatment of oral infection or topical infection. The technique has been shown to be effective in vitro against bacteria (including drug-resistant strains), yeasts, viruses, parasites, and the like.
• Attaching a targeting moiety (e.g., a targeting peptide) to the photosensitizer, e.g., as described herein, provides a means of specifically or preferentially targeting the photosensitizer(s) to particular species or strains(s) of microorganism.
• A wide range of photosensitizers, both natural and synthetic are known to those of skill in the art (see, e.g., Wainwright (1998) J. Antimicrob. Chemotherap. 42: 13-28). Photosensitizers are available with differing physicochemical make-up and light-absorption properties. In various embodiments photosensitizers are usually aromatic molecules that are efficient in the formation of long-lived triplet excited states. In terms of the energy absorbed by the aromatic-system, this again depends on the molecular structure involved. For example, furocoumarin photosensitizers (psoralens) absorb relatively high energy ultraviolet (UV) light (c. 300-350 nm), whereas macrocyclic, heteroaromatic molecules such as the phthalocyanines absorb lower energy, near-infrared light.
• Illustrative photosensitizers include, but are not limited to porphyrinic macrocyles (especially porphyrins, chlorines, etc., see, e.g., FIGS. 1 and 2). In particular, metalloporphyrins, particularly a number of non-iron metalloporphyrins mimic haem in their molecular structure and are actively accumulated by bacteria via high affinity haem-uptake systems. The same uptake systems can be used to deliver antibiotic-porphyrin and antibacterial-porphyrin conjugates. Illustrative targeting porphyrins suitable for this purpose are described in U.S. Pat. No. 6,066,628 and shown herein in FIGS. 1 and 2.
• Illustrative examples of targeted porphyrins are described in Example 5 and associated figures and in FIG. 13.
• For example, certain artificial (non-iron) metalloporphyrins (MPs) (Ga-IX, Mn-IX,) are active against Gram-negative and Gram-positive bacteria and acid-fast bacilli (e.g., Y. enterocolitica, N. meningitides, S. marcescens, E. coli, P. mirabilis, K pneumoniae, K. oxytoca, Ps. aeruginosa, C. freundii, E. aerogenes, F. menigosepticum, S. aureus, B. subtilis, S. pyogenes A, E. faecalis, M. smegmatis, M. bovis, M. tuber., S. crevisiae) as described in Tables 1-5 of U.S. Pat. No. 6,066,628. These MPs can be used as targeting moieties against these microorganisms.
• Similarly, some MPs are also growth-inhibitory against yeasts, indicating their usefulness targeting moieties to target Candida species (e.g., Candida albicans, C. krusei, C. pillosus, C. glabrata, etc.) and other mycoses including but not limited to those caused by as Trichophyton, Epidermophyton, Histoplasma, Aspergillus, Cryptococcus, and the like.
• Other photosensitizers include, but are not limited to cyanines (see, e.g., FIG. 6) and phthalocyanines (see, e.g., FIG. 4), azines (see, e.g., FIG. 5) including especially methylene blue and touidine blue, hypericin (see, e.g., FIG. 8), acridines (see, e.g., FIG. 9) including especially Rose Bengal (see, e.g., FIG. 10), crown ethers (see, e.g., FIG. 11), and the like. In certain embodiments, the photosensitizers include tin chlorin 6 and related compounds (e.g., other chlorines and tin porphyrins).
• Another light-activated compound is cucumin (see, FIG. 12).
• In certain embodiments the photosensitizers are toxic or growth inhibitors without light activation. For example, some non-iron metalloporphyrins (MPs) (see, e.g., FIGS. 1 and 2 herein) possess a powerful light-independent antimicrobial activity. In addition, haemin, the most well known natural porphyrin, possesses a significant antibacterial activity that can augmented by the presence of physiological concentrations of hydrogen peroxide or a reducing agent.
• Typically, when activated by light, the toxicity or growth inhibition effect is substantially increased. Typically, they generate radical species that affect anything within proximity. In certain embodiments to get the best selectivity from targeted photosensitizers, anti-oxidants can be used to quench un-bound photosensitizers, limiting the damage only to cells where the conjugates have accumulated due to the targeting peptide. The membrane structures of the target cell act as the proton donors in this case.
• In typical photodynamic antimicrobial chemotherapy (PACT) the targeted photosensitizer is “activated by the application of a light source (e.g., a visible light source, an ultraviolate light source, an infrared light source, etc.). PACT applications however need not be limited to topical use. Regions of the mouth, throat, nose, sinuses are readily illuminated. Similarly regions of the gut can readily be illuminated using endoscopic techniques. Other internal regions can be illumined using laparoscopic methods or during other surgical procedures. For example, in certain embodiments involving the insertion or repair or replacement of an implantable device (e.g., a prosthetic device) it contemplated that the device can be coated or otherwise contacted with a chimeric moiety comprising a targeting moiety attached to a photosensitizer as described herein. During the surgical procedure and/or just before closing, the device can be illuminated with an appropriate light source to activate the photosensitizer.
• The targeted photosensitizers and uses thereof described herein are illustrative and not to be limiting. Using the teachings provided herein, other targeted photosensitizers and uses thereof will be available to one of skill in the art.
• iv. Antimicrobial Peptides.
• In certain embodiments, the effector can comprise one or more antimicrobial peptides or compound antimicrobial peptides, e.g., as described above. Numerous antimicrobial peptides are well known to those of skill in the art.
• In certain embodiments the antimicrobial peptides comprise one or more amino acid sequences described above (e.g., one or more domains comprising amino acid sequences in Tables 4 and/or 5) and/or one or more of the amino acid sequences shown in Table 14. In certain embodiments the antimicrobial peptides comprise one or more amino acid sequences described in the “Collection of Anti-Microbial Peptides” (CAMP) an online database developed for advancement the understanding of antimicrobial peptides (see, e.g., Thomas et al. (2009) Nucleic Acids Research, 2009, 1-7.doi:10.1093/nar/gkp1021) available at www.bicnirrh.res.in/antimicrobial.

• TABLE 14
  Other illustrative antimicrobial peptides. AP numbers refer to ID in
  antimicrobial peptide database (http://aps.unmc.edu/AP/main.php).

  			SEQ ID
  	Effector	Structure/Sequence	No
  AP00274	1BH4, Circulin A	GIPCGESCVWIPCISAALGCSCKNK	1820
  	(CirA, plant	VCYRN
  	cyclotides,XXC,
  	ZZHp)
  AP00036	1BNB, Beta-	DFASCHTNGGICLPNRCPGHMIQIG	1821
  	defensin 1 (cow)	ICFRPRVKCCRSW
  AP00047	1BNB, Bovine	GPLSCGRNGGVCIPIRCPVPMRQIG	1822
  	neutrophil beta-	TCFGRPVKCCRSW
  	defensin 12
  	(BNBD-12, cow)
  AP00428	1C01, MiAMP1	SAFTVWSGPGCNNRAERYSKCGCS	1823
  	(Macadamia	AIHQKGGYDFSYTGQTAALYNQA
  	integrifolia	GCSGVAHTRFGSSARACNPFGWKS
  	antimicrobial	IFIQC
  	peptide 1, plant)
  AP00154	1CIX, Tachystatin	YSRCQLQGFNCVVRSYGLPTIPCC	1824
  	A2 (Horseshoe	RGLTCRSYFPGSTYGRCQRY
  	crabs, Crustacea,
  	BBS)
  AP00145	1CW5,	VNYGNGVSCSKTKCSVNWGQAFQ	1825
  	Carnobacteriocin	ERYTAGINSFVSGVASGAGSIGRRP
  	B2 (CnbB2, class
  	IIA
  	bacteriocin, bacteria)
  AP00153	1CZ6, Androctonin	RSVCRQIKICRRRGGCYYKCTNRP	1826
  	(scorpions)	Y
  AP00152	1D6X, Tritrpticin	VRRFPWWWPFLRR	1827
  	(synthetic)
  AP00201	1D7N, Mastoparan	INLKALAALAKKIL	1828
  	(insect)
  AP00140	1D9J, CecropinA-	KWKLFKKIGIGKFLHSAKKF	1829
  	Magainin2 hybrid
  	(synthetic)
  AP00178	1DFN, human	DCYCRIPACIAGERRYGTCIYQGRL	1830
  	alpha Defensin	WAFCC
  	HNP-3 (human
  	neutrophil peptide-
  	3, HNP3, human
  	defensin, ZZHh)
  AP01153	1DQC, Tachycitin	YLAFRCGRYSPCLDDGPNVNLYSC	1831
  	(horseshoe crabs,	CSFYNCHKCLARLENCPKGLHYN
  	Crustacea, BBS)	AYLKVCDWPSKAGCT
  AP00437	1DUM, Magainin 2	GIGKYLHSAKKFGKAWVGEIMNS	1832
  	analog (synthetic)
  AP00451	1E4S, Human beta	DHYNCVSSGGQCLYSACPIFTKIQG	1833
  	defensin 1 (HBD-1,	TCYRGKAKCCK
  	human	defensin)
  AP00149	1EWS, Rabbit	NIPCSCKKYCDPWEVIDGSCGLFNS	1834
  	kidney defensin 1	KYICCREK
  	(RK-1)
  AP00141	1F0E, CecropinA-	KWKLFKKIPKFLHSAKKF	1835
  	Magainin2 Hybrid
  	(P18, synthetic)
  AP00142	1F0G, CecropinA-	KLKLFKKIGIGKFLHSAKKF	1836
  	Magainin2 Hybrid
  	(synthetic)
  AP00143	1FOH, CecropinA-	KAKLFKKIGIGKFLHSAKKF	1837
  	Magainin2 Hybrid
  	(synthetic)
  AP00524	1FD4, Human beta	GIGDPVTCLKSGAICHPVFCPRRYK	1838
  	defensin 2 (HBD-2,	QIGTCGLPGTKCCKKP
  	human defensin,
  	ZZHh)
  AP00438	1FJN, Mussel	GFGCPNNYQCHRHCKSIPGRCGGY	1839
  	Defensin MGD-1	CGGWHRLPCTCYRCG
  AP00155	1FRY, SMAP-29	RGLRRLGRKIAHGVKKYGPTVLRII	1840
  	(SMAP29, sheep	RIAG
  	cathelicidin)
  AP00150	1G89, Indolicidin	ILPWKWPWWPWRR	1841
  	(cow cathelicidin,
  	BBN, ZZHa)
  AP00156	1GR4, Microcin	VGIGTPISFYGGGAGHVPEYF	1842
  	J25, linear
  	(MccJ25,
  	bacteriocin,
  	bacteria)
  AP00151	1HR1, Indolicidin	ILAWKWAWWAWRR	1843
  	P to A mutant
  	(synthetic)
  AP00196	1HU5, Ovispirin-1	KNLRRIIRKIIHIIKKYG	1844
  	(synthetic)
  AP00197	1HU6, Novispirin	KNLRRIIRKGIHIIKKYG	1845
  	G10 (synthetic)
  AP00198	1HU7, Novispirin	KNLRRITRKIIHIIKKYG	1846
  	T7 (synthetic)
  AP00445	1HVZ, Monkey	GFCRCLCRRGVCRCICTR	1847
  	RTD-1 (rhesus
  	theta-defensin-1,
  	minidefensin-1,
  	animal defensin,
  	XXC, BBS, lectin,
  	ZZHa)
  AP00103	li2v, Heliomicin	DKLIGSCVWGAVNYTSDCNGECL	1848
  	variant (Hel-LL,	LRGYKGGHCGSFANVNCWCET
  	synthetic)
  AP00216	lICA, Phormia	ATCDLLSGTGINHSACAAHCLLRG	1849
  	defensin A (insect	NRGGYCNGKGVCVCRN
  	defensin A)
  AP01224	1Jo3, Gramicidin B	VGALAVVVWLFLWLW	1850
  	(bacteria)
  AP01225	ljo4, Gramicidin C	VGALAVVVWLYLWLW	1851
  	(bacteria)
  AP00191	1KFP, Gomesin	ECRRLCYKQRCVTYCRGR	1852
  	(Gm, Spider, XXA)
  AP00283	1KJ6, Huamn beta	GIINTLQKYYCRVRGGRCAVLSCL	1853
  	defensin 3 (HBD-3,	PKEEQIGKCSTRGRKCCRRKK
  	human defensin,
  	ZZHh)
  AP00147	1KV4, Moricin	AKIPIKAIKTVGKAVGKGLRAINIA	1854
  	STAND	VFNFLKPKKRKA
  	(insect, silk moth)
  AP00227	1L4V, Sapecin	ATCDLLSGTGINHSACAAHCLLRG	1855
  	(insect, flesh fly)	NRGGYCNGKAVCVCRN
  AP01161	1L9L, Human	GRDYRTCLTIVQKLKKMVDKPTQ	1856
  	granulysin	RSVSNAATRVCTRGRSRWRDVCR
  	(huGran)	NFMRRYQSRVIQGLVAGETAQQIC
  		EDLRLCIPSTGPL
  AP00026	1LFC,	FKCRRWQWRMKKLGAPSITCVRR	1857
  	Lactoferricin B	AF
  	(LfcinB, cow,
  	ZZHa)
  AP00193	1M4F, human	DTHFPICIFCCGCCHRSKCGMCCKT	1858
  	LEAP-1 (Hepcidin
  	25)
  AP00499	1MAG, Gramicidin	VGALAVVVWLWLWLW	1859
  	A (gA, bacteria)
  AP00403	1MM0, Termicin	ACNFQSCWATCQAQHSIYFRRAFC	1860
  	(termite defensin,	DRSQCKCVFVRG
  	insect defensin)
  AP00194	1MMC, Ac-AMP2	VGECVRGRCPSQFGYCGKSGMCC	1861
  	(plant defensin,	GPKYCGR
  	BBS)
  AP01206	1MQZ, Mersacidin	CTFTLPGGGGVCTLTSECIC	1862
  	(bacteria)
  AP00429	1NKL, Porcine	GYFCESCRKIIQKLEDMVGPQPNE	1863
  	NK-Lysin (pig)	DTVTQAASQVCDKLKILRGLCKKI
  		IVIRSFLRRISWDILTGKKPQAICVDI
  		KICKE
  AP00633	log7, Sakacin P/	KYYGNGVHCGKHSCTVDWGTAIG	1864
  	Sakacin 674 (SakP,	NIGNNAAANWATGGNAGWNK
  	class IIA
  	bacteriocin,
  	bacteria)
  AP00195	1PG1, Protegrin 1	RGGRLCYCRRRFCVCVGR	1865
  	(Protegrin-1, PG-1,
  	pig cathelicidin,
  	XXA, ZZHa,
  	BBBm)
  AP00928	1PXQ, Subtilosin	NKGCATCSIGAACLVDGPIPDFEIA	1866
  	A (XXC, class I	GATGLFGLWG
  	bacteriocin, Gram-
  	positive bacteria)
  AP00480	1Q71, Microcin	VGIGTPIFSYGGGAGHVPEYF	1867
  	J25 (cyclic
  	MccJ25, class I
  	microcins,
  	bacteriocins, Gram-
  	negative bacteria,
  	XXC; BBP)
  AP00211	1RKK,	RRWCFRVCYRGFCYRKCR	1868
  	Polyphemusin I
  	(crabs, Crustacea)
  AP00430	1T51, IsCT	ILGKIWEGIKSLF	1869
  	(Scorpion)
  AP00731	1ut3, Spheniscin-2	SFGLCRLRRGFCARGRCRFPSIPIGR	1870
  	(Sphe-2, penguin	CSRFVQCCRRVW
  	defensin, avian
  	defensin)
  AP00013	1VM5, Aurein 1.2	GLFDIIKKIAESF	1871
  	(frog)
  AP00214	1WO1,	KWCFRVCYRGICYRRCR	1872
  	Tachyplesin I
  	(crabs, Crustacea,
  	XXA, ZZHa)
  AP00644	lxc0, Pardaxin 4	GFFALIPKIISSPLFKTLLSAVGSALS	1873
  	(Pardaxin P-4,	SSGGQE
  	Pardaxin P4, Pa4,
  	flat fish)
  AP00493	1XKM, Distinctin	NLVSGLIEARKYLEQLHRKLKNCK	1874
  	(two chains for	V
  	stability and
  	transport frog)
  AP00420	1XV3, Penaeidin-	HSSGYTRPLRKPSRPIFIRPIGCDVC	1875
  	4d (penaeidin 4,	YGIPSSTARLCCFRYGDCCHL
  	shrimp, Crustacea)
  AP00035	lYTR, Plantaricin	KSSAYSLQMGATAIKQVKKLFKK	1876
  	A (PlnA,	WGW
  	bacteriocin,
  	bacteria)
  AP00166	1Z64, Pleurocidin	GWGSFFKKAAHVGKHVGKAALT	1877
  	(fish)	HYL
  AP00780	1Z6V, Human	GRRRRSVQWCAVSQPEATKCFQW	1878
  	lactoferricin	QRNMRKVRGPPVSCIKRDSPIQCIQ
  		A
  AP00549	1ZFU, Plectasin	GFGCNGPWDEDDMQCHNHCKSIK	1879
  	(fungi, fungal	GYKGGYCAKGGFVCKCY
  	defensin)
  AP00177	IZMH, human	CYCRIPACIAGERRYGTCIYQGRL	1880
  	alpha Defensin	WAFCC
  	HNP-2 (human
  	neutrophil peptide-
  	2, HNP2, human
  	defensin, ZZHh)
  AP00179	1ZMM, human	VCSCRLVFCRRTELRVGNCLIGGV	1881
  	alpha Defensin	SFTYCCTRVD
  	HNP-4 (human
  	neutrophil peptide-
  	4, HNP4, human
  	defensin)
  AP00180	1ZMP, human	QARATCYCRTGRCATRESLSGVCE	1882
  	alpha Defensin	ISGRLYRLCCR
  	HD-5 (HD5,
  	human	defensin)
  AP00181	1ZMQ, human	STRAFTCHCRRSCYSTEYSYGTCT	1883
  	alpha Defensin	VMGINHRFCCL
  	HD-6 (HD6,
  	human	defensin)
  AP00399	1ZRW, Spinigerin	HVDKKVADKVLLLKQLRIMRLLT	1884
  	(insect, termite)	RL
  AP01157	1ZRX, Stomoxyn	RGFRKHFNKLVKKVKHTISETAHV	1885
  	(insect)	AKDTAVIAGSGAAVVAAT
  AP00637	2A2B, Curvacin A/	ARSYGNGVYCNNKKCWVNRGEA	1886
  	sakacin A (CurA,	TQSIIGGMISGWASGLAGM
  	SakA, class IIA
  	bacteriocin,
  	bacteria)
  AP00558	2B68, Cg-Def	GFGCPGNQLKCNNHCKSISCRAGY	1887
  	(Crassostrea gigas	CDAATLWLRCTCTDCNGKK
  	defensin, oyster
  	defensin, animal
  	defensin)
  AP01154	2B9K, LCI	AIKLVQSPNGNFAASFVLDGTKWI	1888
  	(bacteria)	FKSKYYDSSKGYWVGIYEVWDRK
  AP01005	2DCV, Tachystatin	YVSCLFRGARCRVYSGRSCCFGYY	1889
  	B1 (BBS,	CRRDFPGSIFGTCSRRNF
  	horseshoe crabs)
  AP01006	2DCW,	YITCLFRGARCRVYSGRSCCFGYY	1890
  	Tachystatin B1	CRRDFPGSIFGTCSRRNF
  	(BBS, horseshoe
  	crabs)
  AP00275	2ERI, Circulin B	CGESCVFIPCISTLLGCSCKNKVCY	1891
  	(CirB, plant	RNGVIP
  	cyclotides,XXC,
  	ZZHp)
  AP00707	2f3a, LLAA (LL-	RLFDKIRQVIRKF	1892
  	37-derived aurein
  	1.2 analog, retro-
  	FK13, synthetic)
  AP00708	2fbs, FK-13 (FK13,	FKRIVQRIKDFLR	1893
  	NMR-discovered
  	LL-37 core peptide,
  	XXA, ZZHs,
  	synthetic)
  AP00088	2G9L, Gaegurin-4	GILDTLKQFAKGVGKDLVKGAAQ	1894
  	(Gaegurin 4, frog)	GVLSTVSCKLAKTC
  AP01011	2G9P, Latarcin 2a	GLFGKLIKKFGRKAISYAVKKARG	1895
  	(Ltc2a, BBM,	KH
  	spider)
  AP00612	2GDL, Fowlicidin-	LVQRGRFGRFLRKIRRFRPKVTITI	1896
  	2 (chCATH-2, bird	QGSARFG
  	cathelicidin,
  	chicken
  	cathelicidin, BBL)
  AP00402	2GL1, VrD2	KTCENLANTYRGPCFTTGSCDDHC	1897
  	(Vigna radiata	KNKEHLRSGRCRDDFRCWCTRNC
  	defensin 2, plant
  	defensin, mung
  	bean)
  AP00285	2GW9, Cryptdin-4	GLLCYCRKGHCKRGERVRGTCGIR	1898
  	(Crp4, animal	FLYCCPRR
  	defensin, alpha,
  	mouse)
  AP00613	2hfr, Fowlicidin-3	RVKRFWPLVPVAINTVAAGINLYK	1899
  	(chCATH-3, bird	AIRRK
  	cathelicidin,
  	chicken
  	cathelicidin)
  AP01007	2JMY, CM15	KWKLFKKIGAVLKVL	1900
  	(Synthetic)
  AP00728	2jni, Arenicin-2	RWCVYAYVRIRGVLVRYRRCW	1901
  	(marine polychaeta,
  	BBBm)
  AP00473	2j0s, Piscidin 1	FFHHIFRGIVHVGKTIHRLVTG	1902
  	(fish)
  AP01151	2JPJ, Lactococcin	GTWDDIGQGIGRVAYWVGKALGN	1903
  	G-a (chain a, class	LSDVNQASRINRKKKH
  	IIb bacteriocin,
  	bacteria. For chain
  	b, see info)
  AP00757	2jpy, Phylloseptin-	FLSLIPHAINAVSTLVHHF	1904
  	H2 (PLS-H2,
  	Phylloseptin-2, PS-
  	2) (XXA, frog)
  AP00546	2jq0, Phylloseptin-	FLSLIPHAINAVSAIAKHN	1905
  	1 (Phylloseptin-H1,
  	PLS-H1, PS-1,
  	XXA, frog)
  AP00758	2jq1, Phylloseptin-	FLSLIPHAINAVSALANHG	1906
  	3 (Phylloseptin-H3,
  	PLS-H3, PS-3)
  	(XXA, frog)
  AP00727	2jsb, Arenicin-1	RWCVYAYVRVRGVLVRYRRCW	1907
  	(marine polychaeta,
  	BBBm)
  AP00592	2k10, Ranatuerin-	GILSSFKGVAKGVAKDLAGKLLET	1908
  	2CSa (frog)	LKCKITGC
  AP00485	2K38, Cupiennin	GFGALFKFLAKKVAKTVAKQAAK	1909
  	1a (spider)	QGAKYVVNKQME
  AP00310	2K6O, Human LL-	LLGDFFRKSKEKIGKEFKRIVQRIK	1910
  	37 (LL37, human	DFLRNLVPRTES
  	cathelicidin;
  	released by
  	proteinase 3 from
  	its precursor in
  	neutrophils; FALL-
  	39; BBB, BBM,
  	BBP, BBW, BBD,
  	BBL, ZZHh)
  AP00199	2LEU, Leucocin A	KYYGNGVHCTKSGCSVNWGEAFS	1911
  	(LeuA, class Ha	AGVHRLANGGNGFW
  	bacteriocin,
  	bacteria)
  AP00144	2MAG, Magainin 2	GIGKFLHSAKKFGKAFVGEIMNS	1912
  	(frog)
  AP00146	2MLT, Melittin	GIGAVLKVLTTGLPALISWIKRKRQ	1913
  	(insect, ZZHa)	Q
  AP01010	2PCO, Latarcin 1	SMWSGMWRRKLKKLRNALKKKL	1914
  	(Ltc1, BBM,	KGEK
  	spider)
  AP00176	2PM1, human	ACYCRIPACIAGERRYGTCIYQGRL	1915
  	alpha Defensin	WAFCC
  	HNP-1 (human
  	neutrophil peptide-
  	1, HNP1, human
  	defensin, ZZHh)
  AP01158	2RLG, RP-1	ALYKKFKKKLLKSLKRL	1916
  	(synthetic)
  AP00102	8TFV, Thanatin	GSKKPVPHYCNRRTGKCQRM	1917
  	(insect)
  AP00995	A58718, Carnocin	GSEIQPR	1918
  	UI49 (bacteria)
  AP01002	AAC18827,	KSWSLCTPGCARTGSFNSYCC	1919
  	Mutacin III
  	(mutacin 1140,
  	bacteria)
  AP00987	ABI74601, Arasin	SRWPSPGRPRPFPGRPKPIFRPRPCN	1920
  	1 (Crustacea)	CYAPPCPCDRW
  AP01000	CAA63706,	GSGVIPTISHECHMNSFQFVFTCCS	1921
  	variacin
  	(lantibiotic, class I
  	bacteriocin,
  	bacteria)
  AP00361	O15946, Lebocin 4	DLRFWNPREKLPLPTLPPFNPKPIYI	1922
  	(insect, silk moth)	DMGNRY
  AP00343	O16825, Andropin	VFIDILDKMENAIHKAAQAGIGIAK	1923
  	(insect, fruit fly)	PIEKMILPK
  AP00417	O17513,	SIGTAVKKAVPIAKKVGKVAIPIAK	1924
  	Ceratotoxin D	AVLSVVGQLVG
  	(insect, fly)
  AP00435	O18494, Styelin C	GWFGKAFRSVSNFYKKHKTYIHA	1925
  	(sea squirt,	GLSAATLL
  	tunicate, XXA)
  AP00330	O18495, Styelin D	GWLRKAAKSVGKFYYKHKYYIKA	1926
  	(Sea squirt,	AWQIGKHAL
  	tunicate, XXA)
  AP00331	O18495, Styelin E	GWLRKAAKSVGKFYYKHKYYIKA	1927
  	(Sea squirt,	AWKIGRHAL
  	tunicate, XXA)
  AP01001	O54329, Mutacin II	NRWWQGVVPTVSYECRMNSWQH	1928
  	(lantibiotic,	VFTCC
  	mutacin H-29B, J-
  	T8, class I
  	bacteriocin,
  	bacteria)
  AP00342	O81338,	AKCIKNGKGCREDQGPPFCCSGFC	1929
  	Antimicrobial	YRQVGWARGYCKNR
  	peptide 1 (plant)
  AP00373	O96059, Moricin 2	AKIPIKAIKTVGKAVGKGLRAINIA	1930
  	(insect)	STANDVFNFLKPKKRKH
  AP00449	P01190,	SYSMEHFRWGKPV	1931
  	Melanotropin alpha
  	(Alpha-MSH)
  AP00187	P01376,	VVCACRRALCLPRERRAGFCRIRG	1932
  	CORTICOSTATIN	RIHPLCCRR
  	III (MCP-1, rabbit
  	neutrophil peptide
  	1, NP-1) (animal
  	defensin, alpha-
  	defensin, rabbit)
  AP00188	P01377,	VVCACRRALCLPLERRAGFCRIRG	1933
  	CORTICOSTATIN	RIHPLCCRR
  	IV ( MCP-2, rabbit
  	neutrophil defensin
  	2, NP-2, animal
  	defensin, rabbit)
  AP00049	P01505, Bombinin	GIGALSAKGALKGLAKGLAEHFAN	1934
  	(toad)
  AP00139	P01507, Cecropin	KWKLFKKIEKVGQNIRDGIIKAGP	1935
  	A (insect, ZZHa)	AVAVVGQATQIAK
  AP00128	P01509, Cecropin	KWKIFKKIEKVGRNIRNGIIKAGPA	1936
  	B (insect, silk	VAVLGEAKAL
  	moth)
  AP00131	P01511, Cecropin	WNPFKELERAGQRVRDAIISAGPA	1937
  	D (insect, moth)	VATVAQATALAK
  AP00136	P01518, Crabrolin	FLPLILRKIVTAL	1938
  	(insect, XXA)
  AP00183	P04142, Cecropin	RWKIFKKIEKMGRNIRDGIVKAGP	1939
  	B (insect)	AIEVLGSAKAI
  AP00448	P04205,	INLKAIAALAKKLL	1940
  	Mastoparan M
  	(MP-M, insect,
  	XXA)
  AP00234	P06833,	SDEKASPDKHHRFSLSRYAKLANR	1941
  	Seminalplasmin	LANPKLLETFLSKWIGDRGNRSV
  	(SPLN, calcium
  	transporter
  	inhibitor, caltrin,
  	cow)
  AP00314	P07466, Rabbit	VFCTCRGFLCGSGERASGSCTINGV	1942
  	neutrophil peptide	RHTLCCRR
  	5 (NP-5, animal
  	defensin, alpha-
  	defensin)
  AP00189	P07467, Rabbit	VSCTCRRFSCGFGERASGSCTVNG	1943
  	neutrophil peptide	VRHTLCCRR
  	4 (NP-4)
  AP00186	P07468,	GRCVCRKQLLCSYRERRIGDCKIR	1944
  	CORTICOSTATIN	GVRFPFCCPR
  	II (Rabbit
  	neutrophil peptide
  	3b (NP-3b, rabbit)
  AP00185	P07469,	ICACRRRFCPNSERFSGYCRVNGA	1945
  	CORTICOSTATIN	RYVRCCSRR
  	I (rabbit)
  AP00217	P07469, Rabbit	GICACRRRFCPNSERFSGYCRVNG	1946
  	neutrophil defensin	ARYVRCCSRR
  	3a (NP-3a, animal
  	defensin, alpha-
  	defensin)
  AP00067	P07493,	SKITDILAKLGKVLAHV	1947
  	Bombolitin II
  	(insect, bee)
  AP00068	P07494,	IKIMDILAKLGKVLAHV	1948
  	Bombolitin III
  	(insect, bee)
  AP00069	P07495,	INIKDILAKLVKVLGHV	1949
  	Bombolitin IV
  	(insect, bee)
  AP00070	P07496,	INVLGILGLLGKALSHL	1950
  	Bombolitin V
  	(insect, bee)
  AP00236	P07504, Pyrularia	KSCCRNTWARNCYNVCRLPGTISR	1951
  	thionin (Pp-TH,	EICAKKCDCKIISGTTCPSDYPK
  	plant)
  AP00230	P08375, Sarcotoxin	GWLKKIGKKIERVGQHTRDATIQG	1952
  	IA (insect, flesh	LGIAQQAANVAATAR
  AP00231	P08376, Sarcotoxin	GWLKKIGKKIERVGQHTRDATIQV	1953
  	IB (insect, flesh	IGVAQQAANVAATAR
  AP00232	P08377, Sarcotoxin	GWLRKIGKKIERVGQHTRDATIQV	1954
  	IC (insect, flesh	LGIAQQAANVAATAR
  AP00066	P10521,	IKITTMLAKLGKVLAHV	1955
  	Bombolitin I
  	(insect, bee)
  AP00206	P10946, Lantibiotic	WKSESLCTPGCVTGALQTCFLQTL	1956
  	subtilin (class I	TCNCKISK
  	bacteriocin,
  	bacteria)
  AP00312	P11477, Cryptdin-2	LRDLVCYCRARGCKGRERMNGTC	1957
  	(Crp2, animal	RKGHLLYMLCCR
  	defensin, alpha,
  	mouse)
  AP00205	P13068, Nisin A	ITSISLCTPGCKTGALMGCNMKTA	1958
  	(lantibiotic, class I	TCHCSIHVSK
  	bacteriocin,
  	bacteria)
  AP00215	P14214,	RWCFRVCYRGICYRKCR	1959
  	Tachyplesin II
  	(crabs, Crustacea)
  AP00212	P14216,	RRWCFRVCYKGFCYRKCR	1960
  	Polyphemusin II
  	(crabs, Crustacea,
  	XXA, ZZHa.
  	Derivatives: T22)
  AP00134	P14661, Cecropin	SWLSKTAKKLENSAKKRISEGIAIA	1961
  	P1 (pig)	IQGGPR
  AP00011	P14662,	WNPFKELERAGQRVRDAVISAAPA	1962
  	Bactericidin B2	VATVGQAAAIARG
  	(insect)
  AP00032	P14663,	WNPFKELERAGQRVRDAIISAGPA	1963
  	Bactericidin B-3	VATVGQAAAIARG
  	(insect)
  AP00033	P14664,	WNPFKELERAGQRVRDAIISAAPA	1964
  	Bactericidin B-4	VATVGQAAAIARG
  	(insect)
  AP00034	P14665,	WNPFKELERAGQRVRDAVISAAA	1965
  	Bactericidin B-5P	VATVGQAAAIARG
  	(insect)
  AP00125	P14666, Cecropin	RWKIFKKIEKVGQNIRDGIVKAGP	1966
  	(insect, silk moth)	AVAVVGQAATI
  AP00002	P15450,	YVPLPNVPQPGRRPFPTFPGQGPFN	1967
  	ABAECIN	PKIKWPQGY
  	(insect,
  	honeybee)
  AP00505	P15516, human	DSHAKRHHGYKRKFHEKHHSHRG	1968
  	Histatin 5 (ZZHs;	Y
  	derivatives Dh-5)
  AP00520	P15516, human	DSHAKRHHGYKRKFHEKHHSHRG	1969
  	Histatin 3	YRSNYLYDN
  AP00523	P15516, human	KFHEKHHSHRGY	1970
  	Histatin 8
  AP00226	P17722, Royalisin	VTCDLLSFKGQVNDSACAANCLSL	1971
  	(insect, honeybee)	GKAGGHCEKVGCICRKTSFKDLW
  		DKRF
  AP00213	P18252,	KWCFRVCYRGICYRKCR	1972
  	Tachyplesin III
  	(horseshoe crabs,
  	Crustacea)
  AP00233	P18312, Sarcotoxin	GWIRDFGKRIERVGQHTRDATIQTI	1973
  	ID (insect, flesh	AVAQQAANVAATLKG
  AP00207	P19578, Lantibiotic	TAGPAIRASVKQCQKTLKATRLFT	1974
  	PEPS (class I	VSCKGKNGCK
  	bacteriocin,
  	bacteria)
  AP00009	P19660,	RFRPPIRRPPIRPPFYPPFRPPIRPPIF	1975
  	BACTENECIN 5	PPIRPPFRPPLGPFP
  	(bac5, cow
  	cathelicidin)
  AP00010	P19661,	RRIRPRPPRLPRPRPRPLPFPRPGPR	1976
  	BACTENECIN 7	PIPRPLPFPRPGPRPIPRPLPFPRPGP
  	(bac7, cow	RPIPRPL
  	cathelicidin)
  AP00200	P21564,	LKLKSIVSWAKKVL	1977
  	Mastoparan B
  	(MP-B, insect,
  	XXA)
  AP00005	P21663, Andropin	VFIDILDKVENAIHNAAQVGIGFAK	1978
  	(insect, fly)	PFEKLINPK
  AP00008	P22226, Cyclic	RLCRIVVIRVCR	1979
  	dodecapeptide
  	(cow cathelicidin)
  AP01205	P23826, Lactocin S	STPVLASVAVSMELLPTASVLYSD	1980
  	(XXD3, bacteria)	VAGCFKYSAKHHC
  AP00239	P24335, XPF (the	GWASKIGQTLGKIAKVGLKELIQP	1981
  	xenopsin precursor	K
  	fragment, African
  	clawed frog)
  AP00235	P25068, Bovine	NPVSCVRNKGICVPIRCPGSMKQIG	1982
  	tracheal	TCVGRAVKCCRKK
  	antimicrobial
  	peptide (TAP, cow)
  AP00418	P25230, CAP18	GLRKRLRKFRNKIKEKLKKIGQKIQ	1983
  	(rabbit cathelicidin,	GFVPKLAPRTDY
  	BBL)
  AP00203	P25403, Mj-AMP1	QCIGNGGRCNENVGPPYCCSGFCL	1984
  	(Mj AMP1, plant	RQPGQGYGYCKNR
  	defensin)
  AP00202	P25404, Mj-AMP2	CIGNGGRCNENVGPPYCCSGFCLR	1985
  	(MjAMP2, plant	QPNQGYGVCRNR
  	defensin)
  AP00138	P28310, Cryptdi n-3	LRDLVCYCRKRGCKRRERMNGTC	1986
  	(Crp3, animal	RKGHLMYTLCCR
  	defensin, alpha,
  	mouse)
  AP00184	P28794, MBP-1	RSGRGECRRQCLRRHEGQPWETQ	1987
  	(plant)	ECMRRCRRRG
  AP00050	P29002, Bombinin-	GIGASILSAGKSALKGLAKGLAEHF	1988
  	like peptide 1	AN
  	(BLP-1, toad)
  AP00051	P29003, Bombinin-	GIGSAILSAGKSALKGLAKGLAEHF	1989
  	like peptide 2	AN
  	(BLP-2, toad)
  AP00052	P29004, Bombinin-	GIGAAILSAGKSALKGLAKGLAEH	1990
  	like peptide 3	F
  	(BLP-3, XXA,
  	toad)
  AP00053	P29005, Bombinin-	GIGAAILSAGKSIIKGLANGLAEHF	1991
  	like peptide 4
  	(BLP-4, toad)
  AP00634	P29430, Pediocin	KYYGNGVTCGKHSCSVDWGKATT	1992
  	PA-1/ AcH	CIINNGAMAWATGGHQGNHKC
  	(PedPA1, class IIA
  	bacteriocin, bacteria)
  AP00204	P29559, Nisin Z	ITSISLCTPGCKTGALMGCNMKTA	1993
  	(lantibiotic, class I	TCNCSIHVSK
  	bacteriocin,
  	bacteria)
  AP00130	P29561, Cecropin	GWLKKLGKRIERIGQHTRDATIQG	1994
  	C (insect, fly)	LGIAQQAANVAATAR
  AP00001	P31107,	GLWSKIKEVGKEAAKAAAKAAGK	1995
  	ADENOREGULIN	AALGAVSEAV
  	(Dermaseptin B2,
  	Dermaseptin-B2,
  	DRS-B2, DRS B2,
  	frog)
  AP00228	P31529, Sapecin B	LTCEIDRSLCLLHCRLKGYLRAYCS	1996
  	(insect, flesh fly)	QQKVCRCVQ
  AP00229	P31530, Sapecin C	ATCDLLSGIGVQHSACALHCVFRG	1997
  	(insect, flesh fly)	NRGGYCTGKGICVCRN
  AP00218	P32195, Protegrin	RGGRLCYCRRRFCICV	1998
  	2 (PG-2, pig
  	cathelicidin)
  AP00219	P32196, Protegrin	RGGGLCYCRRRFCVCVGR	1999
  	3 (PG-3, pig
  	cathelicidin)
  AP00073	P32412, Brevinin-	FLPLLAGLAANFLPKIFCKITRKC	2000
  	1E (frog)
  AP00080	P32414,	GIFSKLGRKKIKNLLISGLKNVGKE	2001
  	Esculentin-1 (frog)	VGMDVVRTGIDIAGCKIKGEC
  AP00074	P32423, Brevinin-1	FLPVLAGIAAKVVPALFCKITKKC	2002
  	(frog)
  AP00075	P32424, Brevinin-2	GLLDSLKGFAATAGKGVLQSLLST	2003
  	(frog)	ASCKLAKTC
  AP00175	P34084, Macaque	DSHEERHHGRHGHHKYGRKFHEK	2004
  	histatin (M-Histatin	HHSHRGYRSNYLYDN
  	1, primate,
  	monkey)
  AP00006	P35581, Apidaecin	GNNRPVYIPQPRPPHPRI	2005
  	IA (insect,
  	honeybee)
  AP00007	P35581, Apidaecin	GNNRPVYIPQPRPPHPRL	2006
  	IB (insect,
  	honeybee)
  AP00414	P36190,	SIGSALKKALPVAKKIGKIALPIAK	2007
  	Ceratotoxin A	AALP
  	(insect, fly)
  AP00415	P36191,	SIGSAFKKALPVAKKIGKAALPIAK	2008
  	Ceratotoxin B	AALP
  	(insect, fly)
  AP00172	P36193, Drosocin	GKPRPYSPRPTSHPRPIRV	2009
  	(insect)
  AP00170	P37362, Pyrrhocoricin	VDKGSYLPRPTPPRPIYNRN	2010
  	(insect)
  AP00635	P38577,	KYYGNGVHCTKSGCSVNWGEAAS	2011
  	Mesentericin Y105	AGIHRLANGGNGFW
  	(MesY105, class
  	IIA bacteriocin,
  	bacteria)
  AP00636	P38579,	AISYGNGVYCNKEKCWVNKAENK	2012
  	Carnobacteriocin	QAITGIVIGGWASSLAGMGH
  	BM1 (CnbBM1,
  	PiscV1b, class IIA
  	bacteriocin,
  	bacteria)
  AP00209	P39080, Peptide	GVLSNVIGYLKKLGTGALNAVLK	2013
  	PGQ (frog)	Q
  AP00513	P39084, Ranalexin	FLGGLIKIVPAMICAVTKKC	2014
  	(frog)
  AP00071	P40835, Brevinin-	FLPAIFRMAAKVVPTIICSITKKC	2015
  	1EA (frog)
  AP00072	P40836, Brevinin-	VIPFVASVAAEMQHVYCAASRKC	2016
  	1EB (frog)
  AP00076	P40837, Brevinin-	GILDTLKNLAISAAKGAAQGLVNK	2017
  	2EA (frog)	ASCKLSGQC
  AP00077	P40838, Brevinin-	GILDTLKNLAKTAGKGALQGLVK	2018
  	2EB (frog)	MASCKLSGQC
  AP00078	P40839, Brevinin-	GILLDKLKNFAKTAGKGVLQSLLN	2019
  	2EC (frog)	TASCKLSGQC
  AP00079	P40840, Brevinin-	GILDSLKNLAKNAGQILLNKASCK	2020
  	2ED (frog)	LSGQC
  AP00081	P40843,	GIFSKLAGKKIKNLLISGLKNVGKE	2021
  	Esculentin-1A	VGMDVVRTGIDIAGCKIKGEC
  	(frog)
  AP00082	P40844,	GIFSKLAGKKLKNLLISGLKNVGK	2022
  	Esculentin-1B	EVGMDVVRTGIDIAGCKIKGEC
  	(frog)
  AP00083	P40845,	GILSLVKGVAKLAGKGLAKEGGKF	2023
  	Esculentin-2A	GLELIACKIAKQC
  	(frog)
  AP00084	P40846,	GIFSLVKGAAKLAGKGLAKEGGKF	2024
  	Esculentin-2B	GLELIACKIAKQC
  	(ES2B RANES,
  	frog)
  AP00299	P46156, Chicken	GRKSDCFRKSGFCAFLKCPSLTLIS	2025
  	gallinacin 1 (Gal 1,	GKCSRFYLCCKRIW
  	avian beta-
  	defensin, bird)
  AP00300	P46157, Gallinacin	GRKSDCFRKNGFCAFLKCPYLTLIS	2026
  	1 alpha (avian beta-	GKCSRFHLCCKRIW
  	defensin, Bird),
  AP00298	P46158, Chicken	LFCKGGSCHFGGCPSHLIKVGSCFG	2027
  	gallinacin 2 (Gal 2,	FRSCCKWPWNA
  	avian beta-
  	defensin, bird)
  AP00037	P46160, Beta-	VRNHVTCRINRGFCVPIRCPGRTRQ	2028
  	defensin 2 (cow)	IGTCFGPRIKCCRSW
  AP00038	P46161, Beta-	QGVRNHVTCRINRGFCVPIRCPGR	2029
  	defensin 3 (cow)	TRQIGTCFGPRIKCCRSW
  AP00039	P46162, Beta-	QRVRNPQSCRWNMGVCIPFLCRV	2030
  	defensin 4 (cow)	GMRQIGTCFGPRVPCCRR
  AP00040	P46163, Beta-	QVVRNPQSCRWNMGVCIPISCPGN	2031
  	defensin 5 (cow)	MRQIGTCFGPRVPCCRRW
  AP00041	P46164, Beta-	QGVRNHVTCRIYGGFCVPIRCPGR	2032
  	defensin 6 (cow)	TRQIGTCFGRPVKCCRRW
  AP00042	P46165, Beta-	QGVRNFVTCRINRGFCVPIRCPGHR	2033
  	defensin 7 (cow)	RQIGTCLGPRIKCCR
  AP00043	P46166, Beta-	VRNFVTCRINRGFCVPIRCPGHRRQ	2034
  	defensin 8 (cow)	IGTCLGPQIKCCR
  AP00044	P46167, Beta-	QGVRNFVTCRINRGFCVPIRCPGHR	2035
  	defensin 9 (cow)	RQIGTCLAPQIKCCR
  AP00045	P46168, Beta-	QGVRSYLSCWGNRGICLLNRCPGR	2036
  	defensin 10 (cow)	MRQIGTCLAPRVKCCR
  AP00046	P46169, Beta-	GPLSCRRNGGVCIPIRCPGPMRQIG	2037
  	defensin 11 (cow)	TCFGRPVKCCRSW
  AP00048	P46171, Bovine	SGISGPLSCGRNGGVCIPIRCPVPM	2038
  	beta-defensin 13	RQIGTCFGRPVKCCRSW
  	(cow)
  AP00350	P48821, Enbocin	PWNIFKEIERAVARTRDAVISAGPA	2039
  	(insect, moth)	VRTVAAATSVAS
  AP00173	P49112, GNCP-2	RCICTTRTCRFPYRRLGTCLFQNRV	2040
  	(Guinea pig	YTFCC
  	neutrophil cationic
  	peptide 2)
  AP00369	P49930, PMAP-23	RIIDLLWRVRRPQKPKFVTVWVR	2041
  	(PMAP23, pig
  	cathelicidin)
  AP00370	P49931, PMAP-36	VGRFRRLRKKTRKRLKKIGKVLK	2042
  	(PMAP36, pig	WIPPIVGSIPLGCG
  	cathelicidin)
  AP00371	P49932, PMAP-37	GLLSRLRDFLSDRGRRLGEKIERIG	2043
  	(PMAP37, pig	QKIKDLSEFFQS
  	cathelicidin)
  AP00220	P49933, Protegrin	RGGRLCYCRGWICFCVGR	2044
  	4 (PG-4, pig
  	cathelicidin)
  AP00221	P49934, Protegrin	RGGRLCYCRPRFCVCVGR	2045
  	5 (PG-5, pig
  	cathelicidin)
  AP00346	P50720, Hyphancin	RWKIFKKIERVGQNVRDGIIKAGP	2046
  	MD (Fall	AIQVLGTAKAL
  	webworm, insect)
  AP00347	P50721, Hyphancin	RWKFFKKIERVGQNVRDGLIKAGP	2047
  	IIIE (Fall	AIQVLGAAKAL
  	webworm, insect)
  AP 00348	P50722, Hyphancin	RWKVFKKIEKVGRNIRDGVIKAGP	2048
  	IIIF (Fall	AIAVVGQAKAL
  	webworm, insect)
  AP00349	P50723, Hyphancin	RWKVFKKIEKVGRHIRDGVIKAGP	2049
  	IIIG (Fall	AITVVGQATAL
  	webworm, insect)
  AP00281	P51473, mCRAMP	GLLRKGGEKIGEKLKKIGQKIKNFF	2050
  	(mouse	QKLVPQPEQ
  	cathelicidin;
  	derivatives:
  	CRAMP 18)
  AP00366	P54228, BMAP-27	GRFKRFRKKFKKLFKKLSPVIPLLH	2051
  	(BMAP27, cow	LG
  	cathelicidin, ZZHs,
  	derivatives BMAP-
  	18 and BMAP-15)
  AP00367	P54229, BMAP-28	GGLRSLGRKILRAWKKYGPIIVPIIR	2052
  	(BMAP28, cow	IG
  	cathelicidin)
  AP00450	P54230, Cyclic	RICRIIFLRVCR	2053
  	dodecapeptide
  	(sheep cathelicidin)
  AP00359	P54684, Lebocin	DLRFLYPRGKLPVPTPPPFNPKPIYI	2054
  	1/2 (insect, silk	DMGNRY
  	moth)
  AP00360	P55796, Lebocin 3	DLRFLYPRGKLPVPTLPPFNPKPIYI	2055
  	(insect, silk moth)	DMGNRY
  AP00307	P55897, Buforin I	AGRGKQGGKVRAKAKTRSSRAGL	2056
  	(toad)	QFPVGRVHRLLRKGNY
  AP00308	P55897, Buforin II	TRSSRAGLQFPVGRVHRLLRK	2057
  	(toad)
  AP00240	P56226, Caerin 1.1	GLLSVLGSVAKHVLPHVVPVIAEH	2058
  	(frog, ZZHa)	L
  AP00241	P56227, Caerin 1.2	GLLGVLGSVAKHVLPHVVPVIAEH	2059
  	(frog)	L
  AP00242	P56228, Caerin 1.3	GLLSVLGSVAQHVLPHVVPVIAEH	2060
  	(frog)	L
  AP00243	P56229, Caerin 1.4	GLLSSLSSVAKHVLPHVVPVIAEHL	2061
  	(frog)
  AP00244	P56230, Caerin 1.5	GLLSVLGSVVKHVIPHVVPVIAEHL	2062
  	(frog)
  AP00245	P56231, Caerin 1.6	GLFSVLGAVAKHVLPHVVPVIAEK	2063
  	(frog)
  AP00246	P56232, Caerin 1.7	GLFKVLGSVAKHLLPHVAPVIAEK	2064
  	(frog)
  AP00249	P56233, Caerin 2.1	GLVSSIGRALGGLLADVVKSKGQP	2065
  	(frog)	A
  AP00250	P56234, Caerin 2.2	GLVSSIGRALGGLLADVVKSKEQP	2066
  	(frog)	A
  AP00251	P56236, Caerin 2.4	GLVSSIGKALGGLLADVVKTKEQP	2067
  	(frog)	A
  AP00252	P56236, Caerin 2.5	GLVSSIGRALGGLLADVVKSKEQP	2068
  	(frog)	A
  AP00253	P56238, Caerin 3.1	GLWQKIKDKASELVSGIVEGVK	2069
  	(frog)
  AP00254	P56238, Caerin 3.2	GLWEKIKEKASELVSGIVEGVK	2070
  	(frog)
  AP00255	P56240, Caerin 3.3	GLWEKIKEKANELVSGIVEGVK	2071
  	(frog)
  AP00256	P56241, Caerin 3.4	GLWEKIREKANELVSGIVEGVK	2072
  	(frog)
  AP00257	P56242, Caerin 4.1	GLWQKIKSAAGDLASGIVEGIKS	2073
  	(frog)
  AP00258	P56243, Caerin 4.2	GLWQKIKSAAGDLASGIVEAIKS	2074
  	(frog)
  AP00259	P56244, Caerin 4.3	GLWQKIKNAAGDLASGIVEGIKS	2075
  	(frog)
  AP00434	P56249, Frenatin 3	GLMSVLGHAVGNVLGGLFKS	2076
  	(frog)
  AP00272	P56386, Murine	DQYKCLQHGGFCLRSSCPSNTKLQ	2077
  	beta-defensin 1	GTCKPDKPNCCKS
  	(mBD-1, mouse)
  AP00368	P56425, BMAP-34	GLFRRLRDSIRRGQQKILEKARRIG	2078
  	(BMAP34, cow	ERIKDIFRG
  	cathelicidin)
  AP00273	P56685, Buthinin	SIVPIRCRSNRDCRRFCGFRGGRCT	2079
  	(Sahara scorpion)	YARQCLCGY
  AP00282	P56872,	SIPCGESCVFIPCTVTALLGCSCKSK	2080
  	Cyclopsychotride	VCYKN
  	A (CPT, plant
  	cyclotides, XXC)
  AP00094	P56917, Temporin	FLPLIGRVLSGIL	2081
  	A (XXA, frog)
  AP00096	P56918, Temporin	LLPILGNLLNGLL	2082
  	C (XXA, frog)
  AP00097	P56920, Temporin	VLPIIGNLLNSLL	2083
  	E (XXA,frog)
  AP00098	P56921, Temporin	FLPLIGKVLSGIL	2084
  	F (XXA,frog)
  AP00100	P56923, Temporin	LLPNLLKSLL	2085
  	K (XXA,frog)
  AP00295	P56928, eNAP-2	EVERKHPLGGSRPGRCPTVPPGTF	2086
  	(horse)	GHCACLCTGDASEPKGQKCCSN
  AP00101	P57104, Temporin	FVQWFSKFLGRIL	2087
  	L (XXA,frog)
  AP00095	P79874, Temporin	LLPIVGNLLKSLL	2088
  	B (XXA, frog)
  AP00099	P79875, Temporin	FFPVIGRILNGIL	2089
  	G (XXA,frog)
  AP00413	P80032,	SLQGGAPNFPQPSQQNGGWQVSP	2090
  	Coleoptericin	DLGRDDKGNTRGQIEIQNKGKDH
  	(insect)	DFNAGWGKVIRGPNKAKPTWHVG
  		GTYRR
  AP00396	P80054, PR-39	RRRPRPPYLPRPRPPPFFPPRLPPRIP	2091
  	(PR39, pig	PGFPPRFPPRFP
  	cathelicidin)
  AP00182	P80154, Insect	GFGCPLDQMQCHRHCQTITGRSGG	2092
  	defensin	YCSGPLKLTCTCYR
  AP00444	P80223,	GICACRRRFCLNFEQFSGYCRVNG	2093
  	Corticostatin VI	ARYVRCCSRR
  	(CS-VI) (animal
  	defensin, rabbit)
  AP00208	P80230, Peptide	RADTQTYQPYNKDWIKEKIYVLLR	2094
  	3910 (pig)	RQAQQAGK
  AP00157	P80277,	ALWKTMLKKLGTMALHAGKAAL	2095
  	Dermaseptin-S1	GAAADTISQGTQ
  	(Dermaseptin S1,
  	DRS S1, DRS-S1,
  	frog)
  AP00158	P80278,	ALWFTMLKKLGTMALHAGKAAL	2096
  	Dermaseptin-S2	GAAANTISQGTQ
  	(Dermaseptin S2,
  	DRS S2, DRS-S2,
  	frog)
  AP00159	P80279,	ALWKNMLKGIGKLAGKAALGAV	2097
  	Dermaseptin-S3	KKLVGAES
  	(Dermaseptin S3,
  	DRS S3, DRS-S3,
  	frog)
  AP00160	P80280,	ALWMTLLKKVLKAAAKALNAVL	2098
  	Dermaseptin-S4	VGANA
  	(Dermaseptin S4,
  	DRS S4, DRS-S4,
  	frog)
  AP00161	P80281,	GLWSKIKTAGKSVAKAAAKAAVK	2099
  	Dermaseptin-S5	AVTNAV
  	(Dermaseptin S5,
  	DRS S5, DRS-S5,
  	frog)
  AP00293	P80282,	AMWKDVLKKIGTVALHAGKAAL	2100
  	Dermaseptin-B1	GAVADTISQ
  	(DRS-B1, DRS B1,
  	frog)
  AP00264	P80389, Chicken	GRKSDCFRKSGFCAFLKCPSLTLIS	2101
  	Heterophil Peptide	GKCSRFYLCCKRIR
  	1 (CHP1, bird,
  	animal)
  AP00265	P80390, Chicken	GRKSDCFRKNGFCAFLKCPYLTLIS	2102
  	Heterophil Peptide	GLCSFHLC
  	2 (CHP2, bird,
  	animal)
  AP00266	P80391, Turkey	GKREKCLRRNGFCAFLKCPTLSVIS	2103
  	Heterophil Peptide	GTCSRFQVCC
  	1 (THP1, turkey)
  AP00267	P80392, Turkey	LFCKRGTCHFGRCPSHLIKVGSCFG	2104
  	Heterophil Peptide	FRSCCKWPWDA
  	2 (THP2, bird,
  	anaimal)
  AP00269	P80393, Turkey	LSCKRGTCHFGRCPSHLIKGSCSGG	2105
  	Heterophil Peptide
  	3 (THP3, bird,
  	animal)
  AP00085	P80395, Gaegurin-	SLFSLIKAGAKFLGKNLLKQGACY	2106
  	1 (Gaegurin 1,	AACKASKQC
  	frog)
  AP00086	P80396, Gaegurin-	GIMSIVKDVAKNAAKEAAKGALST	2107
  	2 (Gaegurin 2,	LSCKLAKTC
  	frog)
  AP00087	P80397, Gaegurin-	GIMSIVKDVAKTAAKEAAKGALST	2108
  	3 (Gaegurin 3,	LSCKLAKTC
  	frog)
  AP00089	P80399, Gaegurin-	FLGALFKVASKVLPSVFCAITKKC	2109
  	5 (Gaegurin 5,
  	frog)
  AP00090	P80400, Gaegurin-	FLPLLAGLAANFLPTIICKISYKC	2110
  	6 (Gaegurin 6,
  	frog)
  AP00362	P80408,	VDKPDYRPRPRPPNM	2111
  	Metalnikowin I
  	(insect)
  AP00363	P80409,	VDKPDYRPRPWPRPN	2112
  	Metalnikowin IIA
  	(insect)
  AP00364	P80410,	VDKPDYRPRPWPRNMI	2113
  	Metalnikowin IIB
  	(insect)
  AP00365	P80411,	VDKPDYRPRPWPRPNM	2114
  	Metalnikowin III
  	(insect)
  AP00632	P80569, Piscicolin	KYYGNGVSCNKNGCTVDWSKAIG	2115
  	126/Piscicocin	IIGNNAAANLTTGGAAGWNKG
  	Via (PiscV1a,
  	Pisc126, class IIA
  	bacteriocin,
  	bacteria)
  AP01003	P80666, Mutacin	FKSWSFCTPGCAKTGSFNSYCC	2116
  	B-Ny266 (bacteria)
  AP00276	P80710, Clavanin	VFQFLGKIIHHVGNFVHGFSHVF	2117
  	A (urochordates,
  	sea squirts, and sea
  	pork, tunicate)
  AP00277	P80711, Clavanin	VFQFLGRIIHHVGNFVHGFSHVF	2118
  	B (Sea squirt,
  	tunicate)
  AP00278	P80712, Clavanin	VFHLLGKIIHHVGNFVYGFSHVF	2119
  	C (Sea squirt,
  	tunicate)
  AP00279	P80713, Clavanin	AFKLLGRIIHHVGNFVYGFSHVF	2120
  	D (Sea squirt,
  	tunicate)
  AP00280	P80713, Clavanin	LFKLLGKIIHHVGNFVHGFSHVF	2121
  	D (Sea squirt,
  	tunicate)
  AP00294	P80930, eNAP-1	DVQCGEGHFCHDQTCCRASQGGA	2122
  	(horse)	CCPYSQGVCCADQRHCCPVGF
  AP00400	P80952, Skin	YPPKPESPGEDASPEEMNKYLTAL	2123
  	peptide tyrosine-	RHYINLVTRQRY
  	tyrosine (skin-
  	PYY, SPYY, frog)
  AP00091	P80954, Rugosin A	GLLNTFKDWAISIAKGAGKGVLTT	2124
  	(frog)	LSCKLDKSC
  AP00092	P80955, Rugosin B	SLFSLIKAGAKFLGKNLLKQGAQY	2125
  	(frog)	AACKVSKEC
  AP00093	P80956, Rugosin C	GILDSFKQFAKGVGKDLIKGAAQG	2126
  	(frog)	VLSTMSCKLAKTC
  AP00392	P81056, Penaeidin-	YRGGYTGPIPRPPPIGRPPLRLVVC	2127
  	1 (shrimp,	ACYRLSVSDARNCCIKFGSCCHLV
  	Crustacea)	K
  AP00393	P81057, Penaeidin-	YRGGYTGPIPRPPPIGRPPFRPVCN	2128
  	2a (shrimp,	ACYRLSVSDARNCCIKFGSCCHLV
  	Crustacea)	K
  AP00394	P81058, Penaeidin-	QVYKGGYTRPIPRPPPFVRPLPGGP	2129
  	3a (shrimp,	IGPYNGCPVSCRGISFSQARSCCSR
  	Crustacea)	LGRCCHVGKGYS
  AP00247	P81251, Caerin 1.8	GLFKVLGSVAKHLLPHVVPVIAEK	2130
  	(frog)
  AP00248	P81252, Caerin 1.9	GLFGVLGSIAKHVLPHVVPVIAEK	2131
  	(frog, ZZHa)
  AP00126	P81417, Cecropin	GGLKKLGKKLEGVGKRVFKASEK	2132
  	A (insect,	ALPVAVGIKALG
  	mosquito)
  AP00169	P81437, Formaecin	GRPNPVNTKPTPYPRL	2133
  	2 (insect, ants)
  AP00168	P81438, Formaecin	GRPNPVNNKPTPHPRL	2134
  	1 (insect, ants)
  AP00296	P81456, Fabatin -1	LLGRCKVKSNRFHGPCLTDTHCST	2135
  	(plant defensin)	VCRGEGYKGGDCHGLRRRCMCLC
  AP00297	P81457, Fabatin -2	LLGRCKVKSNRFNGPCLTDTHCST	2136
  	(plant defensin)	VCRGEGYKGGDCHGLRRRCMCLC
  AP01215	P81463, European	FVPYNPPRPYQSKPFPSFPGHGPFN	2137
  	bumblebee abaecin	PKIQWPYPLPNPGH
  	(insect)
  AP01214	P81464, Apidaecin	GNRPVYIPPPRPPHPRL	2138
  	(insect)
  AP00440	P81465, defensin	VTCFCRRRGCASRERHIGYCRFGN	2139
  	HANP-1 (hamster)	TIYRLCCRR
  AP00441	P81466, defensin	CFCKRPVCDSGETQIGYCRLGNTF	2140
  	HANP-2 (hamster)	YRLCCRQ
  AP00442	P81467, defensin	VTCFCRRRGCASRERLIGYCRFGN	2141
  	HANP-3 (hamster)	TIYGLCCRR
  AP00439	P81468, defensin	VTCFCKRPVCDSGETQIGYCRLGN	2142
  	HANP-4 (hamster)	TFYRLCCRQ
  AP00328	P81469, Styelin A	GFGKAFHSVSNFAKKHKTA	2143
  	(Sea squirt,
  	tunicate, XXA)
  AP00329	P81470, Styelin B	GFGPAFHSVSNFAKKHKTA	2144
  	(Sea squirt,
  	tunicate, XXA)
  AP00492	P81474, Misgurin	RQRVEELSKFSKKGAAARRRK	2145
  	(fish)
  AP00165	P81485,	ALWKNMLKGIGKLAGQAALGAV	2146
  	Dermaseptin-B3	KTLVGAE
  	(Dermaseptin B3,
  	DRS-B3, DRS B3,
  	frog)
  AP00163	P81486,	ALWKDILKNVGKAAGKAVLNTVT	2147
  	Dermaseptin-B4	DMVNQ
  	(Dermaseptin B4,
  	DRS-B4, DRS B4,
  	DRS-TR1, IRP,
  	frog)
  AP00162	P81487,	GLWNKIKEAASKAAGKAALGFVN	2148
  	Dermaseptin-B5	EMV
  	(Dermaseptin B5,
  	DRS-B5, DRS B5,
  	frog)
  AP00164	P81488,	ALWKTIIKGAGKMIGSLAKNLLGS	2149
  	Dermaseptin-B9	QAQPES
  	(Dermaseptin B9,
  	DRS-B9, DRS
  	DRG3, frog)
  AP00167	P81565, Phylloxin	GWMSKIASGIGTFLSGMQQ	2150
  	(phylloxin-B1,
  	PLX-B1, XXA,
  	frog)
  AP00291	P81568, Defensin	NIFFSSKKCKTVSKTFRGPCVRNAN	2151
  	D5 (So-D5) (plant
  	defensin)
  AP00290	P81569, Defensin	NIFFSSKKCKTVSKTFRGPCVRNA	2152
  	D4 (So-D4) (plant
  	defensin)
  AP00289	P81570, Defensin	GIFSSRKCKTVSKTFRGICTRNANC	2153
  	D3 (So-D3) (plant
  	defensin)
  AP00288	P81572, Defensin	TCESPSHKFKGPCATNRNCES	2154
  	D1 (So-D1) (plant
  	defensin)
  AP00292	P81573, Defensin	GIFSSRKCKTPSKTFKGYCTRDSNC	2155
  	D7 (So-D7) (plant	DTSCRYEGYPAGD
  	defensin)
  AP00270	P81591, Pn-AMP	QQCGRQASGRLCGNRLCCSQWGY	2156
  	(PnAMP, plant	CGSTASYCGAGCQSQCRS
  	defensin)
  AP00412	P81592,	SLQPGAPNVNNKDQPWQVSPHISR	2157
  	Acaloleptin A1	DDSGNTRTDINVQRHGENNDFEAG
  	(insect)	WSKVVRGPNKAKPTWHIGGTHRW
  AP00433	P81605, human	SSLLEKGLDGAKKAVGGLGKLGK	2158
  	Dermcidin (DCD-	DAVEDLESVGKGAVHDVKDVLDS
  	1)	V
  AP00332	P81612, Mytilin A	GCASRCKAKCAGRRCKGWASASF	2159
  	(Blue mussel)	RGRCYCKCFRC
  AP00333	P81613, Mytilin B	SCASRCKGHCRARRCGYYVSVLY	2160
  	(Blue mussel)	RGRCYCKCLRC
  AP00334	P81613,	FFHHIFRGIVHVGKTIHKLVTG	2161
  	Moronecidin (fish)
  AP00351	P81835, Citropin	GLFDVIKKVASVIGGL	2162
  	1.1 (amphibian,
  	frog)
  AP00352	P81840, Citropin	GLFDIIKKVASVVGGL	2163
  	1.2 (amphibian,
  	frog)
  AP00353	P81846, Citropin	GLFDIIKKVASVIGGL	2164
  	1.3 (amphibian,
  	frog)
  AP00338	P81903, Hi stone	PDPAKTAPKKGSKKAVTKA	2165
  	H2B-1(HLP-1)
  	(fish)
  AP00271	P82018, ChB ac5	RFRPPIRRPPIRPPFNPPFRPPVRPPF	2166
  	(Goat cathelicidin)	RPPFRPPFRPPIGPFP
  AP00316	P82027, Uperin 2.1	GIVDFAKKVVGGIRNALGI	2167
  	(amphibian, toad)
  AP00317	P82028, Uperin 2.2	GFVDLAKKVVGGIRNALGI	2168
  	(amphibian, toad)
  AP00318	P82029, Uperin 2.3	GFFDLAKKVVGGIRNALGI	2169
  	(amphibian, toad)
  AP00319	P82030, Uperin 2.4	GILDFAKTVVGGIRNALGI	2170
  	(amphibian, toad)
  AP00320	P82031, Uperin 2.5	GIVDFAKGVLGKIKNVLGI	2171
  	(amphibian, toad)
  AP00323	P82032, Uperin 3.1	GVLDAFRKIATVVKNVV	2172
  	(amphibian, toad)
  AP00326	P82035, Uperin 4.1	GVGSFIHKVVSAIKNVA	2173
  	(amphibian, toad)
  AP00321	P82039, Uperin 2.7	GIIDIAKKLVGGIRNVLGI	2174
  	(amphibian, toad)
  AP00322	P82040, Uperin 2.8	GILDVAKTLVGKLRNVLGI	2175
  	(amphibian, toad)
  AP00324	P82042, Uperin 3.5	GVGDLIRKAVSVIKNIV	2176
  	(amphibian, toad)
  AP00325	P82042, Uperin 3.6	GVIDAAKKVVNVLKNLP	2177
  	(amphibian, toad)
  AP00327	P82050, Uperin 7.1	GWFDVVKHIASAV	2178
  	(amphibian, frog)
  AP00260	P82066, Maculatin	GLFVGVLAKVAAHVVPAIAEHF	2179
  	1.1 (XXA, frog,
  	ZZHa)
  AP00261	P82067, Maculatin	GLFVGLAKVAAHNNPAIAEHFQA	2180
  	1.2 (XXA, frog)
  AP00262	P82068, Maculatin	GFVDFLKKVAGTIANVVT	2181
  	2.1 (frog)
  AP00263	P82069, Maculatin	GLLQTIKEKLESLESLAKGIVSGIQ	2182
  	3.1 (frog)	A
  AP00345	P82104, Caerin	GLLSVLGSVAKHVLPHVVPVIAEK	2183
  	1.10 (frog)	L
  AP00456	P82232, Brevinin-	VNPIILGVLPKFVCLITKKC	2184
  	1T (frog)
  AP00459	P82233, Brevinin-	FITLLLRKFICSITKKC	2185
  	1TA (frog)
  AP00457	P82234, Brevinin-	GLWETIKNFGKKFTLNILHKLKCKI	2186
  	2TC (frog)	GGGC
  AP00458	P82235, Brevinin-	GLWETIKNFGKKFTLNILHNLKCKI	2187
  	2TD (frog)	GGGC
  AP00397	P82238,	SGFVLKGYTKTSQ	2188
  	Salmocidin 2A
  	(fish, trout)
  AP00398	P82239,	AGFVLKGYTKTSQ	2189
  	Salmocidin 2B
  	(fish, trout)
  AP00055	P82282, Bombinin	IIGPVLGMVGSALGGLLKKI	2190
  	H1 (frog)
  AP00056	P82284, Bombinin	LIGPVLGLVGSALGGLLKKI	2191
  	H4 (frog, XXA,
  	XXD)
  AP00057	P82285, Bombinin	IIGPVLGLVGSALGGLLKKI	2192
  	H5 (frog, XXD)
  AP00419	P82286, Bombinin-	GIGASILSAGKSALKGFAKGLAEHF	2193
  	like peptides 2	AN
  	(amphibian, toad)
  AP00137	P82293, Cryptdin-1	LRDLVCYCRTRGCKRRERMNGTC	2194
  	(Crp1, animal	RKGHLMYTLCCR
  	defensin, alpha,
  	mouse)
  AP00443	P82317, defensin	ACYCRIPACLAGERRYGTCFYMGR	2195
  	RMAD-2 (monkey)	VWAFCC
  AP00012	P82386, Aurein 1.1	GLFDIIKKIAESI	2196
  	(amphibian,frog)
  AP00014	P82388, Aurein 2.1	GLLDIVKKVVGAFGSL	2197
  	(amphibian,frog)
  AP00015	P82389, Aurein 2.2	GLFDIVKKVVGALGSL	2198
  	(amphibian,frog)
  AP00016	P82390, Aurein 2.3	GLFDIVKKVVGAIGSL	2199
  	(XXA,
  	amphibian,frog)
  AP00017	P82391, Aurein 2.4	GLFDIVKKVVGTIAGL	2200
  	(XXA,
  	amphibian,frog)
  AP00018	P82392, Aurein 2.5	GLFDIVKKVVGAFGSL	2201
  	(XXA,
  	amphibian,frog)
  AP00019	P82393, Aurein 2.6	GLFDIAKKVIGVIGSL	2202
  	(XXA,
  	amphibian,frog)
  AP00020	P82394, Aurein 3.1	GLFDIVKKIAGHIAGSI	2203
  	(XXA,
  	amphibian,frog)
  AP00021	P82395, Aurein 3.2	GLFDIVKKIAGHIASSI	2204
  	(XXA,
  	amphibian,frog)
  AP00022	P82396, Aurein 3.3	GLFDIVKKIAGHIVSSI	2205
  	(XXA,
  	amphibian,frog)
  AP00376	P82414, Ponericin	GWKDWAKKAGGWLKKKGPGMA	2206
  	G1 (ants)	KAALKAAMQ
  AP00377	P82415, Ponericin	GWKDWLKKGKEWLKAKGPGIVK	2207
  	G2 (ants)	AALQAATQ
  AP00378	P82416, Ponericin	GWKDWLNKGKEWLKKKGPGIMK	2208
  	G3 (ants)	AALKAATQ
  AP00379	P82417, Ponericin	DFKDWMKTAGEWLKKKGPGILKA	2209
  	G4 (ants)	AMAAAT
  AP00380	P82418, Ponericin	GLKDWVKIAGGWLKKKGPGILKA	2210
  	G5 (ants)	AMAAATQ
  AP00381	P82419, Ponericin	GLVDVLGKVGGLIKKLLP	2211
  	G6 (ants)
  AP00382	P82420, Ponericin	GLVDVLGKVGGLIKKLLPG	2212
  	G7 (ants)
  AP00383	P82421, Ponericin	LLKELWTKMKGAGKAVLGKIKGL	2213
  	L1 (ants)	L
  AP00384	P82422, Ponericin	LLKELWTKIKGAGKAVLGKIKGLL	2214
  	L2 (ants)
  AP00386	P82423, Ponericin	WLGSALKIGAKLLPSVVGLFKKKK	2215
  	W1 (ants)	Q
  AP00387	P82424, Ponericin	WLGSALKIGAKLLPSVVGLFQKKK	2216
  	W2 (ants)	K
  AP00388	P82425, Ponericin	GIWGTLAKIGIKAVPRVISMLKKK	2217
  	W3 (ants)	KQ
  AP00389	P82426, Ponericin	GIWGTALKWGVKLLPKLVGMAQT	2218
  	W4 (ants)	KKQ
  AP00390	P82427, Ponericin	FWGALIKGAAKLIPSVVGLFKKKQ	2219
  	W5 (ants)
  AP00391	P82428, Ponericin	FIGTALGIASAIPAIVKLFK	2220
  	W6 (ants)
  AP00303	P82651, Tigerinin-	FCTMIPIPRCY	2221
  	1 (frog)
  AP00304	P82652, Tigerinin-	RVCFAIPLPICH	2222
  	2 (frog)
  AP00305	P82653, Tigerinin-	RVCYAIPLPICY	2223
  	3 (frog)
  AP00301	P82656, Hadrurin	GILDTIKSIASKVWNSKTVQDLKR	2224
  	(scorpion)	KGINWVANKLGVSPQAA
  AP00113	P82740,	GLLSGLKKVGKHVAKNVAVSLMD	2225
  	RANATUERIN 1T	SLKCKISGDC
  	(frog)
  AP00114	P82741,	SMLSVLKNLGKVGLGFVACKINK	2226
  	RANATUERIN 1	QC
  	(Ranatuerin-1,
  	frog)
  AP00115	P82742,	GLFLDTLKGAAKDVAGKLEGLKC	2227
  	RANATUERIN 2	KITGCKLP
  	(Ranatuerin-2,
  	frog)
  AP00116	P82780,	GFLDIINKLGKTFAGHMLDKIKCTI	2228
  	RANATUERIN 3	GTCPPSP
  	(Ranatuerin-3,
  	frog)
  AP00117	P82819,	FLPFIARLAAKVFPSIICSVTKKC	2229
  	RANATUERIN 4
  	(Ranatuerin-4,
  	frog)
  AP00405	P82821,	FISAIASMLGKFL	2230
  	RANATUERIN 6
  	(frog)
  AP00406	P82822,	FLSAIASMLGKFL	2231
  	RANATUERI 7
  	(frog)
  AP00407	P82823,	FISAIASFLGKFL	2232
  	RANATUERIN 8
  	(frog)
  AP00408	P82824,	FLFPLITSFLSKVL	2233
  	RANATUERIN 9
  	(frog)
  AP00461	P82825, Brevinin-	FLPMLAGLAASMVPKLVCLITKKC	2234
  	1LA (frog)
  AP00462	P82826, Brevinin-	FLPMLAGLAASMVPKFVCLITKKC	2235
  	1LB (frog)
  AP00118	P82828,	GILDSFKGVAKGVAKDLAGKLLD	2236
  	RANATUERIN	KLKCKITGC
  	2La (Ranatuerin-
  	2La, frog)
  AP00119	P82829,	GILSSIKGVAKGVAKNVAAQLLDT	2237
  	RANATUERIN	LKCKITGC
  	2Lb (Ranatuerin-
  	2Lb, frog)
  AP00109	P82830, Temporin-	VLPLISMALGKLL	2238
  	1La (Temporin
  	1La, frog)
  AP00110	P82831, Temporin-	NFLGTLINLAKKIM	2239
  	1Lb (Temporin
  	1Lb, frog)
  AP00111	P82832, Temporin-	FLPILINLIHKGLL	2240
  	1Lc (Temporin
  	1Lc, frog)
  AP00463	P82833, Brevinin-	FLPFIAGMAAKFLPKIFCAISKKC	2241
  	1BA (frog)
  AP00464	P82834, Brevinin-	FLPAIAGMAAKFLPKIFCAISKKC	2242
  	1BB (frog)
  AP00465	P82835, Brevinin-	FLPFIAGVAAKFLPKIFCAISKKC	2243
  	1BC (frog)
  AP00466	P82836, Brevinin-	FLPAIAGVAAKFLPKIFCAISKKC	2244
  	1BD (frog)
  AP00467	P82837, Brevinin-	FLPAIVGAAAKFLPKIFCVISKKC	2245
  	1BE (frog)
  AP00468	P82838, Brevinin-	FLPFIAGMAANFLPKIFCAISKKC	2246
  	1BF (frog)
  AP00120	P82840,	GLLDTIKGVAKTVAASMLDKLKC	2247
  	RANATUERIN 2B	KISGC
  	(Ranatuerin-2B,
  	frog)
  AP00469	P82841, Brevinin-	FLPIIAGVAAKVFPKIFCAISKKC	2248
  	1PA (frog)
  AP00460	P82842, Brevinin-	FLPIIAGIAAKVFPKIFCAISKKC	2249
  	1PB (frog)
  AP00470	P82843, Brevinin-	FLPIIASVAAKVFSKIFCAISKKC	2250
  	1PC (frog)
  AP00471	P82844, Brevinin-	FLPIIASVAANVFSKIFCAISKKC	2251
  	1PD (frog)
  AP00472	P82845, Brevinin-	FLPIIASVAAKVFPKIFCAISKKC	2252
  	1PE (frog)
  AP00121	P82847,	GLMDTVKNVAKNLAGHMLDKLK	2253
  	RANATUERIN 2P	CKITGC
  	(Ranatuerin-2P,
  	frog)
  AP00112	P82848, Temporin-	FLPIVGKLLSGLL	2254
  	1P (Temporin 1P,
  	frog)
  AP00452	P82871, Brevinin-	FLPVVAGLAAKVLPSIICAVTKKC	2255
  	1SY (frog)
  AP00122	P82875,	SMLSVLKNLGKVGLGLVACKINK	2256
  	Ranatuerin-1C	QC
  	(Ranatuerin 1C,
  	frog)
  AP00514	P82876, Ranalexin-	FLGGLMKAFPALICAVTKKC	2257
  	1Ca (frog)
  AP00515	P82877, Ranalexin-	FLGGLMKAFPAIICAVTKKC	2258
  	1Cb (frog)
  AP00124	P82878,	GLFLDTLKGAAKDVAGKLLEGLK	2259
  	Ranatuerin-2Ca	CKIAGCKP
  	(Ranatuerin 2Ca,
  	frog)
  AP00123	P82879,	GLFLDTLKGLAGKLLQGLKCIKAG	2260
  	Ranatuerin-2Cb	CKP
  	(Ranatuerin 2Cb,
  	frog)
  AP00104	P82880, Temporin-	FLPFLAKILTGVL	2261
  	1Ca (Temporin
  	1Ca, frog)
  AP00105	P82881, Temporin-	FLPLFASLIGKLL	2262
  	1Cb (Temporin
  	1Cb, frog)
  AP00106	P82882, Temporin-	FLPFLASLLTKVL	2263
  	1Cc (Temporin
  	1Cc, frog)
  AP00107	P82883, Temporin-	FLPFLASLLSKVL	2264
  	1Cd (Temporin
  	1Cd, frog)
  AP00108	P82884, Temporin-	FLPFLATLLSKVL	2265
  	1Ce (Temporin
  	1Ce, frog)
  AP00453	P82904, Brevinin-	FLPAIVGAAGQFLPKIFCAISKKC	2266
  	1SA (frog)
  AP00454	P82905, Brevinin-	FLPAIVGAAGKFLPKIFCAISKKC	2267
  	1SB (frog)
  AP00455	P82906, Brevinin-	FFPIVAGVAGQVLKKIYCTISKKC	2268
  	1SC (frog)
  AP00996	P82907, Lichenin	ISLEICAIFHDN	2269
  	(bacteria)
  AP00302	P82951, Hepcidin	GCRFCCNCCPNMSGCGVCCRF	2270
  	(fish)
  AP00058	P83080, Maximin 1	GIGTKILGGVKTALKGALKELAST	2271
  	(toad)	YAN
  AP00059	P83081, Maximin 2	GIGTKILGGVKTALKGALKELAST	2272
  	(toad)	YVN
  AP00060	P83082, Maximin 3	GIGGKILSGLKTALKGAAKELAST	2273
  	(toad, ZZHa)	YLH
  AP00061	P83083, Maximin 4	GIGGVLLSAGKAALKGLAKVLAE	2274
  	(toad)	KYAN
  AP00062	P83084, Maximin 5	SIGAKILGGVKTFFKGALKELASTY	2275
  	(toad)	LQ
  AP00063	P83085, Maximin 6	ILGPVISTIGGVLGGLLKNL	2276
  	(toad)
  AP00064	P83086, Maximin 7	ILGPVLGLVGNALGGLIKNE	2277
  	(toad)
  AP00065	P83087, Maximin 8	ILGPVLSLVGNALGGLLKNE	2278
  	(toad)
  AP00355	P83171,	ANTAFVSSAHNTQKIPAGAPFNRN	2279
  	Ginkbilobin	LRAMLADLRQNAAFAG
  	(Chinese plant)
  AP00475	P83188, Pseudin 1	GLNTLKKVFQGLHEAIKLINNHVQ	2280
  	(frog)
  AP00476	P83189, Pseudin 2	GLNALKKVFQGIHEAIKLINNHVQ	2281
  	(frog)
  AP00477	P83190, Pseudin 3	GINTLKKVIQGLHEVIKLVSNHE	2282
  	(frog)
  AP00478	P83191, Pseudin 4	GINTLKKVIQGLHEVIKLVSNHA	2283
  	(frog)
  AP00410	P83287,	SKGKKANKDVELARG	2284
  	Oncorhyncin III
  	(fish)
  AP00357	P83305, Japonicin-	FFPIGVFCKIFKTC	2285
  	1 (amphibian, frog)
  AP00358	P83306, Japonicin-	FGLPMLSILPKALCILLKRKC	2286
  	2 (amphibian, frog)
  AP00385	P83312,	FKLGSFLKKAWKSKLAKKLRAKG	2287
  	Parabutoporin	KEMLKDYAKGLLEGGSEEVPGQ
  	(scorpion)
  AP00374	P83313,	GKVWDWIKSTAKKLWNSEPVKEL	2288
  	Opistoporin 1	KNTALNAAKNLVAEKIGATPS
  	(scorpion)
  AP00375	P83314,	GKVWDWIKSTAKKLWNSEPVKEL	2289
  	Opistoporin 2	KNTALNAAKNFVAEKIGATPS
  	(scorpion)
  AP00336	P83327, Histone	AERVGAGAPVYL	2290
  	H2A (fish)
  AP00335	P83338, Histone	PKRKSATKGDEPA	2291
  	H6-like protein
  	(fish)
  AP00411	P83374,	KAVAAKKSPKKAKKPAT	2292
  	Oncorhyncin II
  	(fish)
  AP00999	P83375, Serracin-P	DYHHGVRVL	2293
  	43 kDa subunit
  	(bacteria)
  AP00284	P83376,	SHQDCYEALHKCMASHSKPFSCS	2294
  	Dolabellanin B2	MKFHMCLQQQ
  	(sea hare)
  AP00998	P83378, Serracin-P	ALPKKLKYLNLFNDGFNYMGVV	2295
  	23 kDa subunit
  	(bacteriocin,
  	bacteria)
  AP00129	P83403, Cecropin	GWLKKIGKKIERVGQNTRDATVK	2296
  	(insect, moth)	GLEVAQQAANVAATVR
  AP00127	P83413, Cecropin	RWKVFKKIEKVGRNIRDGVIKAAP	2297
  	A (insect, moth)	AIEVLGQAKAL
  AP00372	P83416, Virescein	GKIPIGAIKKAGKAIGKGLRAVNIA	2298
  	(insect)	STAHDVYTFFKPKKRH
  AP00356	P83427, Heliocin	QRFIHPTYRPPPQPRRPVIMRA	2299
  	(insect)
  AP00409	P83428, Locustin	ATTGCSCPQCIIFDPICASSYKNGRR	2300
  	(insect)	GFSSGCHMRCYNRCHGTDYFQISK
  		GSKCI
  AP00339	P83545,	FFGWLIKGAIHAGKAIHGLIHRRRH	2301
  	Chrysophsin-1
  	(Red sea bream,
  	madai)
  AP00340	P83546,	FFGWLIRGAIHAGKAIHGLIHRRRH	2302
  	Chrysophsin-2
  	(Red sea bream,
  	madai)
  AP00341	P83547,	FIGLLISAGKAIHDLIRRRH	2303
  	Chrysophsin-3
  	(Red sea bream,
  	madai)
  AP01004	P84763, Thuricin-S	DWTAWSALVAAACSVELL	2304
  	(bacteria)
  AP00553	P84868, Sesquin	KTCENLADTY	2305
  	(plant, ZZHp)
  AP00132	Q06589, Cecropin	GWLKKIGKKIERVGQHTRDATIQTI	2306
  	1 (insect, fly)	AVAQQAANVAATAR
  AP00135	Q06590, Cecropin	GWLKKIGKKIERVGQHTRDATIQTI	2307
  	2 (insect fly)	GVAQQAANVAATLK
  AP00416	Q17313,	SLGGVISGAKKVAKVAIPIGKAVLP	2308
  	Ceratotoxin C	VVAKLVG
  	(insect, fly)
  AP00171	Q24395,	HRHQGPIFDTRPSPFNPNQPRPGPIY	2309
  	Metchnikowin
  	(insect)
  AP00354	Q27023, Tenecin 1	VTCDILSVEAKGVKLNDAACAAH	2310
  	(insect)	CLFRGRSGGYCNGKRVCVCR
  AP00401	Q28880, Lingual	GFTQGVRNSQSCRRNKGICVPIRCP	2311
  	antimicrobial	GSMRQIGTCLGAQVKCCRRK
  	peptide (LAP, beta
  	defensin, cow)
  AP00224	Q62713, RatNP-3	CSCRTSSCRFGERLSGACRLNGRIY	2312
  	(rat)	RLCC
  AP00225	Q62714, RatNP-4	ACYCRIGACVSGERLTGACGLNGR	2313
  	(rat)	IYRLCCR
  AP00223	Q62715, RatNP-2	VTCYCRSTRCGFRERLSGACGYRG	2314
  	(rat)	RIYRLCCR
  AP00222	Q62716, RatNP-1	VTCYCRRTRCGFRERLSGACGYRG	2315
  	(rat)	RIYRLCCR
  AP00174	Q64365, GNCP-1	RRCICTTRTCRFPYRRLGTCIFQNR	2316
  	(Guinea pig	VYTFCC
  	neutrophil cationic
  	peptide 1)
  AP00311	Q90W78, Galensin	CYSAAKYPGFQEFINRKYKSSRF	2317
  	(frog)
  AP00395	Q95NT0,	HSSGYTRPLPKPSRPIFIIRPIGCDVC	2318
  	Penaeidin-4a	YGIPSSTARLCCFRYGDCCHR
  	(shrimp, Crustacea)
  AP00423	Q962B0,	QGYKGPYTRPILRPYVRPVVSYNA	2319
  	Penaeidin-3n	CTLSCRGITTTQARSCSTRLGRCCH
  	(shrimp, Crustacea)	VAKGYS
  AP00422	Q962B1,	QGCKGPYTRPILRPYVRPVVSYNA	2320
  	Penaeidin-3m	CTLSCRGITTTQARSCCTRLGRCCH
  	(shrimp, Crustacea)	VAKGYS
  AP00421	Q963C3,	YSSGYTRPLPKPSRPIFIRPIGCDVC	2321
  	Penaeidin-4C	YGIPSSTARLCCFRYGDCCHR
  	(shrimp, Crustacea)
  AP00210	Q99134, PGLa	GMASKAGAIAGKIAKVALKAL	2322
  	(African clawed
  	frog, XXA)
  AP00054	Q9DET7,	GIGGALLSAGKSALKGLAKGLAEH	2323
  	Bombinin-like	FAN
  	peptide 7 (BLP-7,
  	toad)
  AP00315	Q9PT75,	SLGSFLKGVGTTLASVGKVVSDQF	2324
  	Dermatoxin (Two-	GKLLQAGQ
  	colored leaf frog)
  AP00133	Q9Y0Y0, Cecropin	GGLKKLGKKLEGVGKRVFKASEK	2325
  	B (insect,	ALPVLTGYKAIG
  	mosquito)
  AP00004	Ref, Ct-AMP1	NLCERASLTWTGNCGNTGHCDTQ	2326
  	(CtAMP1, C.	CRNWESAKHGACHKRGNWKCFC
  	ternatea-	YFDC
  	antimicrobial
  	peptide
  1, plant
  	defensin)
  AP00027	Ref, hexapeptide	RRWQWR	2327
  	(synthetic)
  AP00529	Ref, Lantibiotic	WKSESVCTPGCVTGVLQTCFLQTI	2328
  	Ericin S (bacteria)	TCNCHISK
  AP00306	Ref, Tigerinin-4	RVCYAIPLPIC	2329
  	(frog)
  AP00309	Ref, Human KS-27	KSKEKIGKEFKRIVQRIKDFLRNLV	2330
  	(KS27 from LL-37)	PR
  AP00344	Ref, Apidaecin II	GNNRPIYIPQPRPPHPRL	2331
  	(honeybee, insect)
  AP00424	Ref, XT 1 (frog)	GFLGPLLKLAAKGVAKVIPHLIPSR	2332
  		QQ
  AP00425	Ref, XT 2 (frog)	GCWSTVLGGLKKFAKGGLEAIVNP	2333
  		K
  AP00426	Ref, XT 4 (frog)	GVFLDALKKFAKGGMNAVLNPK	2334
  AP00427	Ref, XT 7 (frog)	GLLGPLLKIAAKVGSNLL	2335
  AP00431	Ref, human LLP 1	RVIEVVQGACRAIRHIPRRIRQGLE	2336
  		RIL
  AP00432	Ref, human LLP	RIAGYGLRGLAVIIRICIRGLNLIFEI	2337
  		IR
  AP00447	Ref, Anoplin	GLLKRIKTLL	2338
  	(insect)
  AP00474	Ref, Piscidin 3	FIHHIFRGIVHAGRSIGRFLTG	2339
  	(fish)
  AP00481	Ref, Kaliocin-1	FFSASCVPGADKGQFPNLCRLCAG	2340
  	(synthetic)	TGENKCA
  AP00482	Ref, Thionin	KSCCRNTWARNCYNVCRLPGTISR	2341
  	mutation	EICAKKCRCKIISGTTCPSDYPK
  	(synthetic)
  AP00484	Ref, Stomoxyn	RGFRKHFNKLVKKVKHTISETAHV	2342
  	(insect, fly)	AKDTAVIAGSGAAVVAAT
  AP00486	Ref, Cupiennin 1b	GFGSLFKFLAKKVAKTVAKQAAK	2343
  	(spider)	QGAKYIANKQME
  AP00487	Ref, Cupiennin 1c	GFGSLFKFLAKKVAKTVAKQAAK	2344
  	(spider)	QGAKYIANKQTE
  AP00488	Ref, Cupiennin 1D	GFGSLFKFLAKKVAKTVAKQAAK	2345
  	(spider)	QGAKYVANKHME
  AP00489	Ref, Hipposin	SGRGKTGGKARAKAKTRSSRAGL	2346
  	(fish)	QFPVGRVHRLLRKGNYAHRVGAG
  		APVYL
  AP00923	Ref,	AISYGNGVYCNKEKCWVNKAENK	2347
  	Carnobacteriocin	QAITGIVIGGWASSLAGMGH
  	B1 (XXO, class Ha
  	bacteriocin,
  	bacteria)
  AP00496	Ref, HP 2-20	AKKVFKRLEKLFSKIQNDK	2348
  	(synthetic)
  AP00497	Ref, Maximin H5	ILGPVLGLVSDTLDDVLGIL	2349
  	(toad)
  AP00498	Ref, rCRAMP (rat	GLVRKGGEKFGEKLRKIGQKIKEF	2350
  	cathelicidin)	FQKLALEIEQ
  AP00500	Ref, S9-P18	KWKLFKKISKFLHLAKKF	2351
  	(synthetic)
  AP00501	Ref, L9-P18	KWKLFKKILKFLHLAKKF	2352
  	(synthetic)
  AP00502	Ref, Clavaspirin	FLRFIGSVIHGIGHLVHHIGVAL	2353
  	(sea squirt,
  	tunicate)
  AP00503	Ref, human P-	AKRHHGYKRKFH	2354
  	113D
  AP00504	Ref, human MUC7	LAHQKPFIRKSYKCLHKRCR	2355
  	20-Mer
  AP00507	Ref, Nigrocin 2	GLLSKVLGVGKKVLCGVSGLC	2356
  	(frog)
  AP00508	Ref, Nigrocin 1	GLLDSIKGMAISAGKGALQNLLKV	2357
  	(frog)	ASCKLDKTC
  AP00509	Ref, human	VAIALKAAHYHTHKE	2358
  	Calcitermin
  AP00510	Ref, Dicynthaurin	ILQKAVLDCLKAAGSSLSKAAITAI	2359
  	(sea peach)	YNKIT
  AP00511	Ref, KIGAKI	KIGAKIKIGAKIKIGAKI	2360
  	(synthetic)
  AP00516	Ref, Lycotoxin I	IWLTALKFLGKHAAKHLAKQQLS	2361
  	(spider)	KL
  AP00517	Ref, Lycotoxin II	KIKWFKTMKSIAKFIAKEQMKKHL	2362
  	(spider)	GGE
  AP00518	Ref, Ib-AMP3	QYRHRCCAWGPGRKYCKRWC	2363
  	(plant defensin,
  	balsam)
  AP00519	Ref, Ib-AMP4	EWGRRCCGWGPGRRYCRRWC	2364
  	(plant defensin,
  	balsam)
  AP00521	Ref, Dhvar4	KRLFKKLLFSLRKY	2365
  	(synthetic)
  AP00522	Ref, Dhvar5	LLLFLLKKRKKRKY	2366
  	(synthetic)
  AP00525	Ref, Maximin H2	ILGPVLSMVGSALGGLIKKI	2367
  	(toad)
  AP00526	Ref, Maximin H3	ILGPVLGLVGNALGGLIKKI	2368
  	(toad)
  AP00527	Ref, Maximin H4	ILGPVISKIGGVLGGLLKNL	2369
  	(toad)
  AP00528	Ref, Anionic	DDDDDD	2370
  	peptide SAAP
  	(sheep)
  AP00530	Ref, Lantibiotic	VLSKSLCTPGCITGPLQTCYLCFPT	2371
  	Ericin A (bacteria)	FAKC
  AP00531	Ref, Kenoj einin I	GKQYFPKVGGRLSGKAPLAAKTH	2372
  	(sea skate)	RRLKP
  AP00532	Ref, Lunatusin	KTCENLADTFRGPCFATSNC	2373
  	(plant, ZZHp)
  AP00533	Ref, Fallaxin (frog)	GVVDILKGAAKDIAGHLASKVMN	2374
  		KL
  AP00534	Ref, Tu-AMP 2	KSCCRNTTARNCYNVCRIPG	2375
  	(TuAMP2, thionin-
  	like antimicrobial
  	peptides, plant
  	defensin, tulip)
  AP00535	Ref, Pilosulin 1	GLGSVFGRLARILGRVIPKVAKKL	2376
  	(Myr b I)	GPKVAKVLPKVMKEAIPMAVEMA
  	(Australian ants)	KSQEEQQPQ
  AP00536	Ref, Luxuriosin	SVRTQDNAVNRQIFGSNGPYRDFQ	2377
  	(insect)	LSDCYLPLETNPYCNEWQFAYHW
  		NNALMDCERAIYHGCNRTRNNFIT
  		LTACKNQAGPICNRRRH
  AP00537	Ref, SAMP H1	AEVAPAPAAAAPAKAPKKKAAAK	2378
  	(fish, Atlantic	PKKAGPS
  	salmon)
  AP00538	Ref, Halocidin	WLNALLHHGLNCAKGVLA	2379
  	(dimer Hal18 +
  	Hal 15) (tunicate)
  AP00539	Ref, AOD	GFGCPWNRYQCHSHCRSIGRLGGY	2380
  	(American oyster	CAGSLRLTCTCYRS
  	defensin, animal
  	defensin)
  AP00540	Ref, Pentadactylin	GLLDTLKGAAKNVVGSLASKVME	2381
  	(frog)	KL
  AP00541	Ref, Polybia-MPI	IDWKKLLDAAKQIL	2382
  	(insect, social
  	wasp)
  AP00542	Ref, Polybia-CP	ILGTILGLLKSL	2383
  	(insect, social
  	wasp)
  AP00543	Ref, Ocellatin-1	GVVDILKGAGKDLLAHLVGKISEK	2384
  	(XXA, frog)	V
  AP00544	Ref, Ocellatin-2	GVLDIFKDAAKQILAHAAEKQI	2385
  	(XXA, frog)
  AP00545	Ref, Ocellatin-3	GVLDILKNAAKNILAHAAEQI	2386
  	(frog)
  AP00548	Ref, CMAP 27	RFGRFLRKIRRFRPKVTITIQGSARF	2387
  	(chicken myeloid	G
  	antimicrobial
  	peptide 27, bird
  	cathelicidin,
  	chicken
  	cathelicidin)
  AP00550	Ref, Tu-AMP-1	KSCCRNTVARNCYNVCRIPGTPRP	2388
  	(TuAMP1, thionin-	VCAATCDCKLITGTKCPPGYEK
  	like antimicrobial
  	peptides, plant
  	defensin, tulip)
  AP00551	Ref, Combi-2	FRWWHR	2389
  	(synthetic)
  AP00552	Ref, Maximin 9	GIGRKFLGGVKTTFRCGVKDFASK	2390
  	(frog)	HLY
  AP00554	Ref, Sl moricin	GKIPVKAIKKAGAAIGKGLRAINIA	2391
  	(insect)	STAHDVYSFFKPKHKKK
  AP00555	Ref, Parasin I	KGRGKQGGKVRAKAKTRSS	2392
  	(catfish)
  AP00556	Ref, Kassinatuerin-	GFMKYIGPLIPHAVKAISDLI	2393
  	1 (frog)
  AP00557	Ref, Fowlicidin-1	RVKRVWPLVIRTVIAGYNLYRAIK	2394
  	(chCATH-1, bird	KK
  	cathelicidin,
  	chicken
  	cathelicidin)
  AP00559	Ref, Eryngin	ATRVVYCNRRSGSVVGGDDTVYY	2395
  	(mushroom, fungi)	EG
  AP00560	Ref, Dendrocin	TTLTLHNLCPYPVWWLVTPNNGG	2396
  	(plant, bamboo)	FPIIDNTPVVLG
  AP00561	Ref, Coconut	EQCREEEDDR	2397
  	antifungal peptide
  	(plant)
  AP00562	Ref, Pandinin 1	GKVWDWIKSAAKKIWSSEPVSQL	2398
  	(African scorpion)	KGQVLNAAKNYVAEKIGATPT
  AP00563	Ref, White cloud	KTCENLADTFRGPCFATSNCDDHC	2399
  	bean defensin	KNKEHLLSGRCRDDFRCWCTRNC
  	(plant defensin)
  AP00564	Ref, Dybowskin-1	FLIGMTHGLICLISRKC	2400
  	(frog)
  AP00565	Ref, Dybowskin-2	FLIGMTQGLICLITRKC	2401
  	(frog)
  AP00566	Ref, Dybowskin-3	GLFDVVKGVLKGVGKNVAGSLLE	2402
  	(frog)	QLKCKLSGGC
  AP00567	Ref, Dybowskin-4	VWPLGLVICKALKIC	2403
  	(frog)
  AP00568	Ref, Dybowskin-5	GLFSVVTGVLKAVGKNVAKNVGG	2404
  	(frog)	SLLEQLKCKKISGGC
  AP00569	Ref, Dybowskin-6	FLPLLLAGLPLKLCFLFKKC	2405
  	(frog)
  AP00570	Ref, Pleurain-A1	SIITMTKEAKLPQLWKQIACRLYNT	2406
  	(frog)	C
  AP00571	Ref, Pleurai n-A2	SIITMTKEAKLPQSWKQIACRLYNT	2407
  	(frog)	C
  AP00574	Ref, Esculentin-	GLFSKFAGKGIKNLIFKGVKHIGKE	2408
  	IGRa (frog)	VGMDVIRTGIDVAGCKIKGEC
  AP00575	Ref, Brevinin-	GLLDTFKNLALNAAKSAGVSVLNS	2409
  	2GRa (frog)	LSCKLSKTC
  AP00576	Ref, Brevinin-	GVLGTVKNLLIGAGKSAAQSVLKT	2410
  	2GRb (frog)	LSCKLSNDC
  AP00577	Ref, Brevinin-	GLFTLIKGAAKLIGKTVAKEAGKT	2411
  	2GRc (frog)	GLELMACKITNQC
  AP00578	Ref, Brevinin-	FLPLLAGLAANFLPKIFCKITKKC	2412
  	1GRa (frog)
  AP00579	Ref, Nigrocin-	GLLSGILGAGKHIVCGLSGLC	2413
  	2GRa (frog)
  AP00580	Ref, Nigrocin-	GLFGKILGVGKKVLCGLSGMC	2414
  	2GRb (frog)
  AP00581	Ref, Nigrocin-	GLLSGILGAGKNIVCGLSGLC	2415
  	2GRc (frog)
  AP00582	Ref, Brevinin-	GFSSLFKAGAKYLLKSVGKAGAQ	2416
  	2GHa (frog)	QLACKAANNCA
  AP00583	Ref, Brevinin-	GVITDALKGAAKTVAAELLRKAH	2417
  	2GHb (frog)	CKLTNSC
  AP00584	Ref, Guentherin	VIDDLKKVAKKVRRELLCKKHHK	2418
  	(frog)	KLN
  AP00585	Ref, Brevinin-	SIWEGIKNAGKGFLVSILDKVRCK	2419
  	2GHc (frog)	VAGGCNP
  AP00586	Ref, Temporin-GH	FLPLLFGAISHLL	2420
  	(frog)
  AP00587	Ref, Brevinin-2T Sa	GIMSLFKGVLKTAGKHVAGSLVD	2421
  	(frog)	QLKCKITGGC
  AP00588	Ref, Brevinin-1T Sa	FLGSIVGALASALPSLISKIRN	2422
  	(frog)
  AP00589	Ref, Temporin-	FLGALAKIISGIF	2423
  	1T S a (frog)
  AP00593	Ref, B revi nin-1CSa	FLPILAGLAAKIVPKLFCLATKKC	2424
  	(frog)
  AP00594	Ref, Temporin-	FLPIVGKLLSGLL	2425
  	1CSa (frog)
  AP00595	Ref, Temporin-	FLPIIGKLLSGLL	2426
  	1CSb (frog)
  AP00596	Ref, Temporin-	FLPLVTGLLSGLL	2427
  	1CSc (frog)
  AP00597	Ref, Temporin-	NFLGTLVNLAKKIL	2428
  	1CSd (frog)
  AP00598	Ref, Temporin-	FLSAITSLLGKLL	2429
  	1SPb (frog)
  AP00599	Ref, Brevinin-2-	GIWDTIKSMGKVFAGKILQNL	2430
  	related (frog)
  AP00600	Ref, Odorranain-	GLLRASSVWGRKYYVDLAGCAKA	2431
  	HP (frog)
  AP00601	Ref, Brevinin-	FLSLALAALPKFLCLVFKKC	2432
  	1DYa (frog)
  AP00602	Ref, Brevinin-	FLSLALAALPKLFCLIFKKC	2433
  	1DYb (frog)
  AP00603	Ref, Brevinin-	FLPLLLAGLPKLLCLFFKKC	2434
  	1DYc (frog)
  AP00607	Ref, Brevinin-	GLFDVVKGVLKGAGKNVAGSLLE	2435
  	2DYb (frog)	QLKCKLSGGC
  AP00608	Ref, Brevinin-	GLFDVVKGVLKGVGKNVAGSLLE	2436
  	2DYc (frog)	QLKCKLSGGC
  AP00609	Ref, Brevinin-	GIFDVVKGVLKGVGKNVAGSLLE	2437
  	2DYd (frog)	QLKCKLSGGC
  AP00610	Ref, Brevinin-	GLFSVVTGVLKAVGKNVAKNVGG	2438
  	2DYe (frog)	SLLEQLKCKISGGC
  AP00611	Ref, Temporin-	FIGPIISALASLFG	2439
  	1DYa (frog)
  AP00615	Ref, Palustrin-1b	ALFSILRGLKKLGNMGQAFVNCKI	2440
  	(frog)	YKKC
  AP00616	Ref, Palustrin-1c	ALSILRGLEKLAKMGIALTNCKAT	2441
  	(frog)	KKC
  AP00617	Ref, Palustrin-1d	ALSILKGLEKLAKMGIALTNCKAT	2442
  	(frog)	KKC
  AP00619	Ref, Palustrin-2b	GFFSTVKNLATNVAGTVIDTLKCK	2443
  	(frog)	VTGGCRS
  AP00620	Ref, Palustrin-2c	GFLSTVKNLATNVAGTVIDTLKCK	2444
  	(frog)	VTGGCRS
  AP00621	Ref, Palustrin-3a	GIFPKIIGKGIKTGIVNGIKSLVKGV	2445
  	(frog)	GMKVFKAGLNNIGNTGCNEDEC
  AP00622	Ref, Palustrin-3b	GIFPKIIGKGIKTGIVNGIKSLVKGV	2446
  	(frog)	GMKVFKAGLSNIGNTGCNEDEC
  AP00624	Ref, human ALL-	ALLGDFFRKSKEKIGKEFKRIVQRI	2447
  	38 (an LL-37	KDFLRNLVPRTES
  	analog released
  	from its precursor
  	hCAP-18 by
  	gastricsin in vivo)
  AP00625	Ref, human KR-20	KRIVQRIKDFLRNLVPRTES	2448
  	(KR20 from LL-
  	37)
  AP00626	Ref, human KS-30	KSKEKIGKEFKRIVQRIKDFLRNLV	2449
  	(KS30 from LL-37)
  		PRTES
  AP00627	Ref, human RK-31	RKSKEKIGKEFKRIVQRIKDFLRNL	2450
  	(RK31 from LL-	VPRTES
  	37)
  AP00628	Ref, human LL-23	LLGDFFRKSKEKIGKEFKRIVQR	2451
  	(LL23 from LL-37)
  AP00629	Ref, human LL-29	LLGDFFRKSKEKIGKEFKRIVQRIK	2452
  	(LL29 from LL-37)	DFLR
  AP00630	Ref, Amoeba	GEILCNLCTGLINTLENLLTTKGAD	2453
  	peptide (protozoan
  	para
  AP00631	Ref, Mundticin	KYYGNGVSCNKKGCSVDWGKAIG	2454
  	(bacteria)	IIGNNSAANLATGGAAGWSK
  AP00638	Ref, Citropin 2.1	GLIGSIGKALGGLLVDVLKPKL	2455
  	(frog)
  AP00639	Ref, Citropin 2.1.3	GLIGSIGKALGGLLVDVLKPKLQA	2456
  	(frog)	AS
  AP00640	Ref, Maculatin 1.3	GLLGLLGSVVSHVVPAIVGHF	2457
  	(frog)
  AP00641	Ref, Pardaxin 1	GFFALIPKIISSPLFKTLLSAVGSALS	2458
  	(Pardaxin P-1,	SSGEQE
  	Pardaxin P1, Pa1,
  	flat fish)
  AP00642	Ref, Pardaxin 2	GFFALIPKIISSPIFKTLLSAVGSALS	2459
  	(Pardaxin P-2,	SSGGQE
  	Pardaxin P2,Pa2,
  	flat fish)
  AP00643	Ref, Pardaxin 3	GFFAFIPKIISSPLFKTLLSAVGSALS	2460
  	(Pardaxin P-3,	SSGEQE
  	Pardaxin P3,Pa3,
  	flat fish)
  AP00645	Ref, Pardaxin 5	GFFAFIPKIISSPLFKTLLSAVGSALS	2461
  	(Pardaxin P-5,	SSGDQE
  	Pardaxin P5, Pa5,
  	flat fish)
  AP00647	Ref, Brevinin-1PLb	FLPLIAGLAANFLPKIFCAITKKC	2462
  	(frog)
  AP00648	Ref, Brevinin-1PLc	FLPVIAGVAAKFLPKIFCAITKKC	2463
  	(frog)
  AP00649	Ref, Esculentin-	GLFPKINKKKAKTGVFNIIKTVGKE	2464
  	1PLa (frog)	AGMDLIRTGIDTIGCKIKGEC
  AP00650	Ref, Esculentin-	GIFTKINKKKAKTGVFNIIKTIGKEA	2465
  	1PLb (frog)	GMDVIRAGIDTISCKIKGEC
  AP00651	Ref, Esculentin-	GLFSILKGVGKIALKGLAKNMGK	2466
  	2PLa (frog)	MGLDLVSCKISKEC
  AP00652	Ref, Ranatuerin-	GIMDTVKNVAKNLAGQLLDKLKC	2467
  	2PLa (frog)	KITAC
  AP00653	Ref, Ranatuerin-	GIMDTVKNAAKDLAGQLLDKLKC	2468
  	2PLb (frog)	RITGC
  AP00654	Ref, Ranatuerin-	GLLDTIKNTAKNLAVGLLDKIKCK	2469
  	2PLc (frog)	MTGC
  AP00655	Ref, Ranatuerin-	GIMDSVKNVAKNIAGQLLDKLKC	2470
  	2PLd (frog)	KITGC
  AP00656	Ref, Ranatuerin-	GIMDSVKNAAKNLAGQLLDTIKCK	2471
  	2PLe (frog)	ITAC
  AP00657	Ref, Ranatuerin-	GIMDTVKNAAKDLAGQLDKLKCR	2472
  	2PLf (frog)	ITGC
  AP00658	Ref, Temporin-	FLPLVGKILSGLI	2473
  	1PLa (frog)
  AP00659	Ref, Ranatuerin 5	FLPIASLLGKYL	2474
  	(frog)
  AP00661	Ref, Esculentin-2L	GILSLFTGGIKALGKTLFKMAGKA	2475
  	(frog)	GAEHLACKATNQC
  AP00662	Ref, Esculentin-2B	GLFSILRGAAKFASKGLGKDLTKL	2476
  	(ESC2B-RANBE,	GVDLVACKISKQC
  	frog)
  AP00663	Ref, Esculentin-2P	GFSSIFRGVAKFASKGLGKDLARL	2477
  	(frog)	GVNLVACKISKQC
  AP00664	Ref, Peptide A1	FLPAIAGILSQLF	2478
  	(frog)
  AP00665	Ref, Peptide B9	FLPLIAGLIGKLF	2479
  	(frog)
  AP00666	Ref, PG-L (frog)	EGGGPQWAVGHFM	2480
  AP00667	Ref, PG-KI (frog)	EPHPDEFVGLM	2481
  AP00668	Ref, PG-KIT (frog)	EPNPDEFVGLM	2482
  AP00669	Ref, PG-KIII (frog)	EPHPNEFVGLM	2483
  AP00670	Ref, PG-SPI (frog)	EPNPDEFFGLM	2484
  AP00660	Ref, Pandinin 2	FWGALAKGALKLIPSLFSSFSKKD	2485
  	(African scorpion)
  AP00671	Ref, PG-SPIT (frog)	EPNPNEFFGLM	2486
  AP00673	Ref, Lantibiotic	WKSESVCTPGCVTGVLQTCFLQTI	2487
  	Ericin S (bacteria	TCNCHISK
  AP00674	Ref, Lantibiotic	VLSKSLCTPGCITGPLQTCYLCFPT	2488
  	Ericin A (bacteria	FAKC
  AP00675	Ref, Human beta	FELDRICGYGTARCRKKCRSQEYRI	2489
  	defensin 4 (HBD-4,	GRCPNTYACCLRKWDESLLNRTKP
  	HBD4, human
  	defensin)
  AP00676	Ref, RL-37 (RL37,	RLGNFFRKVKEKIGGGLKKVGQKI	2490
  	monkey	KDFLGNLVPRTAS
  	cathelicidin)
  AP00677	Ref, CAP11	GLRKKFRKTRKRIQKLGRKIGKTG	2491
  	(Guinea pig	RKVWKAWREYGQIPYPCRI
  	cathelicidin)
  AP00678	Ref, Canine	RLKELITTGGQKIGEKIRRIGQRIKD	2492
  	cathelicidin	FFKNLQPREEKS
  	(K9CATH) (dog)
  AP00679	Ref, Esculentin	GLFSILKGVGKIAIKGLGKNLGKM	2493
  	2VEb (frog)	GLDLVSCKISKEC
  AP00680	Ref, SMAP-34	GLFGRLRDSLQRGGQKILEKAERI	2494
  	(sheep cathelicidin)	WCKIKDIFR
  AP00681	Ref, OaBac5	RFRPPIRRPPIRPPFRPPFRPPVRPPIR	2495
  	(sheep cathelicidin)	PPFRPPFRPPIGPFP
  AP00682	Ref, OaBac6	RRLRPRHQHFPSERPWPKPLPLPLP	2496
  	(sheep cathelicidin)	RPGPRPWPKPLPLPLPRPGLRPWPK
  		PL
  AP00683	Ref, OaBac7.5	RRLRPRRPRLPRPRPRPRPRPRSLPL	2497
  	(sheep cathelicidin)	PRPQPRRIPRPILLPWRPPRPIPRP	Q I
  		QPIPRWL
  AP00684	Ref, OaBac11	RRLRPRRPRLPRPRPRPRPRPRSLPL	2498
  	(sheep cathelicidin)	PRPKPRPIPRPLPLPRPRPKPIPRPLP
  		LPRPRPRRIPRPLPLPRPRPRPIPRPL
  		PLPQPQPSPIPRPL
  AP00685	Ref, Ranatuerin	GIMDTVKGVAKTVAASLLDKLKC	2499
  	2VEb (frog)	KITGC
  AP00686	Ref, eCATH-1	KRFGRLAKSFLRMRILLPRRKILLA	2500
  	(horse cathelicidin)	S
  AP00687	Ref, eCATH-2	KRRHWFPLSFQEFLEQLRRFRDQL	2501
  	(horse cathelicidin)	PFP
  AP00688	Ref, eCATH-3	KRFHSVGSLIQRHQQMIRDKSEAT	2502
  	(horse cathelicidin)	RHGIRIITRPKLLLAS
  AP00689	Ref, P rop h eni n-1	AFPPPNVPGPRFPPPNFPGPRFPPPN	2503
  	(pig cathelicidin)	FPGPRFPPPNFPGPRFPPPNFPGPPFP
  		PPIFPGPWFPPPPPFRPPPFGPPRFP
  AP00690	Ref, Prophenin-2	AFPPPNVPGPRFPPPNVPGPRFPPPN	2504
  	(pig cathelicidin)	FPGPRFPPPNFPGPRFPPPNFPGPPFP
  		PPIFPGPWFPPPPPFRPPPFGPPRFP
  AP00691	Ref, HFIAP-1	GFFKKAWRKVKHAGRRVLDTAK	2505
  	(hagfish	GVGRHYVNNWLNRYR
  	cathelicidin)
  AP00692	Ref, HFIAP-3	GWFKKAWRKVKNAGRRVLKGVG	2506
  	(hagfish	IHYGVGLI
  	cathelicidin)
  AP00693	Ref, Trout cath	RICSRDKNCVSRPGVGSIIGRPGGG	2507
  	(fish cathelicidin)	SLIGRPGGGSVIGRPGGGSPPGGGS
  		FNDEFIRDHSDGNRFA
  AP00694	Ref, MRP	AIGSILGALAKGLPTLISWIKNR	2508
  	(melittin-related
  	peptide)
  AP00695	Ref, Temporin-	FLPILGKLLSGIL	2509
  	1TGa (frog)
  AP00696	Ref, Dahlein 1.1	GLFDIIKNIVSTL	2510
  	(frog)
  AP00697	Ref, Dahlein 1.2	GLFDIIKNIFSGL	2511
  	(frog)
  AP00698	Ref, Dahlein 4.1	GLWQLIKDKIKDAATGFVTGIQS	2512
  	(frog)
  AP00699	Ref, Dahlein 4.2	GLWQFIKDKLKDAATGLVTGIQS	2513
  	(frog)
  AP00700	Ref, Dahlein 4.3	GLWQFIKDKFKDAATGLVTGIQS	2514
  	(frog)
  AP00701	Ref, Dahlein 5.1	GLLGSIGNAIGAFIANKLKP	2515
  	(frog)
  AP00702	Ref, Dahlein 5.2	GLLGSIGNAIGAFIANKLKPK	2516
  	(frog)
  AP00703	Ref, Dahlein 5.3	GLLASLGKVLGGYLAEKLKP	2517
  	(frog)
  AP00704	Ref, Dahlein 5.4	GLLGSIGKVLGGYLAEKLKPK	2518
  	(frog)
  AP00705	Ref, Dahlein 5.5	GLLASLGKVLGGYLAEKLKPK	2519
  	(frog)
  AP00706	Ref, Dahlein 5.6	GLLASLGKVFGGYLAEKLKPK	2520
  	(frog)
  AP00709	Ref, Mytilus	GFGCPNDYPCHRHCKSIPGRAGGY	2521
  	defensin (mytilin)	CGGAHRLRCTCYR
  	A (mollusc)
  AP00711	Ref, Mussel	GFGCPNNYACHQHCKSIRGYCGG	2522
  	defensin MGD2	YCAGWFRLRCTCYRCG
  AP00712	Ref, scorpion	GFGCPLNQGACHRHCRSIRRRGGY	2523
  	defensin	CAGFFKQTCCYRN
  AP00713	Ref, Androctonus	GFGCPFNQGACHRHCRSIRRRGGY	2524
  	defensin	CAGLFKQTCTCYR
  AP00714	Ref, Orinthodoros	GYGCPFNQYQCHSHCSGIRGYKGG	2525
  	defensin A (soft	YCKGTFKQTCKCY
  	ticks)
  AP00715	Ref, VaD1 (plant	RTCMKKEGWGKCLIDTTCAHSCK	2526
  	defensin)	NRGYIGGNCKGMTRTCYCLVNC
  AP00722	Ref, Cryptonin	GLLNGLALRLGKRALKKIIKRLCR	2527
  	(insect, cicada)
  AP00723	Ref, Decoralin	SLLSLLRKLIT	2528
  	(insect)
  AP00724	Ref, RTD-2 (rhesus	RCLCRRGVCRCLCRRGVC	2529
  	theta-defensin-2,
  	minidefensin,
  	XXC, BBS, lectin,
  	ZZHa)
  AP00725	Ref, RTD-3 (rhesus	RCICTRGFCRCICTRGFC	2530
  	theta-defensin-3,
  	minidefensin,
  	XXC, BBS, lectin,
  	ZZHa)
  AP00726	Ref, Combi-1	RRWWRF	2531
  	(synthetic)
  AP00748	Ref, Gm pro-rich	DIQIPGIKKPTHRDIIIPNWNPNVRT	2532
  	peptl (insect)	QPWQRFGGNKS
  AP00749	Ref, Gm anionic	EADEPLWLYKGDNIERAPTTADHP	2533
  	pept 1 (insect)	ILPSIIDDVKLDPNRRYA
  AP00750	Ref, Gm pro-rich	EIRLPEPFRFPSPTVPKPIDIDPILPHP	2534
  	pept 2 (insect)	WSPRQTYPIIARRS
  AP00752	Ref, Gm defensin-	DKLIGSCVWGATNYTSDCNAECK	2535
  	like peptide (insect)	RRGYKGGHCGSFWNVNCWCEE
  AP00753	Ref, Gm	VQETQKLAKTVGANLEETNKKL	A 2536
  	apolipophoricin	PQIKSAYDDFVKQAQEVQKKLHE
  	(insect)	AASKQ
  AP00754	Ref, Gm anionic	ETESTPDYLKNIQQQLEEYTKNFNT	2537
  	pept2 (insect)	QVQNAFDSDKIKSEVNNFIESLGKI
  		LNTEKKEAPK
  AP00755	Ref, Gm cecropin	ENFFKEIERAGQRIRDAIISAAPAVE	2538
  	D-like pept,insect	TLAQAQKIIKGGD
  AP00756	Ref, Dermaseptin-	ALWKDILKNAGKAALNEINQLVN	2539
  	B6 (DRS-B6, DRS	Q
  	B6, XXA, frog)
  AP00759	Ref, Phylloseptin-	FLSLIPHAINAVSTLVHHSG	2540
  	O1 (PLS-O1,
  	Phylloseptin-4, PS-
  	4, XXA, frog)
  AP00760	Ref, Phylloseptin-	FLSLIPHAINAVSAIAKHS	2541
  	O2 (PLS-O2,
  	Phylloseptin-5, PS-
  	5, XXA, frog)
  AP00761	Ref, Phylloseptin-6	SLIPHAINAVSAIAKHF	2542
  	(Phylloseptin-H4,
  	PLS-H4, PS-6,
  	XXA, frog)
  AP00762	Ref, Phylloseptin-7	FLSLIPHAINAVSAIAKHF	2543
  	(Phylloseptin-H5,
  	PLS-H5, PS-7,
  	XXA, frog)
  AP00763	Ref, Dermaseptin	GLWSTIKNVGKEAAIAAGKAALG	2544
  	DPh-1 (XXA, frog)	AL
  AP00764	Ref, Dermaseptin-	GLRSKIWLWVLLMIWQESNKFKK	2545
  	S9 (DRS-S9, DRS	M
  	S9, frog)
  AP00765	Ref, Human salvic	MHDFWVLWVLLEYIYNSACSVLS	2546
  		ATSSVSSRVLNRSLQVKVVKITN
  AP00766	Ref, Gassericin A	IYWIADQFGIHLATGTARKLLDAM	2547
  	(XXC, XXD2,	ASGASLGTAFAAILGVTLPAWALA
  	class IV	AAGALGATAA
  	bacteriocin, Gram-
  	positive bacteria)
  AP00767	Ref, Circularin	AVAGALGVQTAAATTIVNVILNAGT	2548
  	(XXC, class IV	LVTVLGIIASIASGGAGTLMTIGWA
  	bacteriocin, Gram-	TFKATVQKLAKQSMARAIAY
  	positive bacteria)
  AP00768	Ref, Closticin 574	PNWTKIGKCAGSIAWAIGSGLFGG	2549
  	(bacteria)	AKLIKIKKYIAELGGLQKAAKLLV
  		GATTWEEKLHAGGYALINLAAELT
  		GVAGIQANCF
  AP00769	Ref, Caerin 1.11	GLLGAMFKVASKVLPHVVPAITEH	2550
  	(XXA, frog)	F
  AP00770	Ref, Maculatin 1.4	GLLGLLGSVVSHVLPAITQHL	2551
  	(XXA, frog)
  AP00771	Ref, Magainin 1	GIGKFLHSAGKFGKAFVGEIMKS	2552
  	(frog)
  AP00772	Ref, Oxyopinin 1	FRGLAKLLKIGLKSFARVLKKVLP	2553
  	(spider)	KAAKAGKALAKSMADENAIRQQN
  		Q
  AP00773	Ref, Oxyopinin 2a	GKFSVFGKILRSIAKVFKGVGKVR	2554
  	(spider)	KQFKTASDLDKNQ
  AP00774	Ref, Oxyopinin 2b	GKFSGFAKILKSIAKFFKGVGKVR	2555
  	(spider)	KGFKEASDLDKNQ
  AP00775	Ref, Oxyopinin 2c	GKLSGISKVLRAIAKFFKGVGKAR	2556
  	(spider)	KQFKEASDLDKNQ
  AP00776	Ref, Oxyopinin 2d	GKFSVFSKILRSIAKVFKGVGKVRK	2557
  	(spider)	GFKTASDLDKNQ
  AP00777	Ref, NRC-1 (XXA,	GKGRWLERIGKAGGIIIGGALDHL	2558
  	fish, gene
  	predicted)
  AP00778	Ref, NRC-2 (XXA,	WLRRIGKGVKIIGGAALDHL	2559
  	fish, gene
  	predicted)
  AP00779	Ref, NRC-3 (XXA,	GRRKRKWLRRIGKGVKIIGGAALD	2560
  	fish, gene	HL
  	predicted)
  AP00781	Ref, NRC-5 (XXA,	FLGALIKGAIHGGRFIHGMIQNHH	2561
  	fish, gene
  	predicted)
  AP00782	Ref, NRC-6 (XXA,	GWGSIFKHGRHAAKHIGHAAVNH	2562
  	fish, gene	YL
  	predicted)
  AP00783	Ref, NRC-7 (XXA,	RWGKWFKKATHVGKHVGKAALT	2563
  	fish, gene	AYL
  	predicted)
  AP00784	Ref, NRC-10	FFRLLFHGVHHVGKIKPRA	2564
  	(XXA, fish, gene
  	predicted)
  AP00785	Ref, NRC-11	GWKSVFRKAKKVGKTVGGLALD	2565
  	(XXA, fish, gene	HYL
  	predicted)
  AP00786	Ref, NRC-12	GWKKWFNRAKKVGKTVGGLAVD	2566
  	(XXA, fish, gene	HYL
  	predicted)
  AP00787	Ref, NRC-13	GWRLLLKKAEVKTVGKLALKHYL	2567
  	(XXA, fish, gene
  	predicted)
  AP00788	Ref, NRC-14	AGWGSIFKHIFKAGKFIHGAIQAHN	2568
  	(XXA, fish, gene	D
  	predicted)
  AP00789	Ref, NRC-15	GFWGKLFKLGLHGIGLLHLHL	2569
  	(XXA, fish, gene
  	predicted)
  AP00790	Ref, NRC-16	GWKKWLRKGAKHLGQAAIK	2570
  	(XXA, fish, gene
  	predicted)
  AP00791	Ref, NRC-17	GWKKWLRKGAKHLGQAAIKGLA	2571
  	(XXA, fish, gene	S
  	predicted)
  AP00792	Ref, NRC-19	FLGLLFHGVHHVGKWIHGLIHGHH	2572
  	(XXA, fish, gene
  	predicted)
  AP00793	Ref, Bombinin H2	IIGPVLGLVGSALGGLLKKI	2573
  	(XXA, frog)
  AP00794	Ref, Bombinin H3	IIGPVLGMVGSALGGLLKKI	2574
  	(frog, XXD, XXA)
  AP00795	Ref, Bombinin H7	ILGPILGLVSNALGGLL	2575
  	(frog, XXD, XXA)
  AP00796	Ref, Bombinin GH-	IIGPVLGLVGKPLESLLE	2576
  	1L (XXA, toad)
  AP00797	Ref, Bombinin GH-	IIGPVLGLVGKPLESLLE	2577
  	1D (toad,XXD,
  	XXA)
  AP00807	Ref, Enterocin E-	NRWYCNSAAGGVGGAAGCVLAG	2578
  	760 (bacteriocin,	YVGEAKENIAGEVRKGWGMAGGF
  	bacteria)	THNKACKSFPGSGWASG
  AP00808	Ref, hepcidin (fish)	CRFCCRCCPRMRGCGLCCRF	2579
  AP00809	Ref, hepcidin TH1-	GIKCRFCCGCCTPGICGVCCRF	2580
  	5 (fish)
  AP00810	Ref, hepcidin TH2-	QSHLSLCRWCCNCCRSNKGC	2581
  	3 (fish)
  AP00811	Ref, human LEAP-	MTPFWRGVSLRPIGASCRDDSECIT	2582
  	2	RLCRKRRCSLSVAQE
  AP00812	Ref, Enkelytin	FAEPLPSEEEGESYSKEPPEMEKRY	2583
  	(cow)	GGFM
  AP00732	Ref, Spheniscin-1	SFGLCRLRRGSCAHGRCRFPSIPIG	2584
  	(Sphe-1, avian	RCSRFVQCCRRVW
  	defensin)
  AP00733	Ref, Organgutan	LLGDFFRKAREKIGEEFKRIVQRIK	2585
  	ppyLL-37 (Great	DFLRNLVPRTES
  	Ape, primate
  	cathelicidin)
  AP00734	Ref, Gibbon	SLGNFFRKARKKIGEEFKRIVQRIK	2586
  	hmdSL-37	DFLQHLIPRTEA
  	(hylobatidae,
  	primate
  	cathelicidin)
  AP00735	Ref, pobRL-37	RLGNFFRKAKKKIGRGLKKIGQKI	2587
  	(cercopithecidae,	KDFLGNLVPRTES
  	primate
  	cathelicidin)
  AP00736	Ref, cjaRL-37	RLGDILQKAREKIEGGLKKLVQKI	2588
  	(primate	KDFFGKFAPRTES
  	cathelicidin)
  AP00737	Ref, Plasticin	GLVTSLIKGAGKLLGGLFGSVTG	2589
  	PBN2KF (XXA,
  	DRP-PBN2, frog)
  AP00738	Ref, Plasticin	GLVTGLLKTAGKLLGDLFGSLTG	2590
  	ANCKF (XXA,
  	synthetic)
  AP00739	Ref, Plasticin	GVVTDLLKTAGKLLGNLFGSLSG	2591
  	PD36KF (XXA,
  	synthetic)
  AP00740	Ref, Plasticin	GVVTDLLKTAGKLLGNLVGSLSG	2592
  	PD36K (XXA,
  	synthetic)
  AP00741	Ref, Chicken	PITYLDAILAAVRLLNQRISGPCILR	2593
  	cathelicidin-B1	LREAQPRPGWVGTLQRRREVSFLV
  	(bird cathelicidin)	EDGPCPPGVDCRSCEPGALQHCVG
  		TVSIEQQPTAELRCRPLRPQ
  AP00742	Ref, Chicken	MRILYLLLSVLFVVLQGVAGQPYF	2594
  	gallinacin 4 (Gal 4)	SSPIHACRYQRGVCIPGPCRWPYY
  		RVGSCGSGLKSCCVRNRWA
  AP00743	Ref, Chicken	MKILCFFIVLFVAVHGAVGFSRSPR	2595
  	gallinacin 7 (Gal 7)	YHMQCGYRGTFCTPGKCPYGNAY
  		LGLCRPKYSCCRWL
  AP00744	Ref, Chicken	MQILPLLFAVLLLMLRAEPGLSLA	2596
  	gallinacin 9 (Gal 9)	RGLPQDCERRGGFCSHKSCPPGIGR
  		IGLCSKEDFCCRSRWYS
  AP00745	Ref, Chicken	MTPFWRGVSLRPVGASCRDNSECI	2597
  	LEAP-2 (cLEAP-	TMLCRKNRCFLRTASE
  	2)
  AP00814	Ref, Caerulein	GLGSILGKILNVAGKVGKTIGKVA	2598
  	precursor-related	DAVGNKE
  	fragment Ea
  	(CPRF-Ea, frog)
  AP00815	Ref, Caerulein	GLGSFLKNAIKIAGKVGSTIGKVAD	2599
  	precursor-related	AIGNKE
  	fragment Eb
  	(CPRF-Eb, frog)
  AP00816	Ref, Caerulein	GLGSFFKNAIKIAGKVGSTIGKVAD	2600
  	precursor-related	AIGNKE
  	fragment Ec
  	(CPRF-Ec, frog)
  AP00817	Ref, Temporin-10a	FLPLLASLFSRLL	2601
  	(frog)
  AP00818	Ref, Temporin-10b	FLPLIGKILGTIL	2602
  	(frog)
  AP00819	Ref, Temporin-10c	FLPLLASLFSRLF	2603
  	(frog)
  AP00820	Ref, Temporin-10d	FLPLLASLFSGLF	2604
  	(frog)
  AP00821	Ref, Brevinin-20a	GLFNVFKGLKTAGKHVAGSLLNQ	2605
  	(frog)	LKCKVSGGC
  AP00822	Ref, Brevinin-20b	GIFNVFKGALKTAGKHVAGSLLNQ	2606
  	(frog)	LKCKVSGEC
  AP00824	Ref, Temporin-1Gb	SILPTIVSFLSKFL	2607
  	(XXA, frog)
  AP00825	Ref, Temporin-1Gc	SILPTIVSFLTKFL	2608
  	(XXA, frog)
  AP00826	Ref, Temporin-1Gd	FILPLIASFLSKFL	2609
  	(XXA, frog)
  AP00827	Ref, Ranatuerin-	SMISVLKNLGKVGLGFVACKVNK	2610
  	1Ga (frog)	QC
  AP00829	Ref, Ranalexin-1G	FLGGLMKIIPAAFCAVTKKC	2611
  	(frog)
  AP00830	Ref, Ranatuerin-2G	GLLLDTLKGAAKDIAGIALEKLKC	2612
  	(frog)	KITGCKP
  AP00831	Ref, Odorranain-	GLLSGILGAGKHIVCGLTGCAKA	2613
  	NR (frog)
  AP00832	Ref, Maximin H1	ILGPVISTIGGVLGGLLKNL	2614
  	(XXA, toad)
  AP00834	Ref, G. mellonella	KVNANAIKKGGKAIGKGFKVISAA	2615
  	moricin-like	STAHDVYEHIKNRRH
  	peptide A (Gm-
  	mlpA, insect)
  AP00835	Ref, G. mellonella	GKIPVKAIKKGGQIIGKALRGINIAS	2616
  	moricin-like	TAHDIISQFKPKKKKNH
  	peptide B (Gm-
  	m1pB, insect)
  AP00836	Ref, G. mellonella	KVPIGAIKKGGKIIKKGLGVIGAAG	2617
  	moricin-like	TAHEVYSHVKNRH
  	peptide Cl (Gm-
  	m1pC1, insect)
  AP00837	Ref, G. mellonella	KVPIGAIKKGGKIIKKGLGVLGAA	2618
  	moricin-like	GTAHEVYNHVRNRQ
  	peptide C2 (Gm-
  	m1pC2, insect)
  AP00838	Ref, G. mellonella	KVPIGAIKKGGKIIKKGLGVIGAAG	2619
  	moricin-like	TAHEVYSHVKNRQ
  	peptide C3 (Gm-
  	m1pC3, insect)
  AP00839	Ref, G. mellonella	KVPVGAIKKGGKAIKTGLGVVGA	2620
  	moricin-like	AGTAHEVYSHIRNRH
  	peptide C4/C5
  	(Gm-m1pC4/C5,
  	insect)
  AP00840	Ref, G. mellonella	KGIGSALKKGGKIIKGGLGALGAIG	2621
  	moricin-like	TGQQVYEHVQNRQ
  	peptide D (Gm-
  	m1pD, insect)
  AP00841	Ref, Enterocin A	TTHSGKYYGNGVYCTKNKCTVD	2622
  	(EntA, class IIA	WAKATTCIAGMSIGGFLGGAIPGK
  	bacteriocin, i.e.	C
  	pediocin-like
  	peptide, bacteria)
  AP00842	Ref, Divercin V41	TKYYGNGVYCNSKKCWVDWGQA	2623
  	(DvnV41, class IIa	SGCIGQTVVGGWLGGAIPGKC
  	bacteriocin,
  	pediocin-like
  	peptide, bacteria.
  	DvnRV41 is the
  	recombinant form)
  AP00843	Ref, Divergicin	TKYYGNGVYCNSKKCWVDWGTA	2624
  	M35 (class IIa	QGCIDVVIGQLGGGIPGKGKC
  	bacteriocin,
  	pediocin-like
  	peptide, bacteria)
  AP00844	Ref, Coagulin	KYYGNGVTCGKHSCSVDWGKATT	2625
  	(bacteriocin,	CIINNGAMAWATGGHQGTHKC
  	pediocin-like
  	peptide, bacteria)
  AP00845	Ref, Listeriocin	KSYGNGVHCNKKKCWVDWGSAIS	2626
  	743A (class IIa	TIGNNSAANWATGGAAGWKS
  	bacteriocin,
  	pediocin-like
  	peptide, bacteria)
  AP00846	Ref, Mundticin	KSKYYGNGVSCNKKGCSVDWGKAIG	2627
  	(enterocin CRL35,	IIGNNSAANLATGGAAGWKS
  	mundticin ATO6,
  	mundticin QU2,
  	class IIa
  	bacteriocin,
  	pediocin-like
  	peptide, bacteria)
  AP00847	Ref, Sakacin 5X	KYYGNGLSCNKSGCSVDWSKAISII	2628
  	(Sak5X, class IIa	GNNAVANLTTGGAAGWKS
  	bacteriocin,
  	pediocin-like
  	peptide, bacteria)
  AP00848	Ref, Leucocin	CKNYGNGVHCTKKGCSVDWGYAW	2629
  	(class IIa	ANIANNSVMNGLTGGNAGWHN
  	bacteriocin,
  	pediocin-like
  	peptide, bacteria)
  AP00849	Ref, Lactococcin	TSYGNGVHCNKSKCWIDVSELETY	2630
  	MMFII (class IIa	KAGTVSNPKDILW
  	bacteriocin,
  	pediocin-like
  	peptide, bacteria)
  AP00850	Ref, Sakacin G	KYYGNGVSCNSHGCSVNWGQAW	2631
  	(SakG, class IIa	TCGVNHLANGGHGVC
  	bacteriocin,
  	pediocin-like
  	peptide, bacteria)
  AP00851	Ref, Plantaricin	KYYGNGVTCGKHSCSVNWGQAFS	2632
  	423 (class IIa	CSVSHLANFGHGKC
  	bacteriocin,
  	pediocin-like
  	peptide, bacteria)
  AP00852	Ref, Plantaricin	KYYGNGLSCSKKGCTVNWGQAFS	2633
  	C19 (class IIa	CGVNRVATAGHHKC
  	bacteriocin,
  	pediocin-like
  	peptide, bacteria)
  AP00853	Ref, Enterocin P	ATRSYGNGVYCNNSKCWVNWGE	2634
  	(EntP, class IIa	AKENIAGIVISGWASGLAGMGH
  	bacteriocin,
  	pediocin-like
  	peptide, bacteria)
  AP00854	Ref, Bacteriocin 31	ATYYGNGLYCNKQKCWVDWNKA	2635
  	(Bac31, Bac31,	SREIGKIIVNGWVQHGPWAPR
  	class IIa
  	bacteriocin,
  	pediocin-like
  	peptide, bacteria)
  AP00855	Ref, MSI-78	GIGKFLKKAKKFGKAFVKILKK	2636
  	(XXA, synthetic)
  AP00856	Ref, MSI-594	GIGKFLKKAKKGIGAVLKVLTTGL	2637
  	(XXA, synthetic)
  AP00857	Ref, Catestatin	SSMKLSFRARAYGFRGPGPQL	2638
  	(human
  	CHGA(352-372),
  	human Cst)
  AP00858	Ref, Temporin D	LLPIVGNLLNSLL	2639
  	(XXA, frog)
  AP00859	Ref, Temporin H	LSPNLLKSLL	2640
  	(XXA, frog)
  AP00861	Ref, Brevinin-ALb	FLPLAVSLAANFLPKLFCKITKKC	2641
  	(frog)
  AP00862	Ref, Brevinin 1E	FLPLLAGLAANFLPKIFCKITKRC	2642
  	(frog)
  AP00863	Ref, Temporin-	FLPIVGKLLSGLSGLL	2643
  	ALa (XXA, frog)
  AP00864	Ref, Temporin	FLPIVGRLISGLL	2644
  	1ARa (XXA, frog)
  AP00865	Ref, Temporin	FLPIIGQLLSGLL	2645
  	1AUa (XXA,
  	Temporin-lAtJa)
  	(frog)
  AP00866	Ref, Temporin	FLPIIAKVLSGLL	2646
  	1Bya (XXA,
  	Temporin-lBya,
  	frog)
  AP00867	Ref, Temporin 1Ec	FLPVIAGLLSKLF	2647
  	(XXA, frog)
  AP00869	Ref, Temporin 1Ja	ILPLVGNLLNDLL	2648
  	(XXA, Temporin-
  	1Ja, frog)
  AP00873	Ref, Temporin 1Pra	ILPILGNLLNGLL	2649
  	(XXA, frog)
  AP00874	Ref, Temporin 1VE	FLPLVGKILSGLI	2650
  	(XXA, frog)
  AP00875	Ref, Temporin 1Va	FLSSIGKILGNLL	2651
  	(XXA, frog)
  AP00876	Ref, Temporin 1Vb	FLSIIAKVLGSLF	2652
  	(XXA, frog)
  AP00877	Ref, Brevinin-lJa	FLGSLIGAAIPAIKQLLGLKK	2653
  	(frog)
  AP00878	Ref, Brevinin-	FLPILASLAAKFGPKLFCLVTKKC	2654
  	1BYa (frog)
  AP00884	Ref, Ixosin-B (tick)	QLKVDLWGTRSGIQPEQHSSGKSD	2655
  		VRRWRSRY
  AP00885	Ref, Brevinin-	FLPILASLAAKLGPKLFCLVTKKC	2656
  	1BYb (frog)
  AP00886	Ref, Brevinin-	FLPILASLAATLGPKLLCLITKKC	2657
  	1BYc (frog)
  AP00887	Ref, Brevinin-	GILSTFKGLAKGVAKDLAGNLLDK	2658
  	2BYa (frog)	FKCKITGC
  AP00888	Ref, Brevinin-	GIMDSVKGLAKNLAGKLLDSLKC	2659
  	2BYb (frog)	KITGC
  AP00891	Ref, Pilosulin 3	IIGLVSKGTCVLVKTVCKKVLKQG	2660
  	(Myr b III)(ants)
  AP00892	Ref, Pilosulin 4	PDITKLNIKKLTKATCKVISKGASM	2661
  	(Myr b IV)(ants)	CKVLFDKKKQE
  AP00893	Ref, Pilosulin 5	DVKGMKKAIKGILDCVIEKGYDKL	2662
  	(Myr b III)(ants)	AAKLKKVIQQLWE
  AP00894	Ref, Ocellatin 4	GLLDFVTGVGKDIFAQLIKQI	2663
  	(XXA, frog)
  AP00895	Ref, OH-CATH	KRFKKFFKKLKNSVKKRAKKFFK	2664
  	(snake cathelicidin,	KPRVIGVSIPF
  	reptile cathelicidin,
  	or elapid
  	cathelicidins)
  AP00896	Ref, BF-CATH	KRFKKFFKKLKKSVKKRAKKFFK	2665
  	(snake cathelicidin)	KPRVIGVSIPF
  AP00897	Ref, NA-CATH	KRFKKFFKKLKNSVKKRAKKFFK	2666
  	(snake cathelicidin)	KPKVIGVTFPF
  AP00898	Ref, Temporin-1Sa	FLSGIVGMLGKLF	2667
  	(XXA, frog)
  AP00899	Ref, Temporin-1Sb	FLPIVTNLLSGLL	2668
  	(XXA, frog)
  AP00900	Ref, Temporin-1Sc	FLSHIAGFLSNLF	2669
  	(XXA, frog)
  AP00913	Ref, Ib-AMP1	EWGRRCCGWGPGRRYCVRWC	2670
  	(IbAMP1, plant
  	defensin)
  AP00914	Ref, Ib-AMP2	QYGRRCCNWGPGRRYCKRWC	2671
  	(IBAMP2, plant
  	defensin)
  AP00915	Ref, Ee-CBP	QQCGRQAGNRRCANNLCCSQYGY	2672
  	(EeCBP, plant	CGRTNEYCCTSQGCQSQCRRCG
  	defensin, hevein-
  	type, E. europaeus
  	chitin-binding
  	protein)
  AP00916	Ref, Pa-AMP1	AGCIKNGGRCNASAGPPYCCSSYC	2673
  	(PaAMP1, plant	FQIAGQSYGVCKNR
  	defensin, C6 type)
  AP00917	Ref, Pa-AMP2	ACIKNGGRCVASGGPPYCCSNYCL	2674
  	(PaAMP2, plant	QIAGQSYGVCKKH
  	defensin, C6 type)
  AP00924	Ref, Ornithodoros	GYGCPFNQYQCHSHCRGIRGYKG	2675
  	defensin B (soft	GYCTGRFKQTCKCY
  	ticks)
  AP00925	Ref, Ornithodoros	GYGCPFNQYQCHSHCSGIRGYKGG	2676
  	defensin C (soft	YCKGLFKQTCNCY
  	ticks)
  AP00926	Ref, Ornithodoros	GFGCPFNQYECHAHCSGVPGYKG	2677
  	defensin D (soft	GYCKGLFKQTCNCY
  	ticks)
  AP00927	Ref,	IYFIADKMGIQLAPAWYQDIVNWV	2678
  	Butyrivibriocin	SAGGTLTTGFAIIVGVTVPAWIAEA
  	AR10 (XXC, class	AAAFGIASA
  	IV bacteriocin,
  	gram-positive
  	bacteria)
  AP00929	Ref, AS-48	ASLQFLPIAHMAKEFGIPAAVAGT	2679
  	(enterocin 4, XXC,	VINVVEAGGWVTTIVSILTAVGSG
  	class IV bacteriocin	GLSLLAAAGRESIKAYLKKEIKKK
  	or class lid	GKRAVIAW
  	bacteriocin, Gram-
  	positive bacteria)
  AP00930	Ref, Reutericin 6	IYWIADQFGIHLATGTARKLLDAM	2680
  	(XXC, XXD1,	ASGASLGTAFAAILGVTLPAWALA
  	class IV	AAGALGATAA
  	bacteriocin, Gram-
  	positive bacteria)
  AP00931	Ref, Uberolysin	LAGYTGIASGTAKKVVDAIDKGAA	2681
  	(XXC, class IV	AFVIISIISTVISAGALGAVSASADFI
  	bacteriocin, Gram-	ILTVKNYISRNLKAQAVIW
  	positive bacteria)
  AP00932	Ref, Acidocin B	IYWIADQFGIHLATGTARKLLDAV	2682
  	(XXC, class IV	ASGASLGTAFAAILGVTLPAWALA
  	bacteriocin, Gram-	AAGALGATAA
  	positive bacteria)
  AP00980	Ref, Phormia	ATCDLLSGTGINHSACAAHCLLRG	2683
  	defensin B (insect	NRGGYCNRKGVCVCRN
  	defensin B)
  AP00990	Ref, Pth-St1 (plant	RNCESLSHRFKGPCTRDSN	2684
  	defensin)
  AP00991	Ref, Snakin-1	GSNFCDSKCKLRCSKAGLADRCLK	2685
  	(StSN1, plant	YCGICCEECKCVPSGTYGNKHECP
  	defensin)	CYRDKKNSKGKSKCP
  AP00992	Ref, Snakin-2	YSYKKIDCGGACAARCRLSSRPRL	2686
  	(StSN2, plant	CNRACGTCCARCNCVPPGTSGNTE
  	defensin)	TCPCYASLTTHGNKRKCP
  AP00993	Ref, So-D2 (S.	GIFSSRKCKTPSKTFKGICTRDSNC	2687
  	oleracea defensin	DTSCRYEGYPAGDCKGIRRRCMCS
  	D2, plant defensin)	KPC
  AP00994	Ref, So-D6 (S.	GIFSNMYARTPAGYFRGP	2688
  	oleracea defensin
  	D6, plant defensin)
  AP00997	Ref, Nisin Q	ITSISLCTPGCKTGVLMGCNLKTAT	2689
  	(lantibiotic,	CNCSVHVSK
  	bacteriocins,
  	bacteria)
  AP01008	Ref, Tachystatin	YSRCQLQGFNCVVRSYGLPTIPCC	2690
  	A1 (BBS,	RGLTCRSYFPGSTYGRCQRF
  	horseshoe crabs)
  AP01009	Ref, Tachystatin C	DYDWSLRGPPKCATYGQKCRTWS	2691
  	(BBS, horseshoe	PRNCCWNLRCKAFRCRPR
  	crabs)
  AP01012	Ref, Latarcin 3a	SWKSMAKKLKEYMEKLKQRA	2692
  	(Ltc3a, XXA,
  	BBM, spider)
  AP01013	Ref, Latarcin 3b	SWASMAKKLKEYMEKLKQRA	2693
  	(Ltc3b, XXA,
  	BBM, spider)
  AP01014	Ref, Latarcin 4a	GLKDKFKSMGEKLKQYIQTWKAK	2694
  	(Ltc4a, XXA,	F
  	BBM, spider)
  AP01015	Ref, Latarcin 4b	SLKDKVKSMGEKLKQYIQTWKAK	2695
  	(Ltc4b, XXA,	F
  	BBM, spider)
  AP01016	Ref, Latarcin 5	GFFGKMKEYFKKFGASFKRRFANL	2696
  	(Ltc5, XXA, BBM,	KKRL
  	spider)
  AP01018	Ref, Latarcin 6a	QAFQTFKPDWNKIRYDAMKMQTS	2697
  	(Ltc6a, BBM,	LGQMKKRFNL
  	spider)
  AP01019	Ref, Latarcin 7	GETFDKLKEKLKTFYQKLVEKAED	2698
  	(Ltc7, BBM,	LKGDLKAKLS
  	spider)
  AP01049	Ref, Kalata B2	VCGETCFGGTCNTPGCSCTWPICT	2699
  	(plant cyclotides,	RDGLP
  	XXC)
  AP01141	Ref, Cryptdin-6	LRDLVCYCRARGCKGRERMNGTC	2700
  	(Crp6, animal	RKGHLLYMLCCR
  	defensin, alpha,
  	mouse)
  AP01142	Ref, Rabbit kidney	KPYCSCKWRCGIGEEEKGICHKFPI	2701
  	defensin RK-2	VTYVCCRRP
  	(animal defensin,
  	alpha-defensin)
  AP01146	Ref, Gallinacin 6	DTLACRQSHGSCSFVACRAPSVDI	2702
  	(Gal6, Gal-6, avian	GTCRGGKLKCCKWAPSS
  	beta defensin, bird)
  AP01147	Ref, Gallinacin 8	DTVACRIQGNFCRAGACPPTFTISG	2703
  	(Gal8, Gal-8, avian	QCHGGLLNCCAKIPAQ
  	beta defensin, bird)
  AP01148	Ref, Gallinacin 3	IATQCRIRGGFCRVGSCRFPHIAIGK	2704
  	(Gal3, Gal-3, avian	CATFISCCGRAY
  	beta defensin, bird)
  AP01152	Ref, Lactococcin Q	SIWGDIGQGVGKAAYWVGKAMG	2705
  	(class IIb	NMSDVNQASRINRKKKH
  	bacteriocin,
  	bacteria, chain a.
  	For chain b, see
  	Info)
  AP01155	Ref, Enterocin	ESVFSKIGNAVGPAAYWILKGLGN	2706
  	1071 (Ent1071A,	MSDVNQADRINRKKH
  	class IIb
  	bacteriocin,
  	bacteria; chain B is
  	Enterocin 1071B or
  	Ent1071B, see
  	info)
  AP01156	Ref, Plantaricin S	NKLAYNMGHYAGKATIFGLAAW	2707
  	(chain a, class IIb	ALLA
  	bacteriocin,
  	bacteria)
  AP01159	Ref, Hinnavin II	KWKIFKKIEHMGQNIRDGLIKAGP	2708
  	(Hin II, XXA,	AVQVVGQAATIYK
  	insect)
  AP01160	Ref, NK-2	KILRGLCKKIMRSFLRRISWDILTG	2709
  	(synthetic, XXA)	KK
  AP01167	Ref, Plantaricin	LTTKLWSSWGYYLGKKARWNLK	2710
  	NC8 (PLNC8,	HPYVQF
  	chain a, class IIb
  	bacteriocin,
  	bacteria. For chain
  	b, see Info)
  AP01168	Ref, Carnocyclin A	LVAYGIAQGTAEKVVSLINAGLTV	2711
  	(a circular	GSIISILGGVTVGLSGVFTAVKAAI
  	bacteriocin, XXC,	AKQGIKKAIQL
  	bacteria)
  AP01169	Ref, Lactacin F	NRWGDTVLSAASGAGTGIKACKSF	2712
  	(LafX, class IIb	GPWGMAICGVGGAAIGGYFGYTH
  	bacteriocin,	N
  	bacteria. For LafA,
  	see Info)
  AP01170	Ref, Brochocin C	YSSKDCLKDIGKGIGAGTVAGAAG	2713
  	(BrcC, chain BrcA,	GGLAAGLGAIPGAFVGAHFGVIGG
  	class IIb	SAACIGGLLGN
  	bacteriocin,
  	bacteria. For BrcB,
  	see Info)
  AP01171	Ref, Thermophilin	YSGKDCLKDMGGYALAGAGSGAL	2714
  	13 (chain a ThmA,	WGAPAGGVGALPGAFVGAHVGAI
  	2-chain class IIb	AGGFACMGGMIGNKFN
  	bacteriocin,
  	bacteria. For chain
  	B ThmB, see Info)
  AP01172	Ref, ABP-118	KRGPNCVGNFLGGLFAGAAAGVP	2715
  	(chain a:	LGPAGIVGGANLGMVGGALTCL
  	Abp118alpha, class
  	IIb bacteriocin,
  	bacteria. For chain
  	b: Abp118beta, see
  	Info)
  AP01173	Ref, Salivaricin P	KRGPNCVGNFLGGLFAGAAAGVP	2716
  	(chain a: Sln1;	LGPAGIVGGANLGMVGGALTCL
  	class IIb
  	bacteriocin,
  	bacteria. For chain
  	b: Sln2, see Info)
  AP01174	Ref, Mutacin IV	KVSGGEAVAAIGICATASAAIGGL	2717
  	(chain a: NlmA,	AGATLVTPYCVGTWGLIRSH
  	class IIb
  	bacteriocin,
  	bacteria. For chain
  	b:NLmB, see Info)
  AP01175	Ref, Lactocin 705	GMSGYIQGIPDFLKGYLHGISAAN	2718
  	(chain a:	KHKKGRLGY
  	Lac705alpha; class
  	IIb bacteriocin,
  	bacteria. For chain
  	b: Lac705beta, see
  	Info)
  AP01176	Ref, Cytolysin	TTPACFTIGLGVGALFSAKFC	2719
  	(CylLS, bacteria;
  	Chain B: CylLL)
  AP01177	Ref, Plantaricin	EFFNRGGYNFGKSVRHVVDAIGSVA	2720
  	(chain a: PlnE,	GILKSIR
  	class IIb
  	bacteriocin,
  	bacteria. Chain b:
  	PlnF)
  AP01178	Ref, Plantaricin	JKGAWKNFWSSLRKGFYDGEAGRAI	2721
  	(chain a: PlnJ; class	RR
  	IIb bacteriocin,
  	bacteria. Chain b:
  	PlnK)
  AP01179	Ref, Enterocin SE-	NGVYCNKQKCWVDWSRARSEIID	2722
  	K4 (class IIa	RGVKAYVNGFTKVLGGIGGR
  	bacteriocin,
  	bacteria)
  AP01180	Ref, Acidocin	NPKVAHCASQIGRSTAWGAVSGA	2723
  	J1132 (class IIb
  	bacteriocin,
  	bacteria)
  AP01181	Ref, Curvaticin	AYPGNGVHCGKYSCTVDKQTAIG	2724
  	L442 (class IIa	NIGNNAA
  	bacteriocin,
  	bacteria)
  AP01182	Ref, Bacteriocin 32	FTPSVSFSQNGGVVEAAAQRGYIY	2725
  	(Bac 32, class IIa	KKYPKGAKVPNKVKMLVNIRGKQ
  	bacteriocin,	TMRTCYLMSWTASSRTAKYYYYI
  	bacteria)
  AP01183	Ref, Bacteriocin 43	ATYYGNGLYCNKEKCWVDWNQA	2726
  	(Bac 43,	KGEIGKIIVNGWVNHGPWAPRR
  	bacteriocin,
  	bacteria)
  AP01184	Ref, Bacteriocin T8	ATYYGNGLYCNKEKCWVDWNQA	2727
  	(Bac T8, class Ha	KGEIGKIIVNGWVNHGPWAPRR
  	bacteriocin,
  	bacteria)
  AP01185	Ref, Enterocin B	ENDHRMPNNLNRPNNLSKGGAKC	2728
  	(EntB, bacteriocin,	GAAIAGGLFGIPKGPLAWAAGLAN
  	bacteria)	VYSKCN
  AP01186	Ref, Acidocin A	KTYYGTNGVHCTKKSLWGKVRLK	2729
  	(bacteriocin,	NVIPGTLCRKQSLPIKQDLKILLGW
  	bacteria)	ATGAFGKTFH
  AP01187	Ref, Enterocin Q	MNFLKNGIAKWMTGAELQAYKK	2730
  	(EntQ, class IIc	KYGCLPWEKISC
  	bacteriocin,
  	leaderless, i.e. no
  	signal peptide,
  	bacteria)
  AP01188	Ref, Enterocin	MLAKIKAMIKKFPNPYTLAAKLTT	2731
  	EJ97 (EntEJ97,	YEINWYKQQYGRYPWERPVA
  	class IIc
  	bacteriocin,
  	leaderless, i.e. no
  	signal peptide,
  	bacteria)
  AP01189	Ref, Enterocin RJ-	APAGLVAKFGRPIVKKYYKQIIVIQF	2732
  	11 (EntRJ-11, class	IGEGSAINKIIPWIARMWRT
  	IIc bacteriocin,
  	leaderless, i.e. no
  	signal sequence,
  	bacteria)
  AP01190	Ref, Enterocin L50	MGAIAKLVAKFGWPIVKKYYKQI	2733
  	(old name:	MQFIGEGWAINKIIEWIKKHI
  	pediocin L50,
  	EntL50A, a two-
  	chain class He
  	bacteriocin,
  	leaderless, i.e. no
  	signal peptide,
  	bacteria. The
  	sequence of
  	EntL50B is
  	provided in Info)
  AP01191	Ref, MR10	MGAIAKLVAKFGWPIVKKYYKQI	2734
  	(MR10A, class IIc	MQFIGEGWAINKIIDWIKKHI
  	bacteriocin,
  	leaderless, i.e. no
  	signal peptide,
  	bacteria. For the
  	sequence of chain
  	b, see Info)
  AP01192	Ref, Halocin S8	SDCNINSNTAADVILCFNQVGSCA	2735
  	(Hal S8,	LCSPTLVGGPVP
  	microhalocin,
  	archaeocins,
  	archeae)
  AP01193	Ref, Halocin C8	DIDITGCSACKYAAGQVCTIGCSA	2736
  	(HalC8,	AGGFICGLLGITIPVAGLSCLGFVEI
  	microhalocins,	VCTVADEYSGCGDAVAKEACNRA
  	archaeocins,	GLC
  	archaea)
  AP01194	Ref, Lacticin 3147	CSTNTFSLSDYWGNNGAWCTLTH	2737
  	(chain Al, a two-	ECMAWCK
  	chain lantibiotic,
  	bacteriocin,
  	bacteria. The
  	sequence of chain
  	A2 is given in Info;
  	XXD3)
  AP01195	Ref, Salivaricin A	KRGSGWIATITDDCPNSVFVCC	2738
  	(SalA, lantibiotic,
  	bacteriocin,
  	bacteria)
  AP01196	Ref, Microcin E492	ATYYGNGLYCNKEKCWVDWNQA	2739
  	(MccE492, class	KGEIGKIIVNGWVNHGPWAPRR
  	IIb microcins,
  	bacteriocin,
  	bacteria; BBM; u-
  	MccE492,
  	siderophore
  	peptide, BBI, XXG)
  AP01197	Ref, Hiracin JM79	ATYYGNGLYCNKEKCWVDWNQA	2740
  	(HirJM79, a Sec-	KGEIGKIIVNGWVNHGPWAPRR
  	dependent class II
  	bacteriocin,
  	bacteria)
  AP01198	Ref, Thermophilin	LSCDEGMLAVGGLGAVGGPWGA	2741
  	9 (BlpDst, class IIb	AVGVLVGAALYCF
  	bacteriocin,
  	bacteria. beta-
  	chains: BlpUst,
  	BlpEst, BapFst)
  AP01199	Ref, Penocin	AKYYGNGVHCGKKTCYVDWGQAT	2742
  	(PenA, class IIa	ASIGKIIVNGWTQHGPWAHR
  	bacteriocin,
  	bacteria)
  AP01200	Ref, Salivaricin B	GGGVIQTISHECRMNSWQFLFTCC	2743
  	(SalB, lantibotic,	S
  	bacteriocin,
  	bacteria)
  AP01201	Ref, Lacticin 481	KGGSGVIHTISHECNMNSWQFVFT	2744
  	(lantibiotic, class I
  	CCS
  	bacteriocin,
  	bacteria)
  AP01202	Ref, Bacteriocin	KGGSGVIHTISHEVIYNSWNFVFTC	2745
  	J46 (BacJ46, CS
  	bacteriocin,
  	bacteria)
  AP01203	Ref, Nukacin A	KKKSGVIPTVSHDCHMNSFQFVFT	2746
  	(NucA, Nukacin	CCS
  	ISK-1, NukISK-1,
  	bacteriocin,
  	bacteria)
  AP01204	Ref, Streptococcin	GKNGVFKTISHECHLNTWAFLATC	2747
  	A-FF22	CS
  	(LANTIBIOTIC,
  	class I bacteriocin,
  	bacteria)
  AP01210	Ref, Jelleine-I	PFKLSLHL	2748
  	(honeybees, insect,
  	XXA)
  AP01211	Ref, Jelleine-II	TPFKLSLHL	2749
  	(honeybees, insect,
  	XXA)
  AP01212	Ref, Jelleine-III	EPFKLSLHL	2750
  	(honeybees, insect,
  	XXA)
  AP01213	Ref,	EFRGSIVIQGTKEGKSRPSLDIDYK	2751
  	Hymenoptaecin	QRVYDKNGMTGDAYGGLNIRPGQ
  	(honeybees, insect	PSRQHAGFEFGKEYKNGFIKGQSE
  	defensin, XXcooh)	VQRGPGGRLSPYFGINGGFRF
  AP01216	Ref, Ascaphin-1	GFRDVLKGAAKAFVKTVAGHIAN	2752
  	(frog, XXA)
  AP01218	Ref, Ascaphin-3	GFRDVLKGAAKAFVKTVAGHIANI	2753
  	(frog)
  AP01220	Ref, Ascaphin-5	GIKDWIKGAAKKLIKTVASNIANQ	2754
  	(frog)
  AP01222	Ref, Ascaphin-7	GFKDWIKGAAKKLIKTVASSIANQ	2755
  	(frog)
  AP01223	Ref, Ascaphin-8	GFKDLLKGAAKALVKTVLF	2756
  	(frog, XXA)
  AP01226	Ref, Microcin C7	MRTGNAD	2757
  	(MccC7, microcin
  	C51, MccC51,
  	class I microcins,
  	bacteriocins,
  	bacteria. Others:
  	MccA; XXamp;
  	BBPe)
  AP01227	Ref, Microcin B17	VGIGGGGGGGGGGSCGGQGGGCG	2758
  	(MccB17, class I	GCSNGCSGGNGGSGGSGSHI
  	microcins,
  	bacteriocins, Gram-
  	negative bacteria;
  	BBPe)
  AP01228	Ref, Microcin V	ASGRDIAMAIGTLSGQFVAGGIGA	2759
  	(MccV, (old name)	AAGGVAGGAIYDYASTHKPNPAM
  	Colicin V, ColV;	SPSGLGGTIKQKPEGIPSEAWNYAA
  	class II microcins,	GRLCNWSPNNLSDVCL
  	bacteriocins, Gram-
  	negative bacteria)
  AP01229	Ref, Microcin L	GDVNWVDVGKTVATNGAGVIGG	2760
  	(MccL, class Ha	AFGAGLCGPVCAGAFAVGSSAAV
  	microcins,	AALYDAAGNSNSAKQKPEGLPPEA
  	bacteriocins, Gram-	WNYAEGRMCNWSPNNLSDVCL
  	negative bacteria)
  AP01230	Ref, Microcin M	DGNDGQAELIAIGSLAGTFISPGFG	2761
  	(MccM, class IIb	SIAGAYIGDKVHSWATTATVSPSM
  	microcins,	SPSGIGLSSQFGSGRGTSSASSSAGS
  	bacteriocins, Gram-	GS
  	negative bacteria)
  AP01231	Ref, Microcin H47	GGAPATSANAAGAAAIVGALAGIP	2762
  	(MccH47, class IIb	GGPLGVVVGAVSAGLTTGIGSTVG
  	microcins,	SGSASSSAGGGS
  	bacteriocins, Gram-
  	negative bacteria)
  AP 01232	Ref, Microcin 147	MNLNGLPASTNVIDLRGKDMGTYI	2763
  	(MccI47, class IIb	DANGACWAPDTPSIIMYPGGSGPS
  	microcins,	YSMSSSTSSANSGS
  	bacteriocins, Gram-
  	negative bacteria)

  Aibellin	*AcUAUAUAQUFUGUUPVUUEE	2764
  	[NHC(CH2Ph)HCH2NHCH2CH2]OH
  Alamethicin_F-30	*AcUPUAUAQUVUGLUPVUUEQF	2765
  	OH
  Alamethicin_F-50	*AcUPUAUAQUVUGLUPVUUQQF	2766
  	OH
  Alamethicin_II	*AcUPUAUUQUVUGLUPVUUEQF	2767
  	OH
  Ampullosporin	*AcWAUULUQUUUQLUQLOH	2768
  Ampullosporin_B	*AcWAUULUQAUUQLUQLOH	2769
  Ampullosporin_C	*AcWAUULUQUAUQLUQLOH	2770
  Ampullosporin_D	*AcWAUULUQUUAQLUQLOH	2771
  Ampullosporin_E1	*AcWAUULUQAUUQLAQLOH	2772
  Ampullosporin_E2	*AcWAUULUQUAAQLUQLOH	2773
  Ampullosporin_E3	*AcWAUULUQUUAQLAQLOH	2774
  Ampullosporin_E4	*AcWAUULUQAAUQLUQLOH	2775
  Antiamoebin_I	*AcFUUUJGLUUOQJOUPFOH	2776
  Antiamoebin_II	*AcFUUUJGLUUOQJPUPFOH	2777
  Antiamoebin_III	*AcFUUUUGLUUOQJOUPFOH	2778
  Antiamoebin_IV	*AcFUUUJGLUUOQJOUPFOH	2779
  Antiamoebin_V	*AcFUUUJALUUOQJOUPFOH	2780
  Antiamoebin_VI	*AcFUUUUGLUUOQUOUPFOH	2781
  Antiamoebin_VII	*AcFAUJUGLUUOQJOUPFOH	2782
  Antiamoebin_VIII	*AcFUUUJGLUUOQUOUPFOH	2783
  Antiamoebin_IX	*AcFUAUJGLUUOQJOUPFOH	2784
  Antiamoebin_X	*AcFUUUJGLJUOQUOUPFOH	2785
  Antiamoebin_XI	*AcFUUUUALUUOQJOUPFOH	2786
  Antiamoebin_XII	*AcFUUUUGLAUOQJOUPFOH	2787
  Antiamoebin_XIII	*AcVUUUUGLUUOQJOUPFOH	2788
  Antiamoebin_XIV	*AcVUUUVGLUUOQJOUPFOH	2789
  Antiamoebin_XV	*AcLUUUUGLUUOQJOUPFOH	2790
  Antiamoebin_XVI	*AcLUUUJGLUUOQJOUPFOH	2791
  Atroviridin_A	*AcUPUAUAQUVUGLUPVUUQQF	2792
  	OH
  Atroviridin_B	*AcUPUAUAQUVUGLUPVUJQQF	2793
  	OH
  Atroviridin_C	*AcUPUAUUQUVUGLUPVUJQQF	2794
  	OH
  Bergofungin_A	*AcVUUUVGLUUOQJOUFOH	2795
  Bergofungin_B	*AcVUUUVGLVUOQUOUFOH	2796
  Bergofungin_C	*AcVUUUVGLUUOQUOUFOH	2797
  Bergofungin_D	*AcVUUVGLUUOQUOUFOH	2798
  Boletusin	*AcFUAUJLQGUUAAUPUUUQW	2799
  	OH
  Cephaibol_A	*AcFUUUUGLJUOQJOUPFOH	2800
  Cephaibol_A2	*AcFUUUUALJUOQJOUPFOH	2801
  Cephaibol_B	*AcFUUUJGLJUOQJOUPFOH	2802
  Cephaibol_C	*AcFUUUUGLJUOQUOUPFOH	2803
  Cephaibol_D	*AcFUUUUGLUUOQUOUPFOH	2804
  Cephaibol_E	*AcFUUUUGLUUOQJOUPFOH	2805
  Cephaibol_P	*AcFJQUITULUOQUOUPFSOH	2806
  Cephaibol_Q	*AcFJQUITULUPQUOUPFSOH	2807
  Cervinin_1	*AcLUPULUPAUPVLOH	2808
  Cervinin_2	*AcLUPULUPAUPVLOCOCH3	2809
  Chrysospermin_A	*AcFUSUULQGUUAAUPUUUQW	2810
  	OH
  Chrysospermin_B	*AcFUSUULQGUUAAUPJUUQW	2811
  	OH
  Chrysospermin_C	*AcFUSUJLQGUUAAUPUUUQW	2812
  	OH
  Chrysospermin_D	*AcFUSUJLQGUUAAUPJUUQW	2813
  	OH
  Clonostachin	*AcUOLJOLJOUJUOJI	2814
  	O[CH(CH(OH)CH2OH)CH(OH)CH(OH)CH2]OH
  Emerimicin_II_A	*AcWIQUITULUOQUOUPFOH	2815
  Emerimicin_II_B	*AcWIQJITULUOQUOUPFOH	2816
  Emerimicin_III	*AcFUUUVGLUUOQJOUFOH	2817
  Emerimicin_IV	*AcFUUUVGLUUOQJOAFOH	2818
  Harzianin_HB_I	*AcUNLIUPJLUPLOH	2819
  Harzianin_HC_I	*AcUNLUPSVUPULUPLOH	2820
  Harzianin_HC_III	*AcUNLUPSVUPJLUPLOH	2821
  Harzianin_HC_IX	*AcUNLUPAIUPJLUPLOH	2822
  Harzianin_HC_VI	*AcUNLUPAVUPULUPLOH	2823
  Harzianin_HC_VIII	*AcUNLUPAVUPJLUPLOH	2824
  Harzianin_HC_VIII	*AcUNLUPAVUPJLUPLOH	2825
  Harzianin_HC_X	*AcUQLUPAVUPJLUPLOH	2826
  Harzianin_HC_XI	*AcUNLUPSIUPULUPLOH	2827
  Harzianin_HC_XII	*AcUNLUPSIUPJLUPLOH	2828
  Harzianin_HC_XIII	*AcUQLUPSIUPJLUPLOH	2829
  Harzianin_HC_XIV	*AcUNLUPAIUPULUPLOH	2830
  Harzianin_HC_XV	*AcUQLUPAIUPJLUPLOH	2831
  Harzianin_HK_VI	*AcUNIIUPLLUPLOH	2832
  Harzianin_PCU4	*AcUNLUPSIUPULUPVOH	2833
  Helioferin_A	*FaPZZAUIIUUAAE	2834
  Helioferin_B	*FaPZZAUIIUUANIAE	2835
  Heptaibin	*AcFUUUVGLUUOQUOUFOH	2836
  Hypelcin_A	*AcUPUAUUQLUGUUUPVUUQQL	2837
  	OH
  Hypelcin_A_I	*AcUPUAUUQULUGUUPVUUQQL	2838
  	OH
  Hypelcin_A_II	*AcUPUAUAQULUGUUPVUUQQL	2839
  	OH
  Hypelcin_A_III	*AcUPUAUUQULUGUUPVUUQQ	2840
  	[C7H16NO]
  Hypelcin_A_IV	*AcUPUAUUQUIUGUUPVUUQQL	2841
  	OH
  Hypelcin_A-III	*AcUPUAUUQULUGUUPVUJQQL	2842
  	OH
  Hypelcin_A-IX	*AcUPUAUUQUIUGUUPVUJQQL	2843
  	OH
  Hypelcin_A-V	*AcUPUAUUQULUGUUPVUUQQI	2844
  	OH
  Hypelcin_A-VI	*AcUPUAUAQULUGUUPVUUQQI	2845
  	OH
  Hypelcin_A-VII	*AcUPUAUAQULUGUUPVUJQQL	2846
  	OH
  Hypelcin_A-VIII	*AcUPUAUAQUIUGUUPVUUQQL	2847
  	OH
  Hypelcin_B_I	*AcUPUAUUQULUGUUPVUUEQL	2848
  	OH
  Hypelcin_B_II	*AcUPUAUAQULUGUUPVUUEQL	2849
  	OH
  Hypelcin_B_III	*AcUPUAUUQULUGUUPVUJEQL	2850
  	OH
  Hypelcin_B_IV	*AcUPUAUUQUIUGUUPVUUEQL	2851
  	OH
  Hypelcin_B_V	*AcUPUAUUQULUGUUPVUUEQI	2852
  	OH
  Hypomurocin_A_I	*AcUQVVUPLLUPLOH	2853
  Hypomurocin_A_II	*AcJQVVUPLLUPLOH	2854
  Hypomurocin_A_III	*AcUQVLUPLIUPLOH	2855
  Hypomurocin_A_IV	*AcUQIVUPLLUPLOH	2856
  Hypomurocin_A_V	*AcUQIIUPLLUPLOH	2857
  Hypomurocin_A_Va	*AcUQILUPLIUPLOH	2858
  Hypomurocin_B_I	*AcUSALUQUVUGUUPLUUQVOH	2859
  Hypomurocin_B_II	*AcUSALUQUVUGUUPLUUQLOH	2860
  Hypomurocin_B_Ma	*AcUAALUQUVUGUUPLUUQVOH	2861
  Hypomurocin_B_Mb	*AcUSALUQJVUGUUPLUUQVOH	2862
  Hypomurocin_B_IV	*AcUSALUQUVUGJUPLUUQVOH	2863
  Hypomurocin_B_V	*AcUSALUQUVUGJUPLUUQLOH	2864
  Leul_Zervamicin	*AcLIQJITULUOQUOUPFOH	2865
  Longibrachin_A_I	*AcUAUAUAQUVUGLUPVUUQQF	2866
  	OH
  Longibrachin_A_II	*AcUAUAUAQUVUGLUPVUJQQF	2867
  	OH
  Longibrachin_A_III	*AcUAUAUUQUVUGLUPVUUQQF	2868
  	OH
  Longibrachin_A_IV	*AcUAUAUUQUVUGLUPVUJQQF	2869
  	OH
  Longibrachin_B_II	*AcUAUAUAQUVUGLUPVUUEQF	2870
  	OH
  Longibrachin_B_III	*AcUAUAUAQUVUGLUPVUJEQF	2871

  	OH

  LP237_F5	*OcUPYUQQUZorQALOH	2872
  LP237_F7	*AcUPFUQQUUQALOH	2873
  LP237_F8	*OcUPFUQQUZorQALOH	2874
  NA_VII	*AcUAAUJQUUUSLUOCH3	2875
  Paracelsin_A	*AcUAUAUAQUVUGUUPVUUQQ	2876
  	FOH
  Paracelsin_B	*AcUAUAUAQULUGUUPVUUQQF	2877
  	OH
  Paracelsin_C	*AcUAUAUUQUVUGUUPVUUQQ	2878
  	FOH
  Paracelsin_D	*AcUAUAUUQULUGUUPVUUQQF	2879
  	OH
  Paracelsin_E	*AcUAUAUAQULUGUAPVUUQQF	2880
  	OH
  Peptaibolin	*AcLULUFOH	2881
  Peptaivirin_A	*AcFUAUJLQGUUAAUPJUUQW	2882
  	OH
  Peptaivirin_B	*AcFUSUJLQGUUAAUPJUUQFOH	2883
  Polysporin_A	*AcUPUAUUQUVUGVUPVUUQQF	2884
  	OH
  Polysporin_B	*AcUPUAUUQUVUGLUPVUUQQF	2885
  	OH
  Polysporin_C	*AcUPUAUUQUIUGLUPVUUQQF	2886
  	OH
  Polysporin_D	*AcUPUAUUQUIUGLUPVUVQQF	2887
  	OH
  Pseudokinin_KLIII	*AcUNIIUPLLUPNH2	2888
  Pseudokinin_KLVI	*AcUNIIUPLVhydroxyketopiperazine	2889
  Samarosporin_I	*AcFUUUVGLUUOQJOAFOH	2890
  Samarosporin_II	*AcFUUUVGLUUOQJOUFOH	2891
  Saturnisporin_SA_	*AcUAUAUAQULUGUUPVUUQQF
  I	OH	2892
  Saturnisporin_SA_	*AcUAUAUAQULUGUUPVUJQQF
  II	OH
  Saturnisporin_SA_	*AcUAUAUUQULUGUUPVUUQQF	2893
  III	OH	2894
  Saturnisporin_SA_	*AcUAUAUUQULUGUUPVUJQQF
  IV	OH	2895
  Stilbellin_I	*AcFUUUVGLUUOQJOAFOH	2896
  Stilbellin_II	*AcFUUUVGLUUOQJOUFOH	2897
  Stilboflavin_A_1	*AcUPUAUAQUVUGUUPVUUEQV	2898
  	OH
  Stilboflavin_A_2	*AcUPUAUAQULUGUUPVUUEQV	2999
  	OH
  Stilboflavin_A_3	*AcUPUAUUQUVUGUAPVUUEQL	2900
  	OH
  Stilboflavin_A_4	*AcUPUAUAQULUGUUPVUUEQL	2901
  	OH
  Stilboflavin_A_5	*AcUPUAUUQULUGUUPVUUEQV	2902
  	OH
  Stilboflavin_A_6	*AcUPUAUAQULUGUUPVUUEQJ	2903
  	OH
  Stilboflavin_A_7	*AcUPUAUUQULUGUUPVUUEQI	2904
  	OH
  Stilboflavin_B_1	*AcUPUAUAQUVUGUUPVUUQQ	2905
  	VOH
  Stilboflavin_B_2	*AcUPUAUAQULUGUUPVUUQQV	2906
  	OH
  Stilboflavin_B_3	*AcUPUAUAQUVUGUUPVUUQQL	2907
  	OH
  Stilboflavin_B_4	*AcUPUAUAQULUGUUPVUUQQL	2908
  	OH
  Stilboflavin_B_5	*AcUPUAUUQULUGUUPVUUQQV	2909
  	OH
  Stilboflavin_B_6	*AcUPUAUUQUVUGUUPVUUQQ	2910
  	VOH
  Stilboflavin_B_7	*AcUPUAUUQULUGUUPVUUQQL	2911
  	OH
  Stilboflavin_B_8	*AcUPUAUUQUVUGUUPVUUQQL	2912
  	OH
  Stilboflavin_B_9	*AcUPUAUUQULUGUUPVUUQQI	2913
  	OH
  Stilboflavin_B_10	*AcUPUAUUQUVUGUUPVUUQQI	2914
  	OH
  Suzukacillin	*AcUAUAUAQUUUGLUPVUUQQF	2915
  	OH
  Trichobrachin_A-I	*AcUNLLUPLUUPLOH	2916
  Trichobrachin_A-II	*AcUNLLUPVLUPVOH	2917
  Trichobrachin_A-III	*AcUNVLUPLLUPVOH	2918
  Trichobrachin_A-IV	*AcUNLVUPLLUPVOH	2919
  Trichobrachin_B-I	*AcUNLLUPVUVPLOH	2920
  Trichobrachin_B-I_	*AcUNVLUPLUVPLOH	2921
  Trichobrachin_B-III	*AcUNLVUPLUVPLOH	2922
  Trichobrachin_B-IV	*AcUNLLUPLUVPVOH	2923
  Trichocellin_TC-A-I	*AcUAUAUAQULUGUUPVUUQQF	2924
  	OH
  Trichocellin_TC-A-	*AcUAUAUAQULUGUUPVUJQQF	2925
  II	OH
  Trichocellin_TC-A-	*AcUAUAUAQUIUGUUPVUUQQF	2926
  III	OH
  Trichocellin_TC-A-	*AcUAUAUAQUIUGUUPVUJQQF	2927
  IV	OH
  Trichocellin_TC-A-V	*AcUAUAUAQULUGLUPVUUQQF	2928
  	OH
  Trichocellin_TC-A-	*AcUAUAUAQULUGLUPVUJQQF	2929
  VI	OH
  Trichocellin_TC-A-	*AcUAUAUAQUIUGLUPVUUQQF	2930
  VII	OH
  Trichocellin_TC-A-	*AcUAUAUAQUIUGLUPVUJQQF	2931
  VIII	OH
  Trichocellin_TC-B-I	*AcUAUAUAQULUGUUPVUUEQF	2932
  	OH
  Trichocellin_TC-B-II	*AcUAUAUAQULUGUUPVUJEQF	2933
  	OH
  Trichodecenin_TD_I	*(Z)-4-decenoylGGLUGILOH	2934
  Trichodecenin_TD_II	*(Z)-4-decenoylGGLUGLLOH	2935
  Trichogin	AIV*OcUGLUGGLUGILOH	2936
  Trichokindin_Ia	*AcUSAUUQJLUAUUPLUUQIOH	2937
  Trichokindin_Ib	*AcUSAUJQULUAUUPLUUQIOH	2938
  Trichokindin_IIa	*AcUSAUUQULUAJUPLUUQIOH	2939
  Trichokindin_IIb	*AcUSAUJQJLUAUUPLUUQLOH	2940
  Trichokindin_Ma	*AcUSAUUQJLUAJUPLUUQLOH	2941
  Trichokindin_Mb	*AcUSAUJQULUAJUPLUUQLOH	2942
  Trichokindin_IV	*AcUSAUJQJLUAUUPLUUQIOH	2943
  Trichokindin_Va	*AcUSAUUQJLUAJUPLUUQIOH	2944
  Trichokindin_Vb	*AcUSAUJQULUAJUPLUUQIOH	2945
  Trichokindin_VI	*AcUSAUJQJLUAJUPLUUQLOH	2946
  Trichokindin_VII	*AcUSAUJQJLUAJUPLUUQIOH	2947
  Trichokoninb_Ia	*AcUAUAUAQUVUGLAPVUUQQF	2948
  	OH
  Trichokonin_Ib	*AcUGUAUAQUVUGLUPVUUQQF	2949
  	OH
  Trichokonin_IIa	*AcUAUAUAQUVUGLUPAUUQQF	2950
  	OH
  Trichokonin_IIb	*AcAAUAUAQUVUGLUPVUUQQF	2951
  	OH
  Trichokonin_IIc	*AcUAAAUAQUVUGLUPVUUQQF	2952
  	OH
  Trichokonin_V	*AcUAUAUQUVUGLUPVUUQQF	2953
  	OH
  Trichokonin_VII	*AcUAUAUAQUVUGLUPVUJQQF	2954
  	OH
  Trichokonin_VIII	*AcUAUAUUQUVUGLUPVUUQQF	2955
  	OH
  Trichokonin_IX	*AcUAUAUAQUVUGLUPVUJQQF	2956
  	OH
  Tricholongin_BI	*AcUGFUUQUUUSLUPVUUQQL	2957
  	OH
  Tricholongin_BII	*AcUGFUUQUUUSLUPVUJQQL	2958
  	OH
  Trichopolyn_I	*FaPZZAUUIAUUANIAE	2959
  Trichopolyn_II	*FaPZZAUUVAUUANIAE	2960
  Trichopolyn_III	*FaPZZAUUIAUAANIAE	2961
  Trichopolyn_IV	*FaPZZAUUVAUAANIAE	2962
  Trichopolyn_V	*Fa′PZZAUUIAUUAN/JAB	2963
  Trichorovin_TV_Ia	*AcUNVLxUPLxLxUPVOH	2964
  Trichorovin_TV_Ib	*AcUNVVUPLxLxUPLxOH	2965
  Trichorovin_TV_IIa	*AcUNVVUPLxLxUPLxOH	2966
  Trichorovin_TV_IIb	*AcUNLxVUPLxLxUPVOH	2967
  Trichorovin_TV_IIIa	*AcUQVVUPLxLxUPLxOH	2968
  Trichorovin_TV_IIIb	*AcUQVLxUPLxLxUPVOH	2969
  Trichorovin_TV_IVa	*AcUQVVUPLxLxUPLxOH	2970
  Trichorovin_TV_IVb	*AcUQLxVUPLxLxUPVOH	2971
  Trichorovin_TV_IVc	*AcUNVLxUPLxLxUPLxOH	2972
  Trichorovin_TV_IXa	*AcUQVLxUPLxLxUPLxOH	2973
  Trichorovin_TV_IXb	*AcUQLxLxUPLxLxUPVOH	2974
  Trichorovin_TV_Va	*AcUNVLxUPLxLxUPLxOH	2975
  Trichorovin_TV_Vb	*AcUNLxLxUPLxLxUPVOH	2976
  Trichorovin_TV_VIa	*AcUNVLxUPLxLxUPLxOH	2977
  Trichorovin_TV_VIb	*AcUNLxLxUPLxLxUPVOH	2978
  Trichorovin_TV_VIIa	*AcUNLxVUPLxLxUPLxOH	2979
  Trichorovin_TV_VIIb	*AcUQVLxUPLxLxUPVOH	2980
  Trichorovin_TV_VIII	*AcUQVLxUPLxLxUPLxOH	2981
  Trichorovin_TV_Xa	*AcUQLxVUPLxLxUPLxOH	2982
  Trichorovin_TV_Xb	*AcUNLxLxUPLxLxUPLxOH	2983
  Trichorovin_TV_XIIa	*AcUNIIUPLLUPIOH	2984
  Trichorovin_TV_XIIb	*AcUNLxLxUPLxLxUPLOH	2985
  Trichorovin_TV_XIII	*AcUQLxLxUPLxLxUPLxOH	2986
  Trichorovin_TV_XIV	*AcUQLxLxUPLxLxUPLxOH	2987
  Trichorozin_I	*AcUNILUPILUPVOH	2988
  Trichorozin_II	*AcUQILUPILUPVOH	2989
  Trichorozin_III	*AcUNILUPILUPLOH	2990
  Trichorozin_IV	*AcUOILUPILUPLOH	2991
  Trichorzianine_TA_I	*AcUAAUUQUUUSLUPVUIQQW	2992
  IIc	OH
  Trichorzianine_TB_	*AcUAAUUQUUUSLUPLUIQEW	2993
  IIa	OH
  Trichorzianine_TB_	*AcUAAUUQUUUSLUPVUIQEW	2994
  IIIc	OH
  Trichorzianine_TB_	*AcUAAUJQUUUSLUPVUIQEW	2995
  IVb	OH
  Trichorzianine_TB_	*AcUAAUUQUUUSLUPLUIQEFOH	2996
  Vb
  Trichorzianine_TB_	*AcUAAUJQUUUSLUPLUIQEFOH	2997
  VIa
  Trichorzianine_TB_	*AcUAAUUQUUUSLUPVUIQEF	2998
  VIb	OH
  Trichorzianine_TB_	*AcUAAUJQUUUSLUPVUIQEFOH	2999
  VII
  Trichorzin_HA_I	*AcUGAUUQUVUGLUPLUUQLOH	3000
  Trichorzin_HA_II	*AcUGAUUQUVUGLUPLUJQLOH	3001
  Trichorzin_HA_III	*AcUGAUJQUVUGLUPLUUQLOH	3002
  Trichorzin_HA_V	*AcUGAUJQUVUGLUPLUJQLOH	3003
  Trichorzin_HA_VI	*AcUGAUJQJVUGLUPLUJQLOH	3004
  Trichorzin_HA_VII	*AcUGAUJQVVUGLUPLUJQLOH	3005
  Trichorzin_MA_I	*AcUSAUUQULUGLUPLUUQVOH	3006
  Trichorzin_MA_II	*AcUSAUJQULUGLUPLUUQVOH	3007
  Trichorzin_MA_III	*AcUSAUJQJLUGLUPLUUQVOH	3008
  Trichorzin_PA_II	*AcUSAUJQUVUGLUPLUUQWOH	3009
  Trichorzin_PA_IV	*AcUSAUJQJVUGLUPLUUQWOH	3010
  Trichorzin_PA_V	*AcUSAJJQUVUGLUPLUUQWOH	3011
  Trichorzin_PA_VI	*AcUSAUJQUVUGLUPLUUQFOH	3012
  Trichorzin_PA_VII	*AcUSAJJQUVUGLUPLUUQWOH	3013
  Trichorzin_PA_VIII	*AcUSAUJQJVUGLUPLUUQFOH	3014
  Trichorzin_PA_IX	*AcUSAJJQUVUGLUPLUUQFOH	3015
  Trichorzin_PAU4	*AcUSAUUQUVUGLUPLUUQWOH	3016
  Trichosporin_TS-B-	*AcUAGUAUQULxAAVxAPVUVxQ	3017
  1a-1	QFOH
  Trichosporin_TS-B-	*AcUAGAUUQULxAAVxAPVUVxQ	3018
  1a-2	QFOH
  Trichosporin_TS-B-	*AcUAGAUUQULxUGLxAPVUAQ	3019
  1b	QFOH
  Trichosporin_TS-B-	*AcUASAUUQULxUGLxAPVUUQQ	3020
  1d	FOH
  Trichosporin_TS-B-	*AcUAGAUUQULxUGLxUPVUUQ	3021
  1e	QFOH
  Trichosporin_TS-B-	*AcUASAUUQULxUGLxUPVUUQQ	3022
  1f	FOH
  Trichosporin_TS-B-	*AcUAGAUUQULxUGLxAPVUUQ	3023
  1g	QFOH
  Trichosporin_TS-B-	*AcUAGAUUQULxUGLxUPVUVxQ	3024
  1h	QFOH
  Trichosporin_TS-B-Ia	*AcUASAUUQULUGLUPVUUQQF	3025
  	OH
  Trichosporin_TS-B-	*AcUAAAUUQULUGLUPVUUQQF	3026
  IIIa	OH
  Trichosporin_TS-B-	*AcUAAAUUQUIUGLUPVUAQQF	3027
  IIIb	OH
  Trichosporin_TS-B-	*AcUAAAAUQUIUGLUPVUUQQF	3028
  IIIc	OH
  Trichosporin_TS-B-	*AcUAAAUUQUVUGLUPVUUQQF	3029
  IIId	OH
  Trichosporin_TS-B-	*AcUAAAUUQULUGLUPVUJQQF	3030
  IVb	OH
  Trichosporin_TS-B-	*AcUAUAUUQUVUGLUPVUUQQF	3031
  IVc	OH
  Trichosporin_TS-B-	*AcUAAAUUQUVUGLUPVUJQQF	3032
  IVd	OH
  Trichosporin_TS-B-	*AcUAAAUUQUIUGLUPVUUQQF	3033
  V	OH
  Trichosporin_TS-B-	*AcUAUAUUQUIUGLUPVUUQQF	3034
  VIa	OH
  Trichosporin_TS-B-	*AcUAAAUUQUIUGLUPVUJQQF	3035
  VIb	OH
  Trichotoxin_A-40	*AcUGULUEUUUAUUPLUJQVOH	3036
  Trichotoxin_A-40_I	*AcUGULUQUUAAUUPLUUEVOH	3037
  Trichotoxin_A-40_II	*AcUGULUQUUUAAUPLUUEVOH	3038
  Trichotoxin_A-40_III	*AcUGULUQUUAAUUPLUJEVOH	3039
  Trichotoxin_A-40_IV	*AcUGULUQUUUAUUPLUUEVOH	3040
  Trichotoxin_A-40_V	*AcUGULUQUUUAUUPLUJEVOH	3041
  Trichotoxin_A-40_Va	*AcUAULUQUUUAUUPLUUEVOH	3042
  Trichotoxin_A-50_E	*AcUGULUQUUUAAUPLUUQVOH	3043
  Trichotoxin_A-50_F	*AcUGULUQUUAAAUPLUJQVOH	3044
  Trichotoxin_A-50_G	*AcUGULUQUUUAAUPLUJQVOH	3045
  Trichotoxin_A-50_H	*AcUAULUQUUUAAUPLUJQVOH	3046
  Trichotoxin_A-50_I	*AcUGULUQUUUAUUPLUJQVOH	3047
  Trichotoxin_A-50_J	*AcUAULUQUUUAUUPLUJQVOH	3048
  Trichovirin-1a	*AcUGALAQVxVUGUUPLUUQL	3049
  	OH
  Trichovirin-Ib	*AcUGALUQAVUGJUPLUUQLOH	3050
  Trichovirin-IIa	*AcUGALAQUVUGJUPLUUQLOH	3051
  Trichovirin-lIb	*AcUGALUQUVUGUUPLUUQLOH	3052
  Trichovirin-IIc	*AcUGALUQVxVUGUUPLUUQL	3053
  	OH
  Trichovirin-IIIa	*AcUGALUQJVUGUUPLUUQLOH	3054
  Trichovirin-IIb	*AcUGALJQJUUGUUPLUUQLOH	3055
  Trichovirin-IVa	*AcUGALJQJVUGUUPLUUQLOH	3056
  Trichovirin-IVb	*AcUGALUQUVUGJUPLUUQLOH	3057
  Trichovirin-V	*AcUGALUQJVUGJUPLUUQLOH	3058
  Trichovirin-VIa	*AcUGALUQJLUGJUPLUUQLOH	3059
  Trichovirin-VIb	*AcUGALJQJVUGJUPLUUQLOH	3060
  Trikoningin_KA_V	*AcUGAUIQUUUSLUPVUIQQLOH	3061
  Trikoningin_KB_I	*OcUGVUGGVUGILOH	3062
  Trikoningin_KB_II	*OcJGVUGGVUGILOH	3063
  Tylopeptin_A	*AcWVUJAQAUSUALUQLOH	3064
  Tylopeptin_B	*AcWVUUAQAUSUALUQLOH	3065
  XR586	*AcWJQUITULUPQUOJPFGOH	3066
  Zervamicin_A-1-16	*B0cWIAUIVULUPAUPUPFOCH3	3067
  Zervamicin_ZIA	*AcWIEJVTULUOQUOUPFOH	3068
  Zervamicin_ZIB	*AcWVEJITULUOQUOUPFOH	3069
  Zervamicin_ZIB′	*AcWIEUITULUOQUOUPFOH	3070
  Zervamicin_ZIC	*AcWIEJITULUOQUOUPFOH	3071
  Zervamicin_ZII-1	*AcWIQUVTULUOQUOUPFOH	3072
  Zervamicin_ZII-2	*AcWIQUITUVUOQUOUPFOH	3073
  Zervamicin_ZII-3	*AcWVQUITULUOQUOUPFOH	3074
  Zervamicin_ZII-4	*AcWIQJVTULUOQUOUPFOH	3075
  Zervamicin_ZII-5	*AcWIQJITUVUOQUOUPFOH	3076
  Zervamicin_ZIIA	*AcWIQUITULUOQUOUPFOH	3077
  Zervamicin_ZIIB	*AcWIQJITULUOQUOUPFOH	3078
  CAMEL135	GWRLIKKILRVFKGL	3079
  (CAM135)
  Novispirin G2	KNLRIIRKGIHIIKKY*	3080
  B-33	FKKFWKWFRRF	3081
  B-34	LKRFLKWFKRF	3082
  B-35	KLFKRWKHLFR	3083
  B-36	RLLKRFKHLFK	3084
  B-37	FKTFLKWLHRF	3085
  B-38	IKQLLHFFQRF	3086
  B-39	KLLQTFKQIFR	3087
  B-40	RILKELKNLFK	3088
  B-41	LKQFVHFIHRF	3089
  B-42	VKTLLHIFQRF	3090
  B-43	KLVEQLKEIFR	3091
  B-44	RVLQEIKQILK	3092
  B-45	VKNLAELVHRF	3093
  B-46	ATHLLHALQRF	3094
  B-47	KLAENVKEILR	3095
  B-48	RALHEAKEALK	3096
  B-49	FHYFWHWFHRF	3097
  B-50	LYHFLHWFQRF	3098
  B-51	YLFQTWQHLFR	3099
  B-52	YLLTEFQHLFK	3100
  B-53	FKTFLQWLHRF	3101
  B-54	IKTLLHFFQRF	3102
  B-55	KLLQTFNQIFR	3103
  B-56	TILQSLKNIFK	3104
  B-57	LKQFVKFIHRF	3105
  B-58	VKQLLKIFNRF	3106
  B-59	KLVQQLKNIFR	3107
  B-60	RVLNQVKQILK	3108
  B-61	VKKLAKLVRRF	3109
  B-62	AKRLLKVLKRF	3110
  B-63	KLAQKVKRVLR	3111
  B-64	RALKRIKHVLK	3112
  1C-1	RRRRWWW	3113
  1C-2	RRWWRRW	3114
  1C-3	RRRWWWR	3115
  1C-4	RWRWRWR	3116
  2C-1	RRRFWWR	3117
  2C-2	RRWWRRF*	3118
  2C-3	RRRWWWF*	3119
  2C-4	RWRWRWF*	3120
  3C-1	RRRRWWK	3121
  3C-2	RRWWRRK	3122
  3C-3	RRRWWWK	3123
  3C-4	RWRWRWK	3124
  4C-1	RRRKWWK	3125
  4C-2	RRWKRRK	3126
  4C-3	RRRKWWK	3127
  4C-4	RWRKRWK	3128
  a-3	LHLLHQLLHLLHQF*	3129
  a-4	AQAAHQAAHAAHQF*	3130
  a-5	KLKKLLKKLKKLLK	3131
  a-6	LKLLKKLLKLLKKF*	3132
  a-7	LQLLKQLLKLLKQF*	3133
  a-8	AQAAKQAAKAAKQF*	3134
  a-9	RWRRWWRHFHHFFH*	3135
  a-10	KLKKLLKRWRRWWR	3136
  a-11	RWRRLLKKLHHLLH*	3137
  a-12	KLKKLLKHLHHLLH*	3138
  BD-1	FVF RHK WVW KHR FLF	3139
  BD-2	VFI HRH VWV HKH VLF	3140
  BD-3	WR WR ARWR WR LR WR F	3141
  BD-4	WR IH LR AR LH VK FR F	3142
  BD-5	LR IH AR FK VH IR LK F	3143
  BD-6	FH IK FR VH LK VR FH F	3144
  BD-7	FH VK IH FR LH VK FH F	3145
  BD-8	LH IH AH FH VH IH LH F	3146
  BD-9	FK IHFRLK VHIRFK F	3147
  BD-10	FK AH IR FK LR VK FH F	3148
  BD-11	LK AK IK FK VK LK IK F	3149
  BD-12	WIW KHK FL HRH FLF	3150
  BD-13	VFL HRH VI KHK LVF	3151
  BD-14	FL HKH VL RHR IVF	3152
  BD-15	VF KHK IV HRH ILF	3153
  BD-16	FLF KH LFL HR IFF	3154
  BD-17	LF KH ILI HR VIF	3155
  BD-18	FL HKH LF KHK LF	3156
  BD-19	VF RHR FI HRH VF	3157
  BD-20	FI HK LV HKH VLF	3158
  BD-21	VL RH LF RHR IVF	3159
  BD-22	LV HK LIL RH LLF	3160
  BD-23	VF KR VLI HK LIF	3161
  BD-24	IV RK FLF RHK VF	3162
  BD-25	VL KH VIA HKR LF	3163
  BD-26	FI RK FLF KH LF	3164
  BD-27	VI RH VWV RK LF	3165
  BD-28	FLF RHR F RHR LVF	3166
  BD-29	LFL HKH A KHK FLF	3167
  BD-30	F KHK F KHK FIF	3168
  BD-31	L RHR L RHR LIF	3169
  BD-32	LIL K FLF K FVF	3170
  BD-33	VLI R ILV R VIF	3171
  BD-34	F RHR F RHR F	3172
  BD-35	L KHK L KHK F	3173
  BD-36	F K F KHK LIF	3174
  BD-37	L R L RHR VLF	3175
  BD-38	F K FLF K FLF	3176
  BD-39	L R LFL R WLF	3177
  BD-40	F K FLF KHK F	3178
  BD-41	L R LFL RHR F	3179
  BD-42	FKFLFKF	3180
  BD-43	LRLFLRF	3181
  AA-1	HHFFHHFHHFFHHF*	3182
  AA-2	FHFFHEIFFHFFHHF*	3183
  AA-3	KLLK-GAT-FHFFHHFFHFFHHF	3184
  AA-4	KLLK-FHFFHHFFHFFHHF	3185
  AA-5	FHFFHHFFHFFHHFKLLK	3186
  RIP	YSPWTNF*	3187
  Lariatin A	c(Gly-Ser-Gln-Leu-Val-Tyr-Arg-Glu)-Trp-	3188
  (anti-mycobacteria)	Val-Gly-His-Ser-Asn-Val-Ile-Lys-Pro
  Lariatin B	c(Gly-Ser-Gln-Leu-Val-Tyr-Arg-Glu)-Trp-	3189
  (anti-mycobacteria)	Val-Gly-His-Ser-Asn-Val-Ile-Lys-Gly-
  	Pro-Pro
  Abreviations:
  U-Aminoisobutyric Acid (Aib);
  J-Isovaline (Iva);
  O-Hydroxyproline (Hyp);
  Z-Ethylnorvaline (EtNor);
  x or xx means L or I at that position;
  Ac-optionally acetylated N-term;
  OH, OCH3-optional C-term;
  Alkane long chains are noted in brackets;
  *optionally amidated C-terminus. Where protecting groups are shown, the gropus are optional. Conversely any of the peptides shown without protecting groups can, optionally one or more protecting groups. Where peptides are shown circularized, linear forms bear are also contemplated. Conversely, where linear peptides are shown circularlized versions are also contemplated.

• In certain embodiments the antimicrobial peptide consists of or comprises the amino acid sequence of LL-37 (LLGDFFRK SKEKIGKEFKRIVQRIKD FLRNL VPRTES, SEQ ID NO:3190) or a variant of LL-37. LL-37 is a cathelicidin anti-microbial corresponding to amino acids 134-170 of the human cationic antimicrobial protein 18 (hCAP18). In certain embodiments the antimicrobial peptide consists of or comprises the amino acid sequence of an LL-37 variant as described in U.S. Patent Publication No: 2009/0156499 A1). Illustrative variants comprise or consist of the amino acid sequence having at least 90%, 95%, or 98% sequence identity with the amino acid sequence FKRIVQRIKDFLRX₁ (SEQ ID NO:3191), where X₁ is selected from the group consisting of 0, 1, 2, 3, 4, 5, 6, 7, and 8 amino acids. In certain embodiments illustrative variants comprise or consist of the amino acid sequence having at least 90%, 95%, or 98% sequence identity with the amino acid sequence X₁RLFDKIRQVIRKFX₂ (SEQ ID NO:3192) where X₁ is 0, 1, 2, 3, 4, 5, 6, 7, or 8 amino acids and X₂ is 0, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, or 16 amino acids.
• In certain embodiments the antimicrobial peptide consists of or comprises the amino acid sequence of an LL-37 variant shown in Table 15.

• TABLE 15
  LL-37 peptide and variants.

  		SEQ
  		ID
  ID	Amino acid sequence	NO
  LL-37	LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNL	3193
  	VPRTES
  Cys-LL -37	CLLGDFFRKSKEKIGKEFKRIVQRIKDFLRN	3194
  	LVPRTES
  LL-37(17-32)	FKRIVQRIKDFLRNLV	3195
  Cys-LL-37-	CLLGDFFRKSKEKIGKEFKRIVQRIKDFLRN	3196
  Cys	LVPRTESC
  LL-37FK-13	FKRIVQRIKDFLR	3197
  LL-37FKR	FKRIVQRIKDFLRNLVPRTES	3198
  LL-37GKE	GKEFKRIVQRIKDFLRNLVPR	3199
  LL-37KRI	KRIVQRIKDFLRNLVPRTES	3200
  LL-37LLG	LLGDFFRKSKEKIGKEFKRIV	3201
  LL-37RKS	RKSKEKIGKEFKRIVQRIKDFLRNLVPRTES	3202
  LL-37SKE	SKEKIGKEFKRIVQRIKDFLR	3203
  LL-37-Cys	LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNL	3204
  	VPRTESC

• A number of antimicrobial peptides are also disclosed in U.S. Pat. Nos. 7,271,239, 7,223,840, 7,176,276, 6,809,181, 6,699,689, 6,420,116, 6,358,921, 6,316,594, 6,235,973, 6,183,992, 6,143,498, 6,042,848, 6,040,291, 5,936,063, 5,830,993, 5,428,016, 5,424,396, 5,032,574, 4,623,733, which are incorporated herein by reference for the disclosure of particular antimicrobial peptides.
• v. Ligands.
• In certain embodiments the effector can comprise one ore more ligands, epitope tags, and/or antibodies. In certain embodiments preferred ligands and antibodies include those that bind to surface markers on immune cells. Chimeric moieties utilizing such antibodies as effector molecules act as bifunctional linkers establishing an association between the immune cells bearing binding partner for the ligand or antibody and the target microorganism(s).
• The terms “epitope tag” or “affinity tag” are used interchangeably herein, and used refers to a molecule or domain of a molecule that is specifically recognized by an antibody or other binding partner. The term also refers to the binding partner complex as well. Thus, for example, biotin or a biotin/avidin complex are both regarded as an affinity tag. In addition to epitopes recognized in epitope/antibody interactions, affinity tags also comprise “epitopes” recognized by other binding molecules (e.g. ligands bound by receptors), ligands bound by other ligands to form heterodimers or homodimers, His₆ bound by Ni-NTA, biotin bound by avidin, streptavidin, or anti-biotin antibodies, and the like.
• Epitope tags are well known to those of skill in the art. Moreover, antibodies specific to a wide variety of epitope tags are commercially available. These include but are not limited to antibodies against the DYKDDDDK (SEQ ID NO:3205) epitope, c-myc antibodies (available from Sigma, St. Louis), the HNK-1 carbohydrate epitope, the HA epitope, the HSV epitope, the His₄ (SEQ ID NO:3206), His₅ (SEQ ID NO:3207), and His₆ (SEQ ID NO:3208) epitopes that are recognized by the His epitope specific antibodies (see, e.g., Qiagen), and the like. In addition, vectors for epitope tagging proteins are commercially available. Thus, for example, the pCMV-Tag1 vector is an epitope tagging vector designed for gene expression in mammalian cells. A target gene inserted into the pCMV-Tag1 vector can be tagged with the FLAG® epitope (N-terminal, C-terminal or internal tagging), the c-myc epitope (C-terminal) or both the FLAG (N-terminal) and c-myc (C-terminal) epitopes.
• vi. Lipids and Liposomes.
• In certain embodiments the effectors comprise one or more microparticles or nanoparticles that can be loaded with an effector agent (e.g., a pharmaceutical, a label, etc.). In certain embodiments the microparticles or nanoparticles are lipidic particles. Lipidic particles are microparticles or nanoparticles that include at least one lipid component forming a condensed lipid phase. Typically, a lipidic nanoparticle has preponderance of lipids in its composition. Various condensed lipid phases include solid amorphous or true crystalline phases; isomorphic liquid phases (droplets); and various hydrated mesomorphic oriented lipid phases such as liquid crystalline and pseudocrystalline bilayer phases (L-alpha, L-beta, P-beta, Lc), interdigitated bilayer phases, and nonlamellar phases (see, e.g., The Structure of Biological Membranes, ed. by P. Yeagle, CRC Press, Bora Raton, Fla., 1991). Lipidic microparticles include, but are not limited to a liposome, a lipid-nucleic acid complex, a lipid-drug complex, a lipid-label complex, a solid lipid particle, a microemulsion droplet, and the like. Methods of making and using these types of lipidic microparticles and nanoparticles, as well as attachment of affinity moieties, e.g., antibodies, to them are known in the art (see, e.g., U.S. Pat. Nos. 5,077,057; 5,100,591; 5,616,334; 6,406,713; 5,576,016; 6,248,363; Bondi et al. (2003) Drug Delivery 10: 245-250; Pedersen et al., (2006) Eur. J. Pharm. Biopharm. 62: 155-162, 2006 (solid lipid particles); U.S. Pat. Nos. 5,534,502; 6,720,001; Shiokawa et al. (2005) Clin. Cancer Res. 11: 2018-2025 (microemulsions); U.S. Pat. No. 6,071,533 (lipid-nucleic acid complexes), and the like).
• A liposome is generally defined as a particle comprising one or more lipid bilayers enclosing an interior, typically an aqueous interior. Thus, a liposome is often a vesicle formed by a bilayer lipid membrane. There are many methods for the preparation of liposomes. Some of them are used to prepare small vesicles (d<0.05 micrometer), some for larger vesicles (d>0.05 micrometer). Some are used to prepare multilamellar vesicles, some for unilamellar ones. Methods for liposome preparation are exhaustively described in several review articles such as Szoka and Papahadjopoulos (1980) Ann. Rev. Biophys. Bioeng., 9: 467, Deamer and Uster (1983) Pp. 27-51 In: Liposomes, ed. M. J. Ostro, Marcel Dekker, New York, and the like.
• In various embodiments the liposomes include a surface coating of a hydrophilic polymer chain. “Surface-coating” refers to the coating of any hydrophilic polymer on the surface of liposomes. The hydrophilic polymer is included in the liposome by including in the liposome composition one or more vesicle-forming lipids derivatized with a hydrophilic polymer chain. In certain embodiments, vesicle-forming lipids with diacyl chains, such as phospholipids, are preferred. One illustrative phospholipid is phosphatidylethanolamine (PE), which contains a reactive amino group convenient for coupling to the activated polymers. One illustrative PE is distearoyl PE (DSPE). Another example is non-phospholipid double chain amphiphilic lipids, such as diacyl- or dialkylglycerols, derivatized with a hydrophilic polymer chain.
• In certain embodiments a hydrophilic polymer for use in coupling to a vesicle forming lipid is polyethyleneglycol (PEG), preferably as a PEG chain having a molecular weight between 1,000-10,000 Daltons, more preferably between 1,000-5,000 Daltons, most preferably between 2,000-5,000 Daltons. Methoxy or ethoxy-capped analogues of PEG are also useful hydrophilic polymers, commercially available in a variety of polymer sizes, e.g., 120-20,000 Daltons.
• Other hydrophilic polymers that can be suitable include, but are not limited to polylactic acid, polyglycolic acid, polyvinylpyrrolidone, polymethyloxazoline, polyethyloxazoline, polyhydroxypropyl methacrylamide, polymethacrylamide, polydimethylacrylamide, and derivatized celluloses, such as hydroxymethylcellulose or hydroxyethylcellulose.
• Preparation of lipid-polymer conjugates containing these polymers attached to a suitable lipid, such as PE, have been described.
• The liposomes can, optionally be prepared for attachment to one or more targeting moieties described herein. Here the lipid component included in the liposomes would include either a lipid derivatized with the targeting moiety, or a lipid having a polar-head chemical group, e.g., on a linker, that can be derivatized with the targeting moiety in preformed liposomes, according to known methods.
• Methods of functionalizing lipids and liposomes with affinity moieties such as antibodies are well known to those of skill in the art (see, e.g., DE 3,218,121; Epstein et al. (1985) Proc. Natl. Acad. Sci., USA, 82:3688 (1985); Hwang et al. (1980) Proc. Natl. Acad. Sci., USA, 77: 4030; EP 52,322; EP 36,676; EP 88,046; EP 143,949; EP 142,641; Japanese patent application 83-118008; U.S. Pat. Nos. 4,485,045 and 4,544,545; and EP 102,324, all of which are incorporated herein by reference).
• vii. Agents that Physically Disrupt the Extracellular Matrix within a Community of Microorganisms
• In certain embodiments, peptides can be coupled to agents that physically disrupt the extracellular matrix within a community of microorganisms, for example a biofilm. In certain preferred embodiments, such an agent could be a bacterial cell-wall degrading enzyme, for example SAL-2, or any species of glycosidase, alginase, peptidase, proteinase, lipase, or DNA or RNA degrading enzyme or compound, for example rhRNase. Disruption of extracellular matrix of biofilms can result in clearance and therapeutic benefit.
• Peptides can also be attached to antimicrobial proteins, such as Protein Inhibitor C or Colicin, or fragments thereof, for example the IIa domain of Colicin, or the heparin-binding domain of Protein Inhibitor C.
• viii. Polymeric Microparticles and/or Nanoparticles.
• In certain embodiments the effector(s) comprise polymeric microparticles and/or nanoparticles and/or micelles.
• Microparticle and nanoparticle-based drug delivery systems have considerable potential for treatment of various microorganisms. Technological advantages of polymeric microparticles or nanoparticles used as drug carriers are high stability, high carrier capacity, feasibility of incorporation of both hydrophilic and hydrophobic substances, and feasibility of variable routes of administration, including oral application and inhalation. Polymeric nanoparticles can also be designed to allow controlled (sustained) drug release from the matrix. These properties of nanoparticles enable improvement of drug bioavailability and reduction of the dosing frequency.
• Polymeric nanoparticles are typically micron or submicron (<1 μm) colloidal particles. This definition includes monolithic nanoparticles (nanospheres) in which the drug is adsorbed, dissolved, or dispersed throughout the matrix and nanocapsules in which the drug is confined to an aqueous or oily core surrounded by a shell-like wall. Alternatively, in certain embodiments, the drug can be covalently attached to the surface or into the matrix.
• Polymeric microparticles and nanoparticles are typically made from biocompatible and biodegradable materials such as polymers, either natural (e.g., gelatin, albumin) or synthetic (e.g., polylactides, polyalkylcyanoacrylates), or solid lipids. In the body, the drug loaded in nanoparticles is usually released from the matrix by diffusion, swelling, erosion, or degradation. One commonly used material is poly(lactide-co-glycolide) (PLG).
• Methods of fabricating and loading polymeric nanoparticles or microparticles are well known to those of skill in the art. Thus, for example, Matsumoto et al. (1999) Intl. J. Pharmaceutics, 185: 93-101 teaches the fabrication of poly(L-lactide)-poly(ethylene glycol)-poly(L-lactide) nanoparticles, Chawla et al. (2002) Intl. J. Pharmaceutics 249: 127-138, teaches the fabrication and use of poly(e-caprolactone) nanoparticles delivery of tamifoxen, and Bodmeier et al. (1988) Intl. J. Pharmaceutics, 43: 179-186, teaches the preparation of poly(D,L-lactide) microspheres using a solvent evaporation method. “Intl. J. Pharmaceutics, 1988, 43, 179-186. Other nanoparticle formulations are described, for example, by Williams et al. (2003) J. Controlled Release, 91: 167-172; Leroux et al. (1996) J. Controlled Release, 39: 339-350; Soppimath et al. (2001) J. Controlled Release, 70: 1-20; Brannon-Peppas (1995) Intl. J. Pharmaceutics, 116: 1-9; and the like.
• C) Peptide Preparation.
• The peptides described herein can be chemically synthesized using standard chemical peptide synthesis techniques or, particularly where the peptide does not comprise “D” amino acid residues, the peptide can be recombinantly expressed. Where the “D” polypeptides are recombinantly expressed, a host organism (e.g. bacteria, plant, fungal cells, etc.) can be cultured in an environment where one or more of the amino acids is provided to the organism exclusively in a D form. Recombinantly expressed peptides in such a system then incorporate those D amino acids.
• In certain embodiments, D amino acids can be incorporated in recombinantly expressed peptides using modified amino acyl-tRNA synthetases that recognize D-amino acids.
• In certain embodiments the peptides are chemically synthesized by any of a number of fluid or solid phase peptide synthesis techniques known to those of skill in the art. Solid phase synthesis in which the C-terminal amino acid of the sequence is attached to an insoluble support followed by sequential addition of the remaining amino acids in the sequence is a preferred method for the chemical synthesis of the polypeptides of this invention. Techniques for solid phase synthesis are well known to those of skill in the art and are described, for example, by Barany and Merrifield (1963) Solid-Phase Peptide Synthesis; pp. 3-284 in The Peptides: Analysis, Synthesis, Biology. Vol. 2: Special Methods in Peptide Synthesis, Part A.; Merrifield et al. (1963) J. Am. Chem. Soc., 85: 2149-2156, and Stewart et al. (1984) Solid Phase Peptide Synthesis, 2nd ed. Pierce Chem. Co., Rockford, Ill.
• In one embodiment, the peptides can be synthesized by the solid phase peptide synthesis procedure using a benzhyderylamine resin (Beckman Bioproducts, 0.59 mmol of NH₂/g of resin) as the solid support. The COOH terminal amino acid (e.g., t-butylcarbonyl-Phe) is attached to the solid support through a 4-(oxymethyl)phenacetyl group. This is a more stable linkage than the conventional benzyl ester linkage, yet the finished peptide can still be cleaved by hydrogenation. Transfer hydrogenation using formic acid as the hydrogen donor can be used for this purpose.
• It is noted that in the chemical synthesis of peptides, particularly peptides comprising D amino acids, the synthesis usually produces a number of truncated peptides in addition to the desired full-length product. Thus, the peptides are typically purified using, e.g., HPLC.
• D-amino acids, beta amino acids, non-natural amino acids, and the like can be incorporated at one or more positions in the peptide simply by using the appropriately derivatized amino acid residue in the chemical synthesis. Modified residues for solid phase peptide synthesis are commercially available from a number of suppliers (see, e.g., Advanced Chem Tech, Louisville; Nova Biochem, San Diego; Sigma, St Louis; Bachem Calif. Inc., Torrance, etc.). The D-form and/or otherwise modified amino acids can be completely omitted or incorporated at any position in the peptide as desired. Thus, for example, in certain embodiments, the peptide can comprise a single modified acid, while in other embodiments, the peptide comprises at least two, generally at least three, more generally at least four, most generally at least five, preferably at least six, more preferably at least seven or even all modified amino acids. In certain embodiments, essentially every amino acid is a D-form amino acid.
• As indicated above, the peptides and/or fusion proteins of this invention can also be recombinantly expressed. Accordingly, in certain embodiments, the antimicrobial peptides and/or targeting moieties, and/or fusion proteins of this invention are synthesized using recombinant expression systems. Generally this involves creating a DNA sequence that encodes the desired peptide or fusion protein, placing the DNA in an expression cassette under the control of a particular promoter, expressing the peptide or fusion protein in a host, isolating the expressed peptide or fusion protein and, if required, renaturing the peptide or fusion protein.
• DNA encoding the peptide(s) or fusion protein(s) described herein can be prepared by any suitable method as described above, including, for example, cloning and restriction of appropriate sequences or direct chemical synthesis.
• This nucleic acid can be easily ligated into an appropriate vector containing appropriate expression control sequences (e.g. promoter, enhancer, etc.), and, optionally, containing one or more selectable markers (e.g. antibiotic resistance genes).
• The nucleic acid sequences encoding the peptides or fusion proteins described herein can be expressed in a variety of host cells, including, but not limited to, E. coli, other bacterial hosts, yeast, fungus, and various higher eukaryotic cells such as insect cells (e.g. SF3), the COS, CHO and HeLa cells lines and myeloma cell lines. The recombinant protein gene will typically be operably linked to appropriate expression control sequences for each host. For E. coli this can include a promoter such as the T7, trp, or lambda promoters, a ribosome binding site and preferably a transcription termination signal. For eukaryotic cells, the control sequences can include a promoter and often an enhancer (e.g., an enhancer derived from immunoglobulin genes, SV40, cytomegalovirus, etc.), and a polyadenylation sequence, and may include splice donor and acceptor sequences.
• The plasmids can be transferred into the chosen host cell by well-known methods such as calcium chloride transformation for E. coli and calcium phosphate treatment or electroporation for mammalian cells. Cells transformed by the plasmids can be selected by resistance to antibiotics conferred by genes contained on the plasmids, such as the amp, gpt, neo and hyg genes.
• Once expressed, the recombinant peptide(s) or fusion protein(s) can be purified according to standard procedures of the art, including ammonium sulfate precipitation, affinity columns, column chromatography, gel electrophoresis and the like (see, generally, R. Scopes, (1982) Protein Purification, Springer-Verlag, N.Y.; Deutscher (1990) Methods in Enzymology Vol. 182: Guide to Protein Purification., Academic Press, Inc. N.Y.). Substantially pure compositions of at least about 90 to 95% homogeneity are preferred, and 98 to 99% or more homogeneity are most preferred.
• One of skill in the art would recognize that after chemical synthesis, biological expression, or purification, the peptide(s) or fusion protein(s) may possess a conformation substantially different than desired native conformation. In this case, it may be necessary to denature and reduce the peptide or fusion protein and then to cause the molecule to re-fold into the preferred conformation. Methods of reducing and denaturing proteins and inducing re-folding are well known to those of skill in the art (see, e.g., Debinski et al. (1993) J. Biol. Chem., 268: 14065-14070; Kreitman and Pastan (1993) Bioconjug. Chem., 4: 581-585; and Buchner, et al., (1992) Anal. Biochem., 205: 263-270). Debinski et al., for example, describes the denaturation and reduction of inclusion body proteins in guanidine-DTE. The protein is then refolded in a redox buffer containing oxidized glutathione and L-arginine.
• One of skill would recognize that modifications can be made to the peptide(s) and/or fusion protein(s) proteins without diminishing their biological activity. Some modifications may be made to facilitate the cloning, expression, or incorporation of the targeting molecule into a fusion protein. Such modifications are well known to those of skill in the art and include, for example, a methionine added at the amino terminus to provide an initiation site, or additional amino acids (e.g., poly His) placed on either terminus to create conveniently located restriction sites or termination codons or purification sequences.
• D) Joining Targeting Moieties to Effectors.
• i. Chemical Conjugation.
• Chimeric moieties are formed by joining one or more of the targeting moieties described herein to one or more effectors. In certain embodiments the targeting moieties are attached directly to the effector(s) via naturally occurring reactive groups or the targeting moiety and/or the effector(s) can be functionalized to provide such reactive groups.
• In various embodiments the targeting moieties are attached to effector(s) via one or more linking agents. Thus, in various embodiments the targeting moieties and the effector(s) can be conjugated via a single linking agent or multiple linking agents. For example, the targeting moiety and the effector can be conjugated via a single multifunctional (e.g., bi-, tri-, or tetra-) linking agent or a pair of complementary linking agents. In another embodiment, the targeting moiety and the effector are conjugated via two, three, or more linking agents. Suitable linking agents include, but are not limited to, e.g., functional groups, affinity agents, stabilizing groups, and combinations thereof
• In certain embodiments the linking agent is or comprises a functional group. Functional groups include monofunctional linkers comprising a reactive group as well as multifunctional crosslinkers comprising two or more reactive groups capable of forming a bond with two or more different functional targets (e.g., labels, proteins, macromolecules, semiconductor nanocrystals, or substrate). In some preferred embodiments, the multifunctional crosslinkers are heterobifunctional crosslinkers comprising two or more different reactive groups.
• Suitable reactive groups include, but are not limited to thiol (—SH), carboxylate (COOH), carboxyl (—COOH), carbonyl, amine (NH₂), hydroxyl (—OH), aldehyde (—CHO), alcohol (ROH), ketone (R₂CO), active hydrogen, ester, sulfhydryl (SH), phosphate (—PO₃), or photoreactive moieties. Amine reactive groups include, but are not limited to e.g., isothiocyanates, isocyanates, acyl azides, NHS esters, sulfonyl chlorides, aldehydes and glyoxals, epoxides and oxiranes, carbonates, arylating agents, imidoesters, carbodiimides, and anhydrides. Thiol-reactive groups include, but are not limited to e.g., haloacetyl and alkyl halide derivates, maleimides, aziridines, acryloyl derivatives, arylating agents, and thiol-disulfides exchange reagents. Carboxylate reactive groups include, but are not limited to e.g., diazoalkanes and diazoacetyl compounds, such as carbonyldiimidazoles and carbodiimides. Hydroxyl reactive groups include, but are not limited to e.g., epoxides and oxiranes, carbonyldiimidazole, oxidation with periodate, N,N′-disuccinimidyl carbonate or N-hydroxylsuccimidyl chloroformate, enzymatic oxidation, alkyl halogens, and isocyanates. Aldehyde and ketone reactive groups include, but are not limited to e.g., hydrazine derivatives for schiff base formation or reduction amination. Active hydrogen reactive groups include, but are not limited to e.g., diazonium derivatives for mannich condensation and iodination reactions. Photoreactive groups include, but are not limited to e.g., aryl azides and halogenated aryl azides, benzophenones, diazo compounds, and diazirine derivatives.
• Other suitable reactive groups and classes of reactions useful in forming chimeric moieties include those that are well known in the art of bioconjugate chemistry. Currently favored classes of reactions available with reactive chelates are those which proceed under relatively mild conditions. These include, but are not limited to, nucleophilic substitutions (e.g., reactions of amines and alcohols with acyl halides, active esters), electrophilic substitutions (e.g., enamine reactions), and additions to carbon-carbon and carbon-heteroatom multiple bonds (e.g., Michael reaction, Diels-Alder addition). These and other useful reactions are discussed in, for example, March (1985) Advanced Organic Chemistry, 3rd Ed., John Wiley & Sons, New York, Hermanson (1996) Bioconjugate Techniques, Academic Press, San Diego; and Feeney et al. (1982) Modification of Proteins; Advances in Chemistry Series, Vol. 198, American Chemical Society, Washington, D.C.
• In certain embodiments, the linking agent comprises a chelator. For example, the chelator comprising the molecule, DOTA (DOTA=1,4,7,10-tetrakis(carboxymethyl)-1,4,7,10-tetraazacyclododecane), can readily be labeled with a radiolabel, such as Gd³⁺ and ⁶⁴Cu, resulting in Gd³⁺-DOTA and ⁶⁴Cu-DOTA respectively, attached to the targeting moiety. Other suitable chelates are known to those of skill in the art, for example, 1,4,7-triazacyclononane-N,N′,N″-triacetic acid (NOTA) derivatives being among the most well known (see, e.g., Lee et al. (1997) Nucl Med Biol. 24: 2225-23019).
• A “linker” or “linking agent” as used herein, is a molecule that is used to join two or more molecules. In certain embodiments the linker is typically capable of forming covalent bonds to both molecule(s) (e.g., the targeting moiety and the effector). Suitable linkers are well known to those of skill in the art and include, but are not limited to, straight or branched-chain carbon linkers, heterocyclic carbon linkers, or peptide linkers. In certain embodiments the linkers can be joined to the constituent amino acids through their side groups (e.g., through a disulfide linkage to cysteine). However, in certain embodiments, the linkers will be joined to the alpha carbon amino and carboxyl groups of the terminal amino acids.
• A bifunctional linker having one functional group reactive with a group on one molecule (e.g., a targeting peptide), and another group reactive on the other molecule (e.g., an antimicrobial peptide), can be used to form the desired conjugate. Alternatively, derivatization can be performed to provide functional groups. Thus, for example, procedures for the generation of free sulfhydryl groups on peptides are also known (See U.S. Pat. No. 4,659,839).
• In certain embodiments the linking agent is a heterobifunctional crosslinker comprising two or more different reactive groups that form a heterocyclic ring that can interact with a peptide. For example, a heterobifunctional crosslinker such as cysteine may comprise an amine reactive group and a thiol-reactive group can interact with an aldehyde on a derivatized peptide. Additional combinations of reactive groups suitable for heterobifunctional crosslinkers include, for example, amine- and sulfhydryl reactive groups; carbonyl and sulfhydryl reactive groups; amine and photoreactive groups; sulfhydryl and photoreactive groups; carbonyl and photoreactive groups; carboxylate and photoreactive groups; and arginine and photoreactive groups. In one embodiment, the heterobifunctional crosslinker is SMCC.
• Many procedures and linker molecules for attachment of various molecules to peptides or proteins are known (see, e.g., European Patent Application No. 188,256; U.S. Pat. Nos. 4,671,958, 4,659,839, 4,414,148, 4,699,784; 4,680,338; 4,569,789; and 4,589,071; and Borlinghaus et al. (1987) Cancer Res. 47: 4071-4075). Illustrative linking protocols are provided herein in Examples 2 and 3.
• ii. Fusion Proteins.
• In certain embodiments where the targeting moiety and effector are both peptides or both comprise peptides, the chimeric moiety can be chemically synthesized or recombinantly expressed as a fusion protein (i.e., a chimeric fusion protein).
• In certain embodiments the chimeric fusion proteins are synthesized using recombinant DNA methodology. Generally this involves creating a DNA sequence that encodes the fusion protein, placing the DNA in an expression cassette under the control of a particular promoter, expressing the protein in a host, isolating the expressed protein and, if required, renaturing the protein.
• DNA encoding the fusion proteins can be prepared by any suitable method, including, for example, cloning and restriction of appropriate sequences or direct chemical synthesis by methods such as the phosphotriester method of Narang et al. (1979) Meth. Enzymol. 68: 90-99; the phosphodiester method of Brown et al. (1979)Meth. Enzymol. 68: 109-151; the diethylphosphoramidite method of Beaucage et al. (1981) Tetra. Lett., 22: 1859-1862; and the solid support method of U.S. Pat. No. 4,458,066.
• Chemical synthesis produces a single stranded oligonucleotide. This can be converted into double stranded DNA by hybridization with a complementary sequence or by polymerization with a DNA polymerase using the single strand as a template. One of skill would recognize that while chemical synthesis of DNA is limited to sequences of about 100 bases, longer sequences can be obtained by the ligation of shorter sequences.
• Alternatively, subsequences can be cloned and the appropriate subsequences cleaved using appropriate restriction enzymes. The fragments can then be ligated to produce the desired DNA sequence.
• In certain embodiments, DNA encoding fusion proteins of the present invention may be cloned using DNA amplification methods such as polymerase chain reaction (PCR). Thus, for example, the nucleic acid encoding a targeting antibody, a targeting peptide, and the like is PCR amplified, using a sense primer containing the restriction site for NdeI and an antisense primer containing the restriction site for HindIII. This produces a nucleic acid encoding the targeting sequence and having terminal restriction sites. Similarly an effector and/or effector/linker/spacer can be provided having complementary restriction sites. Ligation of sequences and insertion into a vector produces a vector encoding the fusion protein.
• While the targeting moieties and effector(s) can be directly joined together, one of skill will appreciate that they can be separated by a peptide spacer/linker consisting of one or more amino acids. Generally the spacer will have no specific biological activity other than to join the proteins or to preserve some minimum distance or other spatial relationship between them. However, the constituent amino acids of the spacer may be selected to influence some property of the molecule such as the folding, net charge, or hydrophobicity.
• The nucleic acid sequences encoding the fusion proteins can be expressed in a variety of host cells, including E. coli, other bacterial hosts, yeast, and various higher eukaryotic cells such as the COS, CHO and HeLa cells lines and myeloma cell lines. The recombinant protein gene will be operably linked to appropriate expression control sequences for each host. For E. coli this includes a promoter such as the T7, trp, or lambda promoters, a ribosome binding site and preferably a transcription termination signal. For eukaryotic cells, the control sequences will include a promoter and preferably an enhancer derived from immunoglobulin genes, SV40, cytomegalovirus, etc., and a polyadenylation sequence, and may include splice donor and acceptor sequences.
• The plasmids can be transferred into the chosen host cell by well-known methods such as calcium chloride transformation for E. coli and calcium phosphate treatment or electroporation for mammalian cells. Cells transformed by the plasmids can be selected by resistance to antibiotics conferred by genes contained on the plasmids, such as the amp, gpt, neo and hyg genes.
• Once expressed, the recombinant fusion proteins can be purified according to standard procedures of the art, including ammonium sulfate precipitation, affinity columns, column chromatography, gel electrophoresis and the like (see, generally, R. Scopes (1982) Protein Purification, Springer-Verlag, N.Y.; Deutscher (1990) Methods in Enzymology Vol. 182: Guide to Protein Purification., Academic Press, Inc. N.Y.). Substantially pure compositions of at least about 90 to 95% homogeneity are preferred, and 98 to 99% or more homogeneity are most preferred for pharmaceutical uses. Once purified, partially or to homogeneity as desired, the polypeptides may then be used therapeutically.
• One of skill in the art would recognize that after chemical synthesis, biological expression, or purification, the fusion protein may possess a conformation substantially different than the native conformations of the constituent polypeptides. In this case, it may be necessary to denature and reduce the polypeptide and then to cause the polypeptide to re-fold into the preferred conformation. Methods of reducing and denaturing proteins and inducing re-folding are well known to those of skill in the art (See, Debinski et al. (1993) J. Biol. Chem., 268: 14065-14070; Kreitman and Pastan (1993) Bioconjug. Chem., 4: 581-585; and Buchner, et al. (1992) Anal. Biochem., 205: 263-270).
• One of skill would recognize that modifications can be made to the fusion proteins without diminishing their biological activity. Some modifications may be made to facilitate the cloning, expression, or incorporation of the targeting molecule into a fusion protein. Such modifications are well known to those of skill in the art and include, for example, a methionine added at the amino terminus to provide an initiation site, or additional amino acids placed on either terminus to create conveniently located restriction sites or termination codons.
• As indicated above, in various embodiments a peptide linker/spacer is used to join the one or more targeting moieties to one or more effector(s). In various embodiments the peptide linker is relatively short, typically less than about 10 amino acids, preferably less than about 8 amino acids and more preferably about 3 to about 5 amino acids. Suitable illustrative linkers include, but are not limited to PSGSP ((SEQ ID NO:3209), ASASA (SEQ ID NO: 3210), or GGG. In certain embodiments longer linkers such as (GGGGS)₃ (SEQ ID NO:3211) can be used. Illustrative peptide linkers and other linkers are shown in Table 16.

• TABLE 16
  Illustrative peptide and non-peptide linkers.

  Linker	SEQ ID NO:
  AAA
  GGG
  GGGG	3212
  SGG
  GGSGGS	3213
  SAT
  PYP
  PSPSP	3214
  ASA
  ASASA	3215
  PSPSP	3216
  KKKK	3217
  RRRR	3218
  GGGGS	3219
  GGGGS GGGGS	3220
  GGGGS GGGGS GGGGS	3221
  GGGGS GGGGS GGGGS GGGGS	3222
  GGGGS GGGGS GGGGS GGGGS GGGGS	3223
  GGGGS GGGGS GGGGS GGGGS GGGGS GGGGS	3224
  2-nitrobenzene or O-nitrobenzyl
  Nitropyridyl disulfide
  Dioleoylphosphatidylethanolamine (DOPE)
  S-acetylmercaptosuccinic acid
  1, 4, 7, 10-tetraa7acyclododecane-1, 4, 7, 10-tetracetic acid (DOTA)
  β-glucuronide and β-glucuronide variants
  Poly(alkylacrylic acid)
  Benzene-based linkers (for example: 2,5-Bis(hexyloxy)-1,4-bis[2,5-
  bis(hexyloxy)-4-formyl-phenylenevinylene]benzene) and like
  molecules
  Disulfide linkages
  Poly(amidoamine) or like dendrimers linking multiple target
  and killing peptides in one molecule
  Carbon nanotubes
  Hydrazone and hydrazone variant linkers
  PEG of any chain length
  Succinate, formate, acetate butyrate, other like organic acids
  Aldols, alcohols, or enols
  Peroxides
  alkane or alkene groups of any chain length
  One or more porphyrin or dye molecules containing free amide and
  carboxylic acid groups
  One or more DNA or RNA nucleotides, including polyamine and
  polycarboxyl-containing variants
  Inulin, sucrose, glucose, or other single, di or polysaccharides
  Linoleic acid or other polyunsaturated fatty acids
  Variants of any of the above linkers containing halogen or thiol
  groups
  (All amino-acid-based linkers could be L, D, combinations of L and D forms, β-form, and the like)

• E) Multiple Targeting Moieties and/or Effectors.
• As indicated above, in certain embodiments, the chimeric moieties described herein comprise multiple targeting moieties attached to a single effector or multiple effectors attached to a single targeting moiety, or multiple targeting moieties attached to multiple effectors.
• Where the chimeric construct is a fusion protein this is easily accomplished by providing multiple domains that are targeting domains attached to one or more effector domains. FIG. 14 schematically illustrates a few, but not all, configurations. In various embodiments the multiple targeting domains and/or multiple effector domains can be attached to each other directly or can be separated by linkers (e.g., amino acid or peptide linkers as described above).
• When the chimeric construct is a chemical conjugate linear or branched configurations (e.g., as illustrated in FIG. 14) are readily produced by using branched or multifunctional linkers and/or a plurality of different linkers.
• F) Protecting Groups.
• While the various peptides (e.g., targeting peptides, antimicrobial peptides, STAMPs) described herein may be shown with no protecting groups, in certain embodiments they can bear one, two, three, four, or more protecting groups. In various embodiments, the protecting groups can be coupled to the C- and/or N-terminus of the peptide(s) and/or to one or more internal residues comprising the peptide(s) (e.g., one or more R-groups on the constituent amino acids can be blocked). Thus, for example, in certain embodiments, any of the peptides described herein can bear, e.g., an acetyl group protecting the amino terminus and/or an amide group protecting the carboxyl terminus. One example of such a protected peptide is the 1845L6-21 STAMP having the amino acid sequence KFINGVLSQFVLERKPYPKLFKFLRKHLL* (SEQ ID NO:3225), where the asterisk indicates an amidated carboxyl terminus. Of course, this protecting group can be can be eliminated and/or substituted with another protecting group as described herein.
• Without being bound by a particular theory, it was discovered that addition of a protecting group, particularly to the carboxyl and in certain embodiments the amino terminus can improve the stability and efficacy of the peptide.
• A wide number of protecting groups are suitable for this purpose. Such groups include, but are not limited to acetyl, amide, and alkyl groups with acetyl and alkyl groups being particularly preferred for N-terminal protection and amide groups being preferred for carboxyl terminal protection. In certain particularly preferred embodiments, the protecting groups include, but are not limited to alkyl chains as in fatty acids, propionyl, formyl, and others. Particularly preferred carboxyl protecting groups include amides, esters, and ether-forming protecting groups. In one preferred embodiment, an acetyl group is used to protect the amino terminus and an amide group is used to protect the carboxyl terminus. These blocking groups enhance the helix-forming tendencies of the peptides. Certain particularly preferred blocking groups include alkyl groups of various lengths, e.g., groups having the formula: CH₃—(CH₂)_n—CO— where n ranges from about 1 to about 20, preferably from about 1 to about 16 or 18, more preferably from about 3 to about 13, and most preferably from about 3 to about 10.
• In certain embodiments, the protecting groups include, but are not limited to alkyl chains as in fatty acids, propionyl, formyl, and others. Particularly preferred carboxyl protecting groups include amides, esters, and ether-forming protecting groups. In one embodiment, an acetyl group is used to protect the amino terminus and/or an amino group is used to protect the carboxyl terminus (i.e., amidated carboxyl terminus). In certain embodiments blocking groups include alkyl groups of various lengths, e.g., groups having the formula: CH₃—(CH₂)_n—CO— where n ranges from about 3 to about 20, preferably from about 3 to about 16, more preferably from about 3 to about 13, and most preferably from about 3 to about 10.
• In certain embodiments, the acid group on the C-terminal can be blocked with an alcohol, aldehyde or ketone group and/or the N-terminal residue can have the natural amide group, or be blocked with an acyl, carboxylic acid, alcohol, aldehyde, or ketone group.
• Other protecting groups include, but are not limited to Fmoc, t-butoxycarbonyl (t-BOC), 9-fluoreneacetyl group, 1-fluorenecarboxylic group, 9-florenecarboxylic group, 9-fluorenone-1-carboxylic group, benzyloxycarbonyl, xanthyl (Xan), trityl (Trt), 4-methyltrityl (Mtt), 4-methoxytrityl (Mmt), 4-methoxy-2,3,6-trimethyl-benzenesulphonyl (Mtr), Mesitylene-2-sulphonyl (Mts), 4,4-dimethoxybenzhydryl (Mbh), Tosyl (Tos), 2,2,5,7,8-pentamethyl chroman-6-sulphonyl (Pmc), 4-methylbenzyl (MeBzl), 4-methoxybenzyl (MeOBzl), benzyloxy (BzlO), benzyl (Bzl), benzoyl (Bz), 3-nitro-2-pyridinesulphenyl (Npys), 1-(4,4-dimentyl-2,6-diaxocyclohexylidene)ethyl (Dde), 2,6-dichlorobenzyl (2,6-DiCl-Bzl), 2-chlorobenzyloxycarbonyl (2-Cl—Z), 2-bromobenzyloxycarbonyl (2-Br—Z), Benzyloxymethyl (Bom), cyclohexyloxy (cHxO), t-butoxymethyl (Bum), t-butoxy (tBuO), t-Butyl (tBu), Acetyl (Ac), and Trifluoroacetyl (TFA).
• Protecting/blocking groups are well known to those of skill as are methods of coupling such groups to the appropriate residue(s) comprising the peptides of this invention (see, e.g., Greene et al., (1991) Protective Groups in Organic Synthesis, 2nd ed., John Wiley & Sons, Inc. Somerset, N.J.). In illustrative embodiment, for example, acetylation is accomplished during the synthesis when the peptide is on the resin using acetic anhydride. Amide protection can be achieved by the selection of a proper resin for the synthesis. For example, a rink amide resin can be used. After the completion of the synthesis, the semipermanent protecting groups on acidic bifunctional amino acids such as Asp and Glu and basic amino acid Lys, hydroxyl of Tyr are all simultaneously removed. The peptides released from such a resin using acidic treatment comes out with the n-terminal protected as acetyl and the carboxyl protected as NH₂ and with the simultaneous removal of all of the other protecting groups.
• Where amino acid sequences are disclosed herein, amino acid sequences comprising, one or more protecting groups, e.g., as described above (or any other commercially available protecting groups for amino acids used, e.g., in boc or fmoc peptide synthesis) are also contemplated.
• G) Peptide Circularization.
• In certain embodiments the peptides described herein (e.g., AMPs, compound AMPs, STAMPs, etc.) are circularized/cyclized to produce cyclic peptides. Cyclic peptides, as contemplated herein, include head/tail, head/side chain, tail/side chain, and side chain/side chain cyclized peptides. In addition, peptides contemplated herein include homodet, containing only peptide bonds, and heterodet containing in addition disulfide, ester, thioester-bonds, or other bonds.
• The cyclic peptides can be prepared using virtually any art-known technique for the preparation of cyclic peptides. For example, the peptides can be prepared in linear or non-cyclized form using conventional solution or solid phase peptide syntheses and cyclized using standard chemistries. Preferably, the chemistry used to cyclize the peptide will be sufficiently mild so as to avoid substantially degrading the peptide. Suitable procedures for synthesizing the peptides described herein as well as suitable chemistries for cyclizing the peptides are well known in the art.
• In various embodiments cyclization can be achieved via direct coupling of the N- and C-terminus to form a peptide (or other) bond, but can also occur via the amino acid side chains. Furthermore it can be based on the use of other functional groups, including but not limited to amino, hydroxy, sulfhydryl, halogen, sulfonyl, carboxy, and thiocarboxy. These groups can be located at the amino acid side chains or be attached to their N- or C-terminus.
• Accordingly, it is to be understood that the chemical linkage used to covalently cyclize the peptides of the invention need not be an amide linkage. In many instances it may be desirable to modify the N- and C-termini of the linear or non-cyclized peptide so as to provide, for example, reactive groups that may be cyclized under mild reaction conditions. Such linkages include, by way of example and not limitation amide, ester, thioester, CH₂—NH, etc. Techniques and reagents for synthesizing peptides having modified termini and chemistries suitable for cyclizing such modified peptides are well-known in the art.
• Alternatively, in instances where the ends of the peptide are conformationally or otherwise constrained so as to make cyclization difficult, it may be desirable to attach linkers to the N- and/or C-termini to facilitate peptide cyclization. Of course, it will be appreciated that such linkers will bear reactive groups capable of forming covalent bonds with the termini of the peptide. Suitable linkers and chemistries are well-known in the art and include those previously described.
• Cyclic peptides and depsipeptides (heterodetic peptides that include ester (depside) bonds as part of their backbone) have been well characterized and show a wide spectrum of biological activity. The reduction in conformational freedom brought about by cyclization often results in higher receptor-binding affinities. Frequently in these cyclic compounds, extra conformational restrictions are also built in, such as the use of D- and N-alkylated-amino acids, α,β-dehydro amino acids or α,α-disubstituted amino acid residues.
• Methods of forming disulfide linkages in peptides are well known to those of skill in the art (see, e.g., Eichler and Houghten (1997) Protein Pept. Lett. 4: 157-164). Reference may also be made to Marlowe (1993) Biorg. Med. Chem. Lett. 3: 437-44 who describes peptide cyclization on TFA resin using trimethylsilyl (TMSE) ester as an orthogonal protecting group; Pallin and Tam (1995) J. Chem. Soc. Chem. Comm. 2021-2022) who describe the cyclization of unprotected peptides in aqueous solution by oxime formation; Algin et al. (1994) Tetrahedron Lett. 35: 9633-9636 who disclose solid-phase synthesis of head-to-tail cyclic peptides via lysine side-chain anchoring; Kates et al. (1993) Tetrahedron Lett. 34: 1549-1552 who describe the production of head-to-tail cyclic peptides by three-dimensional solid phase strategy; Tumelty et al. (1994) J. Chem. Soc. Chem. Comm. 1067-1068, who describe the synthesis of cyclic peptides from an immobilized activated intermediate, where activation of the immobilized peptide is carried out with N-protecting group intact and subsequent removal leading to cyclization; McMurray et al. (1994) Peptide Res. 7: 195-206) who disclose head-to-tail cyclization of peptides attached to insoluble supports by means of the side chains of aspartic and glutamic acid; Hruby et al. (1994) Reactive Polymers 22: 231-241) who teach an alternate method for cyclizing peptides via solid supports; and Schmidt and Langer (1997) J. Peptide Res. 49: 67-73, who disclose a method for synthesizing cyclotetrapeptides and cyclopentapeptides.
• These methods of peptide cyclization are illustrative and non-limiting. Using the teaching provide herein, other cyclization methods will be available to one of skill in the art.
• H) Identification/Verification of Active Peptides
• The active AMPs, STAMPs and the like can be identified and/or validated using an in vitro screening assay. Indeed, in many instances the AMPs and/or STAMPS described herein will be used in vitro as preservatives, topical antimicrobial treatments, and the like. Additionally, despite certain apparent limitations of in vitro susceptibility tests, clinical data indicate that a good correlation exists between minimal inhibitory concentration (MIC) test results and in vivo efficacy of antibiotic compounds (see, e.g., Murray et al. (1994) Antimicrobial Susceptibility Testing, Poupard et al., eds., Plenum Press, New York; Knudsen et al. (1995) Antimicrob. Agents Chemother. 39(6): 1253-1258; and the like). Thus, AMPs useful for treating infections and diseases related thereto are also conveniently identified by demonstrated in vitro antimicrobial activity against specified microbial targets, e.g., as illustrated in Table 4).
• Typically, the in vitro antimicrobial activity of antimicrobial agents is tested using standard NCCLS bacterial inhibition assays, or MIC tests (see, National Committee on Clinical Laboratory Standards “Performance Standards for Antimicrobial Susceptibility Testing,” NCCLS Document M100-S5 Vol. 14, No. 16, December 1994; “Methods for dilution antimicrobial susceptibility test for bacteria that grow aerobically-Third Edition,” Approved Standard M7-A3, National Committee for Clinical Standards, Villanova, Pa.).
• It will be appreciated that other assays as are well known in the art or that will become apparent to those having skill in the art upon review of this disclosure may also be used to identify active AMPs. Such assays include, for example, the assay described in Lehrer et al. (1988) J. Immunol. Meth., 108: 153 and Steinberg and Lehrer, “Designer Assays for Antimicrobial Peptides: Disputing the ‘One Size Fits All’ Theory,” In: Antibacterial Peptide Protocols, Shafer, Ed., Humana Press, N.J. Generally, active peptides of the invention will exhibit MICs (as measured using the assays described in the examples) of less than about 100 preferably less than about 80 or 60 more preferably about 50 μM or less, about 25 μM or less, or about 15 μM or less, or about 10 μM or less.
IV. Administration and Formulations.
• A) Pharmaceutical Formulations.
• In certain embodiments, the antimicrobial peptides and/or the chimeric constructs (e.g., targeting moieties attached to antimicrobial peptide(s), targeting moieties attached to detectable label(s), etc.) are administered to a mammal in need thereof, to a cell, to a tissue, to a composition (e.g., a food), etc.). In various embodiments the compositions can be administered to detect and/or locate, and/or quantify the presence of particular microorganisms, microorganism populations, biofilms comprising particular microorganisms, and the like. In various embodiments the compositions can be administered to inhibit particular microorganisms, microorganism populations, biofilms comprising particular microorganisms, and the like.
• These active agents (antimicrobial peptides and/or chimeric moieties) can be administered in the “native” form or, if desired, in the form of salts, esters, amides, prodrugs, derivatives, and the like, provided the salt, ester, amide, prodrug or derivative is suitable pharmacologically, i.e., effective in the present method(s). Salts, esters, amides, prodrugs and other derivatives of the active agents can be prepared using standard procedures known to those skilled in the art of synthetic organic chemistry and described, for example, by March (1992) Advanced Organic Chemistry; Reactions, Mechanisms and Structure, 4th Ed. N.Y. Wiley-Interscience.
• Methods of formulating such derivatives are known to those of skill in the art. For example, the disulfide salts of a number of delivery agents are described in PCT Publication WO 2000/059863 which is incorporated herein by reference. Similarly, acid salts of therapeutic peptides, peptoids, or other mimetics, and can be prepared from the free base using conventional methodology that typically involves reaction with a suitable acid. Generally, the base form of the drug is dissolved in a polar organic solvent such as methanol or ethanol and the acid is added thereto. The resulting salt either precipitates or can be brought out of solution by addition of a less polar solvent. Suitable acids for preparing acid addition salts include, but are not limited to both organic acids, e.g., acetic acid, propionic acid, glycolic acid, pyruvic acid, oxalic acid, malic acid, malonic acid, succinic acid, maleic acid, fumaric acid, tartaric acid, citric acid, benzoic acid, cinnamic acid, mandelic acid, methanesulfonic acid, ethanesulfonic acid, p-toluenesulfonic acid, salicylic acid, and the like, as well as inorganic acids, e.g., hydrochloric acid, hydrobromic acid, sulfuric acid, nitric acid, phosphoric acid, and the like. An acid addition salt can be reconverted to the free base by treatment with a suitable base. Certain particularly preferred acid addition salts of the active agents herein include halide salts, such as may be prepared using hydrochloric or hydrobromic acids. Conversely, preparation of basic salts of the active agents of this invention are prepared in a similar manner using a pharmaceutically acceptable base such as sodium hydroxide, potassium hydroxide, ammonium hydroxide, calcium hydroxide, trimethylamine, or the like. In certain embodiments basic salts include alkali metal salts, e.g., the sodium salt, and copper salts.
• For the preparation of salt forms of basic drugs, the pKa of the counterion is preferably at least about 2 pH lower than the pKa of the drug. Similarly, for the preparation of salt forms of acidic drugs, the pKa of the counterion is preferably at least about 2 pH higher than the pKa of the drug. This permists the counterion to bring the solution's pH to a level lower than the pHmax to reach the salt plateau, at which the solubility of salt prevails over the solubility of free acid or base. The generalized rule of difference in pKa units of the ionizable group in the active pharmaceutical ingredient (API) and in the acid or base is meant to make the proton transfer energetically favorable. When the pKa of the API and counterion are not significantly different, a solid complex may form but may rapidly disproportionate (i.e., break down into the individual entities of drug and counterion) in an aqueous environment.
• Preferably, the counterion is a pharmaceutically acceptable counterion. Suitable anionic salt forms include, but are not limited to acetate, benzoate, benzylate, bitartrate, bromide, carbonate, chloride, citrate, edetate, edisylate, estolate, fumarate, gluceptate, gluconate, hydrobromide, hydrochloride, iodide, lactate, lactobionate, malate, maleate, mandelate, mesylate, methyl bromide, methyl sulfate, mucate, napsylate, nitrate, pamoate (embonate), phosphate and diphosphate, salicylate and disalicylate, stearate, succinate, sulfate, tartrate, tosylate, triethiodide, valerate, and the like, while suitable cationic salt forms include, but are not limited to aluminum, benzathine, calcium, ethylene diamine, lysine, magnesium, meglumine, potassium, procaine, sodium, tromethamine, zinc, and the like.
• In various embodiments preparation of esters typically involves functionalization of hydroxyl and/or carboxyl groups that are present within the molecular structure of the active agent. In certain embodiments, the esters are typically acyl-substituted derivatives of free alcohol groups, i.e., moieties that are derived from carboxylic acids of the formula RCOOH where R is alky, and preferably is lower alkyl. Esters can be reconverted to the free acids, if desired, by using conventional hydrogenolysis or hydrolysis procedures.
• Amides can also be prepared using techniques known to those skilled in the art or described in the pertinent literature. For example, amides may be prepared from esters, using suitable amine reactants, or they may be prepared from an anhydride or an acid chloride by reaction with ammonia or a lower alkyl amine.
• In various embodiments, the active agents identified herein are useful for parenteral, topical, oral, nasal (or otherwise inhaled), rectal, or local administration, such as by aerosol or transdermally, for detection and/or quantification, and or localization, and/or prophylactic and/or therapeutic treatment of infection (e.g., microbial infection). The compositions can be administered in a variety of unit dosage forms depending upon the method of administration. Suitable unit dosage forms, include, but are not limited to powders, tablets, pills, capsules, lozenges, suppositories, patches, nasal sprays, injectables, implantable sustained-release formulations, lipid complexes, etc.
• The active agents (e.g., antimicrobial peptides and/or chimeric constructs) described herein can also be combined with a pharmaceutically acceptable carrier (excipient) to form a pharmacological composition. In certain embodiments, pharmaceutically acceptable carriers include those approved by a regulatory agency of the Federal or a state government or listed in the U.S. Pharmacopeia or other generally recognized pharmacopeia for use in/on animals, and more particularly in/on humans. A “carrier” refers to, for example, a diluent, adjuvant, excipient, auxiliary agent or vehicle with which an active agent of the present invention is administered.
• Pharmaceutically acceptable carriers can contain one or more physiologically acceptable compound(s) that act, for example, to stabilize the composition or to increase or decrease the absorption of the active agent(s). Physiologically acceptable compounds can include, for example, carbohydrates, such as glucose, sucrose, or dextrans, antioxidants, such as ascorbic acid or glutathione, chelating agents, low molecular weight proteins, protection and uptake enhancers such as lipids, compositions that reduce the clearance or hydrolysis of the active agents, or excipients or other stabilizers and/or buffers.
• Other physiologically acceptable compounds, particularly of use in the preparation of tablets, capsules, gel caps, and the like include, but are not limited to binders, diluent/fillers, disentegrants, lubricants, suspending agents, and the like.
• In certain embodiments, to manufacture an oral dosage form (e.g., a tablet), an excipient (e.g., lactose, sucrose, starch, mannitol, etc.), an optional disintegrator (e.g. calcium carbonate, carboxymethylcellulose calcium, sodium starch glycollate, crospovidone etc.), a binder (e.g. alpha-starch, gum arabic, microcrystalline cellulose, carboxymethylcellulose, polyvinylpyrrolidone, hydroxypropylcellulose, cyclodextrin, etc.), and an optional lubricant (e.g., talc, magnesium stearate, polyethylene glycol 6000, etc.), for instance, are added to the active component or components (e.g., active peptide) and the resulting composition is compressed. Where necessary the compressed product is coated, e.g., known methods for masking the taste or for enteric dissolution or sustained release. Suitable coating materials include, but are not limited to ethyl-cellulose, hydroxymethylcellulose, polyoxyethylene glycol, cellulose acetate phthalate, hydroxypropylmethylcellulose phthalate, and Eudragit (Rohm & Haas, Germany; methacrylic-acrylic copolymer).
• Other physiologically acceptable compounds include wetting agents, emulsifying agents, dispersing agents or preservatives that are particularly useful for preventing the growth or action of microorganisms. Various preservatives are well known and include, for example, phenol and ascorbic acid. One skilled in the art would appreciate that the choice of pharmaceutically acceptable carrier(s), including a physiologically acceptable compound depends, for example, on the route of administration of the active agent(s) and on the particular physio-chemical characteristics of the active agent(s).
• In certain embodiments the excipients are sterile and generally free of undesirable matter. These compositions can be sterilized by conventional, well-known sterilization techniques. For various oral dosage form excipients such as tablets and capsules sterility is not required. The USP/NF standard is usually sufficient.
• In certain therapeutic applications, the compositions of this invention are administered, e.g., topically administered or administered to the oral or nasal cavity, to a patient suffering from infection or at risk for infection or prophylactically to prevent dental caries or other pathologies of the teeth or oral mucosa characterized by microbial infection in an amount sufficient to prevent and/or cure and/or at least partially prevent or arrest the disease and/or its complications. An amount adequate to accomplish this is defined as a “therapeutically effective dose.” Amounts effective for this use will depend upon the severity of the disease and the general state of the patient's health. Single or multiple administrations of the compositions may be administered depending on the dosage and frequency as required and tolerated by the patient. In any event, the composition should provide a sufficient quantity of the active agents of the formulations of this invention to effectively treat (ameliorate one or more symptoms in) the patient.
• The concentration of active agent(s) can vary widely, and will be selected primarily based on activity of the active ingredient(s), body weight and the like in accordance with the particular mode of administration selected and the patient's needs. Concentrations, however, will typically be selected to provide dosages ranging from about 0.1 or 1 mg/kg/day to about 50 mg/kg/day and sometimes higher. Typical dosages range from about 3 mg/kg/day to about 3.5 mg/kg/day, preferably from about 3.5 mg/kg/day to about 7.2 mg/kg/day, more preferably from about 7.2 mg/kg/day to about 11.0 mg/kg/day, and most preferably from about 11.0 mg/kg/day to about 15.0 mg/kg/day. In certain preferred embodiments, dosages range from about 10 mg/kg/day to about 50 mg/kg/day. In certain embodiments, dosages range from about 20 mg to about 50 mg given orally twice daily. It will be appreciated that such dosages may be varied to optimize a therapeutic and/or phophylactic regimen in a particular subject or group of subjects.
• In certain embodiments, the active agents of this invention are administered to the oral cavity. This is readily accomplished by the use of lozenges, aersol sprays, mouthwash, coated swabs, and the like.
• In certain embodiments, the active agent(s) of this invention are administered topically, e.g., to the skin surface, to a topical lesion or wound, to a surgical site, and the like.
• In certain embodiments the active agents of this invention are administered systemically (e.g., orally, or as an injectable) in accordance with standard methods well known to those of skill in the art. In other preferred embodiments, the agents, can also be delivered through the skin using conventional transdermal drug delivery systems, i.e., transdermal “patches” wherein the active agent(s) are typically contained within a laminated structure that serves as a drug delivery device to be affixed to the skin. In such a structure, the drug composition is typically contained in a layer, or “reservoir,” underlying an upper backing layer. It will be appreciated that the term “reservoir” in this context refers to a quantity of “active ingredient(s)” that is ultimately available for delivery to the surface of the skin. Thus, for example, the “reservoir” may include the active ingredient(s) in an adhesive on a backing layer of the patch, or in any of a variety of different matrix formulations known to those of skill in the art. The patch may contain a single reservoir, or it may contain multiple reservoirs.
• In one embodiment, the reservoir comprises a polymeric matrix of a pharmaceutically acceptable contact adhesive material that serves to affix the system to the skin during drug delivery. Examples of suitable skin contact adhesive materials include, but are not limited to, polyethylenes, polysiloxanes, polyisobutylenes, polyacrylates, polyurethanes, and the like. Alternatively, the drug-containing reservoir and skin contact adhesive are present as separate and distinct layers, with the adhesive underlying the reservoir which, in this case, may be either a polymeric matrix as described above, or it may be a liquid or hydrogel reservoir, or may take some other form. The backing layer in these laminates, which serves as the upper surface of the device, preferably functions as a primary structural element of the “patch” and provides the device with much of its flexibility. The material selected for the backing layer is preferably substantially impermeable to the active agent(s) and any other materials that are present.
• Other formulations for topical delivery include, but are not limited to, ointments, gels, sprays, fluids, and creams. Ointments are semisolid preparations that are typically based on petrolatum or other petroleum derivatives. Creams containing the selected active agent are typically viscous liquid or semisolid emulsions, often either oil-in-water or water-in-oil. Cream bases are typically water-washable, and contain an oil phase, an emulsifier and an aqueous phase. The oil phase, also sometimes called the “internal” phase, is generally comprised of petrolatum and a fatty alcohol such as cetyl or stearyl alcohol; the aqueous phase usually, although not necessarily, exceeds the oil phase in volume, and generally contains a humectant. The emulsifier in a cream formulation is generally a nonionic, anionic, cationic or amphoteric surfactant. The specific ointment or cream base to be used, as will be appreciated by those skilled in the art, is one that will provide for optimum drug delivery. As with other carriers or vehicles, an ointment base should be inert, stable, nonirritating and nonsensitizing.
• As indicated above, various buccal, and sublingual formulations are also contemplated.
• In certain embodiments, one or more active agents of the present invention can be provided as a “concentrate”, e.g., in a storage container (e.g., in a premeasured volume) ready for dilution, or in a soluble capsule ready for addition to a volume of water, alcohol, hydrogen peroxide, or other diluent.
• While the invention is described with respect to use in humans, it is also suitable for animal, e.g., veterinary use. Thus certain preferred organisms include, but are not limited to humans, non-human primates, canines, equines, felines, porcines, ungulates, largomorphs, and the like.
• B) Nanoemulsion Formulations.
• In certain embodiments the targeting peptides, antimicrobial peptides and/or chimeric moieties (e.g., STAMPs) as described herein are formulated in a nanoemulsion. Nanoemulsions include, but are not limited to oil in water (O/W) nanoemulsions, and water in oil (W/O) nanoemulsions. Nanoemulsions can be defined as emulsions with mean droplet diameters ranging from about 20 to about 1000 nm. Usually, the average droplet size is between about 20 nm or 50 nm and about 500 nm. The terms sub-micron emulsion (SME) and mini-emulsion are used as synonyms.
• Illustrative oil in water (O/W) nanoemulsions include, but are not limited to:
• Surfactant micelles—micelles composed of small molecules surfactants or detergents (e.g., SDS/PBS/2-propanol) which are suitable for predominantly hydrophobic peptides.
• Polymer micelles—micelles composed of polymer, copolymer, or block copolymer surfactants (e.g., Pluronic L64/PBS/2-propanol) which are suitable for predominantly hydrophobic peptides;
• Blended micelles: micelles in which there is more than one surfactant component or in which one of the liquid phases (generally an alcohol or fatty acid compound) participates in the formation of the micelle (e.g., Octanoic acid/PBS/EtOH) which are suitable for predominantly hydrophobic peptides;
• Integral peptide micelles—blended micelles in which the peptide serves as an auxiliary surfactant, forming an integral part of the micelle (e.g., amphipathic peptide/PBS/mineral oil) which are suitable for amphipathic peptides; and
• Pickering (solid phase) emulsions—emulsions in which the peptides are associated with the exterior of a solid nanoparticle (e.g., polystyrene nanoparticles/PBS/no oil phase) which are suitable for amphipathic peptides.
• Illustrative water in oil (W/O) nanoemulsions include, but are not limited to:
• Surfactant micelles—micelles composed of small molecules surfactants or detergents (e.g., dioctyl sulfosuccinate/PBS/2-propanol, Isopropylmyristate/PBS/2-propanol, etc.) which are suitable for predominantly hydrophilic peptides;
• Polymer micelles—micelles composed of polymer, copolymer, or block copolymer surfactants (e.g., PLURONIC® L121/PBS/2-propanol), which are suitable for predominantly hydrophilic peptides;
• Blended micelles—micelles in which there is more than one surfactant component or in which one of the liquid phases (generally an alcohol or fatty acid compound) participates in the formation of the micelle (e.g., capric/caprylic diglyceride/PBS/EtOH) which are suitable for predominantly hydrophilic peptides;
• Integral peptide micelles—blended micelles in which the peptide serves as an auxiliary surfactant, forming an integral part of the micelle (e.g., amphipathic peptide/PBS/polypropylene glycol) which are suitable for amphipathic peptides; and
• Pickering (solid phase) emulsions—emulsions in which the peptides are associated with the exterior of a solid nanoparticle (e.g., chitosan nanoparticles/no aqueous phase/mineral oil) which are suitable for amphipathic peptides.
• As indicated above, in certain embodiments the nanoemulsions comprise one or more surfactants or detergents. In some embodiments the surfactant is a non-anionic detergent (e.g., a polysorbate surfactant, a polyoxyethylene ether, etc.). Surfactants that find use in the present invention include, but are not limited to surfactants such as the TWEEN®, TRITON®, and TYLOXAPOL® families of compounds.
• In certain embodiments the emulsions further comprise one or more cationic halogen containing compounds, including but not limited to, cetylpyridinium chloride. In still further embodiments, the compositions further comprise one or more compounds that increase the interaction (“interaction enhancers”) of the composition with microorganisms (e.g., chelating agents like ethylenediaminetetraacetic acid, or ethylenebis(oxyethylenenitrilo)tetraacetic acid in a buffer).
• In some embodiments, the nanoemulsion further comprises an emulsifying agent to aid in the formation of the emulsion. Emulsifying agents include compounds that aggregate at the oil/water interface to form a kind of continuous membrane that prevents direct contact between two adjacent droplets. Certain embodiments of the present invention feature oil-in-water emulsion compositions that may readily be diluted with water to a desired concentration without impairing their anti-pathogenic properties.
• In addition to discrete oil droplets dispersed in an aqueous phase, certain oil-in-water emulsions can also contain other lipid structures, such as small lipid vesicles (e.g., lipid spheres that often consist of several substantially concentric lipid bilayers separated from each other by layers of aqueous phase), micelles (e.g., amphiphilic molecules in small clusters of 50-200 molecules arranged so that the polar head groups face outward toward the aqueous phase and the apolar tails are sequestered inward away from the aqueous phase), or lamellar phases (lipid dispersions in which each particle consists of parallel amphiphilic bilayers separated by thin films of water).
• These lipid structures are formed as a result of hydrophobic forces that drive apolar residues (e.g., long hydrocarbon chains) away from water. The above lipid preparations can generally be described as surfactant lipid preparations (SLPs). SLPs are minimally toxic to mucous membranes and are believed to be metabolized within the small intestine (see e.g., Hamouda et al., (1998) J. Infect. Disease 180: 1939).
• In certain embodiments the emulsion comprises a discontinuous oil phase distributed in an aqueous phase, a first component comprising an alcohol and/or glycerol, and a second component comprising a surfactant or a halogen-containing compound. The aqueous phase can comprise any type of aqueous phase including, but not limited to, water (e.g., dionized water, distilled water, tap water) and solutions (e.g., phosphate buffered saline solution, or other buffer systems). The oil phase can comprise any type of oil including, but not limited to, plant oils (e.g., soybean oil, avocado oil, flaxseed oil, coconut oil, cottonseed oil, squalene oil, olive oil, canola oil, corn oil, rapeseed oil, safflower oil, and sunflower oil), animal oils (e.g., fish oil), flavor oil, water insoluble vitamins, mineral oil, and motor oil. In certain embodiments, the oil phase comprises 30-90 vol % of the oil-in-water emulsion (i.e., constitutes 30-90% of the total volume of the final emulsion), more preferably 50-80%.
• In certain embodiments the alcohol, when present, is ethanol.
• While the present invention is not limited by the nature of the surfactant, in some preferred embodiments, the surfactant is a polysorbate surfactant (e.g., TWEEN 20®, TWEEN 40®, TWEEN 60®, and TWEEN 80®)), a pheoxypolyethoxyethanol (e.g., TRITON® X-100, X-301, X-165, X-102, and X-200, and TYLOXAPOL®), or sodium dodecyl sulfate, and the like.
• In certain embodiments a halogen-containing component is present. the nature of the halogen-containing compound, in some preferred embodiments the halogen-containing compound comprises a chloride salt (e.g., NaCl, KCl, etc.), a cetylpyridinium halide, a cetyltrimethylammonium halide, a cetyldimethylethylammonium halide, a cetyldimethylbenzylammonium halide, a cetyltributylphosphonium halide, dodecyltrimethylammonium halides, tetradecyltrimethylammonium halides, cetylpyridinium chloride, cetyltrimethylammonium chloride, cetylbenzyldimethylammonium chloride, cetylpyridinium bromide, cetyltrimethylammonium bromide, cetyldimethylethylammonium bromide, cetyltributylphosphonium bromide, dodecyltrimethylammonium bromide, tetradecyltrimethylammonium bromide, and the like
• In certain embodiments the emulsion comprises a quaternary ammonium compound. Quaternary ammonium compounds include, but are not limited to, N-alkyldimethyl benzyl ammonium saccharinate, 1,3,5-Triazine-1,3,5(2H,4H,6H)-triethanol; 1-Decanaminium, N-decyl-N,N-dimethyl-, chloride (or) Didecyl dimethyl ammonium chloride; 2-(2-(p-(Diisobuyl)cresosxy)ethoxy)ethyl dimethyl benzyl ammonium chloride; 2-(2-(p-(Diisobutyl)phenoxy)ethoxy)ethyl dimethyl benzyl ammonium chloride; alkyl 1 or 3 benzyl-1-(2-hydroxethyl)-2-imidazolinium chloride; alkyl bis(2-hydroxyethyl)benzyl ammonium chloride; alkyl demethyl benzyl ammonium chloride; alkyl dimethyl 3,4-dichlorobenzyl ammonium chloride (100% C12); alkyl dimethyl 3,4-dichlorobenzyl ammonium chloride (50% C14, 40% C12, 10% C16); alkyl dimethyl 3,4-dichlorobenzyl ammonium chloride (55% C14, 23% C12, 20% C16); alkyl dimethyl benzyl ammonium chloride; alkyl dimethyl benzyl ammonium chloride (100% C14); alkyl dimethyl benzyl ammonium chloride (100% C16); alkyl dimethyl benzyl ammonium chloride (41% C14, 28% C12); alkyl dimethyl benzyl ammonium chloride (47% C12, 18% C14); alkyl dimethyl benzyl ammonium chloride (55% C16, 20% C14); alkyl dimethyl benzyl ammonium chloride (58% C14, 28% C16); alkyl dimethyl benzyl ammonium chloride (60% C14, 25% C12); alkyl dimethyl benzyl ammonium chloride (61% C11, 23% C14); alkyl dimethyl benzyl ammonium chloride (61% C12, 23% C14); alkyl dimethyl benzyl ammonium chloride (65% C12, 25% C14); alkyl dimethyl benzyl ammonium chloride (67% C12, 24% C14); alkyl dimethyl benzyl ammonium chloride (67% C12, 25% C14); alkyl dimethyl benzyl ammonium chloride (90% C14, 5% C12); alkyl dimethyl benzyl ammonium chloride (93% C14, 4% C12); alkyl dimethyl benzyl ammonium chloride (95% C16, 5% C18); alkyl dimethyl benzyl ammonium chloride (and) didecyl dimethyl ammonium chloride; alkyl dimethyl benzyl ammonium chloride (as in fatty acids); alkyl dimethyl benzyl ammonium chloride (C12-C16); alkyl dimethyl benzyl ammonium chloride (C12-C18); alkyl dimethyl benzyl and dialkyl dimethyl ammonium chloride; alkyl dimethyl dimethybenzyl ammonium chloride; alkyl dimethyl ethyl ammonium bromide (90% C14, 5% C16, 5% C12); alkyl dimethyl ethyl ammonium bromide (mixed alkyl and alkenyl groups as in the fatty acids of soybean oil); alkyl dimethyl ethylbenzyl ammonium chloride; alkyl dimethyl ethylbenzyl ammonium chloride (60% C14); alkyl dimethyl isoproylbenzyl ammonium chloride (50% C12, 30% C14, 17% C16, 3% C18); alkyl trimethyl ammonium chloride (58% C18, 40% C16, 1% C14, 1% C12); alkyl trimethyl ammonium chloride (90% C18, 10% C16); alkyldimethyl(ethylbenzyl) ammonium chloride (C12-18); Di-(C8-10)-alkyl dimethyl ammonium chlorides; dialkyl dimethyl ammonium chloride; dialkyl dimethyl ammonium chloride; dialkyl dimethyl ammonium chloride; dialkyl methyl benzyl ammonium chloride; didecyl dimethyl ammonium chloride; diisodecyl dimethyl ammonium chloride; dioctyl dimethyl ammonium chloride; dodecyl bis(2-hydroxyethyl) octyl hydrogen ammonium chloride; dodecyl dimethyl benzyl ammonium chloride; dodecylcarbamoyl methyl dimethyl benzyl ammonium chloride; heptadecyl hydroxyethylimidazolinium chloride; hexahydro-1,3,5-thris(2-hydroxyethyl)-s-triazine; myristalkonium chloride (and) Quat RNIUM 14; N,N-Dimethyl-2-hydroxypropylammonium chloride polymer; n-alkyl dimethyl benzyl ammonium chloride; n-alkyl dimethyl ethylbenzyl ammonium chloride; n-tetradecyl dimethyl benzyl ammonium chloride monohydrate; octyl decyl dimethyl ammonium chloride; octyl dodecyl dimethyl ammonium chloride; octyphenoxyethoxyethyl dimethyl benzyl ammonium chloride; oxydiethylenebis (alkyl dimethyl ammonium chloride); quaternary ammonium compounds, dicoco alkyldimethyl, chloride; trimethoxysily propyl dimethyl octadecyl ammonium chloride; trimethoxysilyl quats, trimethyl dodecylbenzyl ammonium chloride; n-dodecyl dimethyl ethylbenzyl ammonium chloride; n-hexadecyl dimethyl benzyl ammonium chloride; n-tetradecyl dimethyl benzyl ammonium chloride; n-tetradecyl dimethyl ethylbenzyl ammonium chloride; and n-octadecyl dimethyl benzyl ammonium chloride.
• Nanoemulsion formulations and methods of making such are well known to those of skill in the art and described for example in U.S. Pat. Nos. 7,476,393, 7,468,402, 7,314,624, 6,998,426, 6,902,737, 6,689,371, 6,541,018, 6,464,990, 6,461,625, 6,419,946, 6,413,527, 6,375,960, 6,335,022, 6,274,150, 6,120,778, 6,039,936, 5,925,341, 5,753,241, 5,698,219, an d5,152,923 and in Fanun et al. (2009) Microemulsions: Properties and Applications (Surfactant Science), CRC Press, Boca Ratan Fl.
• C) Formulations Optimizing Activity.
• In certain embodiments, formulations are selected to optimize binding specificity, and/or binding avidity, and/or antimicrobial activity, and/or stability/conformation of the targeting peptide, antimicrobial peptide, chimeric moiety, and/or STAMP. In this regard, it was a surprising discovery that the activity of certain STAMPs, and presumably the constituent targeting peptides and/or antimicrobial peptides was optimized in the presence of a salt. Accordingly, certain embodiments are contemplated where the targeting peptide and/or antimicrobial peptide, and/or STAMP is formulated in combination with one or more salts. The formulations disclosed herein, however, are not limited to those containing salt(s). Embodiments, are also contemplated where the targeting peptide and/or antimicrobial peptide, and/or STAMP is formulated without the presence of a salt.
• In certain embodiments, sodium chloride plus a little potassium chloride resulted in the best activity of the salts tested. However, other salts, e.g., CaCl₂, MgCl₂, MnCl₂ also enhanced activity. Accordingly, in certain embodiments, it is contemplated that the targeting peptide(s), and/or antimicrobial peptide(s), and/or chimeric moieties, and/or STAMPs are formulated with one or more salts.
• In certain embodiments suitable salts include any of a number of pharmaceutically acceptable salts. Representative salts include the hydrobromide, hydrochloride, sulfate, bisulfate, phosphate, nitrate, acetate, valerate, oleate, palmitate, stearate, laurate, benzoate, lactate, phosphate, tosylate, citrate, maleate, fumarate, succinate, tartrate, napthylate, mesylate, besylate, glucoheptonate, lactobionate, and laurylsulphonate salts and the like (see, e.g., Berge et al. (1977) J. Pharm. Sci. 66: 1-19), although it is noted that citrate salts appear to inhibit the activity of certain STAMPs.
• In certain embodiments pharmaceutically acceptable salts of the present invention include the conventional nontoxic salts or quaternary ammonium salts of the compounds, e.g., from non-toxic organic or inorganic acids. For example, such conventional nontoxic salts include those derived from inorganic acids such as hydrochloride, hydrobromic, sulfuric, sulfamic, phosphoric, nitric, and the like; and the salts prepared from organic acids such as acetic, propionic, succinic, glycolic, stearic, lactic, malic, tartaric, citric, ascorbic, palmitic, maleic, hydroxymaleic, phenylacetic, glutamic, benzoic, salicyclic, sulfanilic, 2-acetoxybenzoic, fumaric, toluenesulfonic, methanesulfonic, benzenesulfonic, ethane disulfonic, oxalic, isothionic, and the like.
• In other cases, the compounds of the present invention may contain one or more acidic functional groups and, thus, are capable of forming pharmaceutically-acceptable salts with pharmaceutically-acceptable bases. The term “pharmaceutically-acceptable salts” in these instances refers to the relatively non-toxic, inorganic and organic base addition salts of compounds of the present invention. These salts can likewise be prepared in situ in the administration vehicle or the dosage form manufacturing process, or by separately treating the compound in its free acid form with a suitable base, such as the hydroxide, carbonate or bicarbonate of a pharmaceutically-acceptable metal cation, with ammonia, or with a pharmaceutically-acceptable organic primary, secondary or tertiary amine. Representative alkali or alkaline earth salts include the lithium, sodium, potassium, calcium, magnesium, and aluminum salts and the like. Representative organic amines useful for the formation of base addition salts include ethylamine, diethylamine, ethylenediamine, ethanolamine, diethanolamine, piperazine and the like (see, for example, Berge et al., supra; and Stahl and Wermuth (2002) Handbook of Pharmaceutical Salts: Properties, Selection, and Use, Wiley-VCH, Zurich, Switzerland).
• In various embodiments, the salt is simply a sodium chloride and/or a potassium chloride and can readily be prepared, for example, as a phosphate buffered saline (PBS) solution. In certain embodiments, the salt concentration is comparable to that found in 0.5×PBS to about 2.5×PBS, more preferably from about 0.5×PBS to about 1.5×PBS. In certain embodiments optimum activity has been observed in 1×PBS.
• In various embodiments, the pH of the formulation ranges from about pH 5.0 to about pH 8.5, preferably from about pH 6.0 to about pH 8.0, more preferably from about pH 7.0 to about pH 8.0. In certain embodiments the pH is about pH 7.4.
• While optimum results have been observed for certain STAMPS using a PBS buffer system, other buffer systems are also acceptable. Such buffers include, but are not limited to sulfate buffers, carbonate buffers, Tris buffers, CHAPS buffers, PIPES buffers, and the like, as long as the salt is included.
• In various embodiments, the targeting peptide, and/or antimicrobial peptide, and/or chimeric moiety, and/or STAMP is present in the formulation at a concentration ranging from about 1 nM, to about 1, 10, or 100 mM, more preferably from about 1 nM, about 10 nM, about 100 nM, about 1 or about 10 μM to about 50 about 100 about 200 μm, about 300 about 400 or about 500 preferably from about 1 about 10 about 25 or about 50 μM to about 1 mM, about 10 mM, about 20 mM, or about 5 mM, most preferably from about 10 about 20 or about 50 μM to about 100 μM, about 150 μM, or about 200 μM.
• D) Home Health Care/Hygiene Product Formulations.
• In certain embodiments, one or more of the targeting peptide(s), and/or antimicrobial peptides (AMPs) and/or chimeric moieties, and/or STAMPS described herein are incorporated into healthcare formulations, e.g., for home use. Such formulations include, but are not limited to toothpaste, mouthwash, tooth whitening strips or solutions, contact lens storage, wetting, or cleaning solutions, dental floss, toothpicks, toothbrush bristles, oral sprays, oral lozenges, nasal sprays, aerosolizers for oral and/or nasal application, wound dressings (e.g., bandages), and the like.
• For example, chimeric moieties and/or STAMPs, and/or AMPs directed against S. mutans are well suited for inhibiting frequency or severity of dental caries formation, plaque formation, periodontal disease, and/or halitosis.
• Chimeric moieties and/or STAMPs, and/or AMPs directed against Corynebacterium spp, when applied to a skin surface can reduce/eliminate Corynebacterium resulting in a reduction of odors. Such moieties are readily incorporated in soaps, antibiotics, antiseptics, disinfectants, and the like.
• The formulation of such health products is well known to those of skill, and the antimicrobial peptides and/or chimeric constructs are simply added to such formulations in an effective dose (e.g., a prophylactic dose to inhibit dental carie formation, etc.).
• For example, toothpaste formulations are well known to those of skill in the art. Typically such formulations are mixtures of abrasives and surfactants; anticaries agents, such as fluoride; tartar control ingredients, such as tetrasodium pyrophosphate and methyl vinyl ether/maleic anhydride copolymer; pH buffers; humectants, to prevent dry-out and increase the pleasant mouth feel; and binders, to provide consistency and shape (see, e.g., Table 17). Binders keep the solid phase properly suspended in the liquid phase to prevent separation of the liquid phase out of the toothpaste. They also provide body to the dentifrice, especially after extrusion from the tube onto the toothbrush.

• TABLE 17
  Typical components of toothpaste.

  	Ingredients	Wt %
  	Humectants	40-70
  	Water	0-50
  	Buffers/salts/tartar	0.5-10
  	control
  	Organic thickeners	0.4-2
  	(gums)
  	Inorganic thickeners	0-12
  	Abrasives	10-50
  	Actives (e.g., triclosan)	0.2-1.5
  	Surfactants	0.5-2
  	Flavor and sweetener	0.8-1.5

  
  Fluoride sources provide 1000-15000 ppm fluorine.
• Table 18 lists typical ingredients used in formulations; the final combination will depend on factors such as ingredient compatibility and cost, local customs, and desired benefits and quality to be delivered in the product. It will be recognized that one or more antimicrobial peptides and/or chimeric constructs described herein can simply be added to such formulations or used in place of one or more of the other ingredients.

• TABLE 18
  List of typical ingredients.

  					Tartar
  	Inorganic				Control
  Gums	Thickeners	Abrasives	Surfactants	Humectants	Ingredient
  Sodium	Silica	Hydrated	Sodium	Glycerine	Tetrasodium
  carboxymethyl	thickeners	silica	lauryl sulfate		pyrophosphate
  cellulose
  Cellulose ethers	Sodium	Dicalcium	Sodium N-	Sorbitol	Gantrez S-70
  	aluminum	phosphate	lauryl
  	silicates	digydrate	sarcosinate
  Xanthan Gum	Clays	Calcium	Pluronics	Propylene	Sodium tri-
  		carbonate		glycol	polyphosphate
  Carrageenans		Sodium		Xylitol
  		bicarbonate
  Sodium alginate		Calcium	Sodium	Polyethylene
  		pyrophosphate	lauryl	glycol
  			sulfoacetate
  Carbopols		Alumina

• One illustrative formulation described in U.S. Pat. No. 6,113,887 comprises (1) a water-soluble bactericide selected from the group consisting of pyridinium compounds, quaternary ammonium compounds and biguanide compounds in an amount of 0.001% to 5.0% by weight, based on the total weight of the composition; (2) a cationically-modified hydroxyethylcellulose having an average molecular weight of 1,000,000 or higher in the hydroxyethylcellulose portion thereof and having a cationization degree of 0.05 to 0.5 mol/glucose in an amount of 0.5% to 5.0% by weight, based on the total weight of the composition; (3) a surfactant selected from the group consisting of polyoxyethylene polyoxypropylene block copolymers and alkylolamide compounds in an amount of 0.5% to 13% by weight, based on the total weight of the composition; and (4) a polishing agent of the non-silica type in an amount of 5% to 50% by weight, based on the total weight of the composition. In certain embodiments, the antimicrobial peptide(s) and/or chimeric construct(s) described herein can be used in place of the bactericide or in combination with the bactericide.
• Similarly, mouthwash formulations are also well known to those of skill in the art. Thus, for example, mouthwashes containing sodium fluoride are disclosed in U.S. Pat. Nos. 2,913,373, 3,975,514, and 4,548,809, and in US Patent Publications US 2003/0124068 A1, US 2007/0154410 A1, and the like. Mouthwashes containing various alkali metal compounds are also known: sodium benzoate (WO 9409752); alkali metal hypohalite (US 20020114851A1); chlorine dioxide (CN 1222345); alkali metal phosphate (US 2001/0002252 A1, US 2003/0007937 A1); hydrogen sulfate/carbonate (JP 8113519); cetylpyridium chloride (CPC) (see, e.g., U.S. Pat. No. 6,117,417, U.S. Pat. No. 5,948,390, and JP 2004051511). Mouthwashes containing higher alcohol (see, e.g., US 2002/0064505 A1, US 2003/0175216 A1); hydrogen peroxide (see, e.g., CN 1385145); CO₂ gas bubbles (see, e.g., JP 1275521 and JP 2157215) are also known. In certain embodiments, these and other mouthwash formulations can further comprise one or more of the AMPs or compound AMPs of this invention.
• Contact lens storage, wetting, or cleaning solutions, dental floss, toothpicks, toothbrush bristles, oral sprays, oral lozenges, nasal sprays, and aerosolizers for oral and/or nasal application, and the like are also well known to those of skill in the art and can readily be adapted to incorporate one or more antimicrobial peptide(s) and/or chimeric construct(s) described herein.
• The foregoing pharmaceutical and/or home healthcare formulations and/or devices are meant to be illustrative and not limiting. Using teaching provided herein, the antimicrobial peptide(s) and/or chimeric construct(s) described herein can readily be incorporated into other products.
• E) Illustrative Oral Care Formulations.
• The targeting peptide(s), and/or antimicrobial peptide(s), and/or chimeric moieties, and/or STAMPs described herein can be used for a number of applications, e.g., as described above. In certain embodiments anti-S. mutans STAMPs, AMPs, and/or other chimeric moieties can be used to reduce the incidence or severity of dental caries, inhibit plaque formation, reduce halitosis, and the like. Accordingly, in certain embodiments, such moieties are included in devices and formulations for dental applications e.g., tea or other drinks, toothpick coatings, dental floss coatings, toothpaste, gel, mouthwash, varnish, even professional dental products.
• In certain embodiments, methods of treating or reducing the incidence, duration, or severity of periodontal disease are provided. The methods can include applying to the gingival crevice or periodontal pocket a composition comprising a targeting peptide, and/or antimicrobial peptide, and/or STAMP, and/or other chimeric moiety as described herein with a carrier/stabilizing agent. In the composition applied, the carrier/stabilizing agent can provide retention, tissue penetration, deposition and sustained release of the active agent (e.g., STAMP) for reducing the population of specific bacterial species within a periodontal biofilm and associated tissues. In certain embodiments, the carrier agent provides penetration and retention into the gingival crevice or periodontal pocket and associated tissues with sustained release of the active agent to enhance the reduction in population of select bacteria within the gingival tissue and dentinal tubule tissue.
• In various embodiments, carrier agents can include, but are not limited to polylactide, polyglycolide, polylactide-co-glycolide, polycaprolactone, cellulosic-based polymers, ethylene glycol polymers and its copolymers, oxyethylene polymers, polyvinyl alcohol, chitosan and hyaluronan and its copolymers. In an aspect, the carrier agents include hydroxyethyl cellulose, hydroxypropyl cellulose, hydroxypropylmethyl cellulose, hydroxymethyl cellulose, polyvinyl alcohol, polyethylene glycol, polyethylene oxide, ethylene oxide-propylene oxide co-polymers, chitosan, hyaluronan and its copolymers, or combinations thereof. In another aspect, the carrier agents include hyaluronan or hyaluronic acid and copolymers including salts of hyaluronic acid, esters of hyaluronic acid, cross-linked gels of hyaluronic acid, enzymatic derivatives of hyaluronic acid, chemically modified derivatives of hyaluronic acid or combinations thereof. As used herein, hyaluronic acid broadly refers to naturally occurring, microbial and synthetic derivatives of acidic polysaccharides of various molecular weights constituted by residues of D-glucuronic acid polysaccharides and N-acetyl-D-glucosamine.
• In certain embodiments, the active agent (e.g., STAMP, AMP, etc.) and the carrier agent are in the form of an admixture, in the form of a complex, covalently coupled, or a combination thereof. In certain embodiments, the carrier agent comprises a bioadhesive. Suitable bioadhesive carrier agents include, but are not limited to a cellulose based polymer and/or a dextrin. Suitable cellulose based polymers include, but are not limited to hydroxyethyl cellulose, hydroxypropyl cellulose, hydroxymethyl cellulose, or a mixture thereof. In one illustrative embodiment, the bioadhesive carrier agent includes polylactide, polyglycolide, polylactide-co-glycolide, polyethylene glycol, hyaluronan, hyaluronic acid, chitosan, or a mixture thereof. In certain embodiments the bioadhesive carrier agent can include a copolymer comprising polyethylene glycol, hyaluronan, hyaluronic acid, chitosan, or a mixture thereof.
• In certain embodiments, the carrier agent penetrates periodontal tissues. Suitable penetrating carrier agents include, but are not limited to hyaluronic acid, a hyaluronic acid derivative, chitosan, a chitosan derivative, or a mixture thereof. In an embodiment, the penetrating carrier agent includes a salt of hyaluronic acid, an ester of hyaluronic acid, an enzymatic derivative of hyaluronic acid, a cross-linked gel of hyaluronic acid, a chemically modified derivative of hyaluronic acid, or a mixture thereof.
V. Microorganism Detection.
• As indicated above, the targeting moieties and/or STAMPs are useful in diagnostic compositions and methods to determine the presence or absence and/or to quantify the amount of one or microorganisms present in the environment, in a food stuff, in a biological sample, and the like.
• For example, targeting peptide-antimicrobial peptide conjugates (e.g. Specifically targeted antimicrobial peptides (STAMPs)) can be used as diagnostic reagents. STAMPs (and other targeted antimicrobial constructs described herein) have the ability to specifically bind to microorganisms, for example, S. mutans, and permeabilize or disrupt their membrane such that cell impermeable dyes or other reagent (propidium iodide, etc.) may enter the microorganism or intracellular molecules or contents (ATP, DNA, Calcium, etc.) of the targeted microorganism are caused to be released into the environment for analysis. In one method a STAMP, for example, C16G2, can permeabilize or disrupt the membrane of target microorganisms, for example, S. mutans, in a prepared culture or clinical sample by itself, in a biofilm in vitro or in vivo. To the sample a cell impermeable dye (e.g. propidium iodide, etc.) is added to label and allow for detection of those microorganisms targeted by the STAMP. Cell permeable dyes (e.g. SYTO9) can also be added to label and detect the entire population of microorganisms in the sample. Labeled cells can then be quantified by fluorescence microscopy, fluorometry, flow cytometry or other method.
• In another example, a STAMP treated sample is mixed with luciferase and luciferin which reacts with the ATP released from the STAMP treated cells and the resulting luminescence is used to detected and quantify targeted cells.
VI. Kits.
• In another embodiment this invention provides kits for the inhibition of an infection and/or for the treatment and/or prevention of dental caries in a mammal. The kits typically comprise a container containing one or more of the active agents (i.e., the antimicrobial peptide(s) and/or chimeric construct(s)) described herein. In certain embodiments the active agent(s) can be provided in a unit dosage formulation (e.g., suppository, tablet, caplet, patch, etc.) and/or may be optionally combined with one or more pharmaceutically acceptable excipients.
• In certain embodiments the kits comprise one or more of the home healthcare product formulations described herein (e.g., toothpaste, mouthwash, tooth whitening strips or solutions, contact lens storage, wetting, or cleaning solutions, dental floss, toothpicks, toothbrush bristles, oral sprays, oral lozenges, nasal sprays, aerosolizers for oral and/or nasal application, and the like).
• In certain embodiments kits are provided for detecting and/or locating and/or quantifying certain target microorganisms and/or cells or tissues comprising certain target microorganisms, and/or prosthesis bearing certain target microorganisms, and/or biofilms comprising certain target microorganisms. In various embodiments these kits typically comprise a chimeric moiety comprising a targeting moiety and a detectable label as described herein and/or a targeting moiety attached to an affinity tag for use in a pretargeting strategy as described herein.
• In addition, the kits optionally include labeling and/or instructional materials providing directions (i.e., protocols) for the practice of the methods or use of the “therapeutics” or “prophylactics” or detection reagents of this invention. Certain instructional materials describe the use of one or more active agent(s) of this invention to therapeutically or prophylactically to inhibit or prevent infection and/or to inhibit the formation of dental caries. The instructional materials may also, optionally, teach preferred dosages/therapeutic regiment, counter indications and the like.
• While the instructional materials typically comprise written or printed materials they are not limited to such. Any medium capable of storing such instructions and communicating them to an end user is contemplated by this invention. Such media include, but are not limited to electronic storage media (e.g., magnetic discs, tapes, cartridges, chips), optical media (e.g., CD ROM), and the like. Such media may include addresses to internet sites that provide such instructional materials.
EXAMPLES
• The following examples are offered to illustrate, but not to limit the claimed invention.
Example 1 Design and Activity of a “Dual-Targeted” Antimicrobial Peptide
• Numerous reports have indicated the important role of human normal flora in the prevention of microbial pathogenesis and disease. Evidence suggests that infections at mucosal surfaces result from the outgrowth of subpopulations or clusters within a microbial community, and are not linked to one pathogenic organism alone. In order to preserve the protective normal flora while treating the majority of infective bacteria in the community, a tunable therapeutic is necessary that can discriminate between benign bystanders and multiple pathogenic organisms. Here we describe the proof-of-principle for such a multi-targeted antimicrobial: a multiple-headed specifically-targeted antimicrobial peptide (MH-STAMP). The completed MH-STAMP, M8(KH)-20, displays specific activity against targeted organisms in vitro (Pseudomonas aeruginosa and Streptococcus mutans) and can remove both species from a mixed planktonic culture with little impact against untargeted bacteria. These results demonstrate that a functional, dual-targeted molecule can be constructed from wide-spectrum antimicrobial peptide precursor.
Introduction
• For nearly 30 years antimicrobial peptides (AMPs) have been rigorously investigated as alternatives to small molecule antibiotics and potential solutions to the growing crisis of antibiotic resistant bacterial infections (Ganz (2003) Nat Rev Immunol., 3: 710-720; Hancock and Lehrer (1998)., 16: 82-88). Numerous reports have characterized potential AMPs from natural sources, and a great body of work has been carried out designing “tailor-made” AMPs due to the approachable nature of solid-phase peptide synthesis (SPPS) (Genco et al. (2003) Int J Antimicrob Agents, 21: 75-78; He and Eckert (2007) Antimicrob Agents Chemother., 51: 1351-1358). Several examples of the latter have shown remarkable activities in vitro against fungi, Gram-positive and Gram-negative bacteria, as well as some enveloped viruses (Brogden (2005) Nat Rev Microbiol. 3: 238-250).
• Unlike small molecule antibiotics that may lose activity when their basic structures are modified even incrementally, peptides are a convenient canvas for molecular alteration. AMPs can be optimized through the incorporation of more or less hydrophobic or charged amino acids, which has been shown to affect selectivity for Gram-positive, Gram-negative or fungal membranes (Muhle and Tam J P (2001) Biochemistry, 40: 5777-5785; Tossi et al. (2000) Biopolymers 55: 4-30). Additionally, lysine residues can be utilized to improve AMP activity per μM. In this approach, multiple AMP chains can be attached to a single peptide scaffold through branching from lysine epsilon-amines (Tam et al. (2992) Eur. J. Biochem., 269: 923-932; Pini et al. (2005) Antimicrob Agents Chemother., 2005; 49: 2665-2672). AMP activity can be specifically tuned through the attachment of a targeting peptide region, as described for a novel class of molecules, the specifically-targeted antimicrobial peptides, or STAMPs (Eckert et al. (2006) Antimicrob Agents Chemother., 50: 3651-3657; Eckert et al. (2006) Antimicrob Agents Chemother., 50: 1480-1488). These chimeric molecules can consist of functionally independent targeting and killing moieties within a linear peptide sequence. A pathogenic bacterium recognized (i.e. bound) by the targeting peptide can be eliminated from a multi-species community with little impact to bystander normal flora. As an extension of this concept, we hypothesized that a STAMP could be constructed with multiple targeting peptide “heads” attached to a single AMP by utilizing a central lysine residue branch point. Potentially, targeting “heads” could be specific for the same pathogen, or have different binding profiles. Utilizing the former approach, microbial resistance evolution linked to a targeting peptide could be inhibited or reduced, as no single microbial population would have the genetic diversity necessary to mutate multiple discrete targeting peptide receptors in one cell (Drake et al. (1998) Genetics 148: 1667-1686).
• Multi-headed STAMP (MH-STAMP) molecules with differing bacterial targets may have appeal in treating poly-microbial infections, or where it may be advantageous to remove a cluster of biofilm constituents without utilizing several distinct molecules; for example in the simultaneously treatment of dental caries and periodontitis, or in the eradication of the Propionibacteria spp. and Staphylococcus spp. involved in acne and skin infections, respectively.
• In this example, we present the proof-of-principle design, synthesis and in vitro activity of such a MH-STAMP, M8(KH)-20. Previously, we identified two functional STAMP targeting domains, one with specific recognition of the cariogenic pathogen S. mutans (Eckert et al. (2006) Antimicrob Agents Chemother., 50: 3651-3657), and the other with Pseudomonas spp.-level selectivity (Eckert et al. (2006) Antimicrob Agents Chemother., 50: 3833-3838). Conjoined to a normally wide-spectrum linear AMP, we observed antimicrobial effects directed specifically to P. aeruginosa and S. mutans in vitro. Additionally, treatment of mixed bacterial communities with the multi-headed MH-STAMP resulted in the specific eradication of the target organisms with little impact on bystander population levels.
Materials and Methods
• Bacterial Strains and Growth Conditions
• P. aeruginosa ATCC 15692, Klebsiella pneumoniae KAY 2026 (Sprenger and Lengeler (1984) J Bacteriol., 157: 39-45), Escherichia coli DH5α (pFW5, spectinomycin resistance) (Podbielski et al. (1996) Gene, 177: 137-147), Staphylococcus aureus Newmann (Duthie and Lorenz (1952) J Gen Microbiol., 6: 95-107), and Staphylococcus epidermidis ATCC 35984 were cultivated under aerobic conditions at 37° C. with vigorous shaking. Aerobic Gram-negative organisms were grown in Lauri-Bertaini (LB) broth and Gram-positive bacteria in Brain-heart infusion (BHI) broth. Streptococcus mutans JM11 (spectinomycin resistant, UA140 background) was grown in Todd-Hewitt (TH) broth under anaerobic conditions (80% N2, 15% CO₂, 5% H2) at 37° C. Merritt et al. (2005) J Microbiol Meth., 61: 161-170. All bacteria were grown overnight to an OD600 of 0.8-1.0 prior to appropriate dilution and antimicrobial testing.
• Synthesis of Multi-Head STAMP Peptides
• Conventional solid-phase peptide synthesis (SPPS) methodologies were utilized for the construction of all peptides shown in FIG. 15 (Symphony Synthesizer, PTI, Tucson, Ariz.). Chemicals, amino acids, and synthesis resins were purchased from Anaspec (San Jose, Calif.). BD2.20 (FIRKFLKKWLL (SEQ ID NO:3226), amidated c-terminus, mw 1491.92), an antimicrobial peptide developed in our laboratory with robust antimicrobial activity against a number of bacterial species (Table 19), served as the root sequence to which differing targeting peptides were attached: Firstly, BD2.20 was synthesized by SPPS (Rink-Amide-MBHA resin, 0.015 mmol), followed by the stepwise coupling of a functionalized alkane (NH₂(CH₂)₇COOH), and an Fmoc-protected Lys (side-chain protected with 4-methyltrityl (Mtt)) to the N-terminus. Standard SPPS methods were then employed for the step-wise addition of the S. mutans targeting peptide M8 plus a tri-Gly linker region (TFFRFLNR-GGG (SEQ ID NO:3227)) to the N-terminal of the central Lys. After assembly of Fmoc-M8-GGG-K(Mtt)-(CH₂)₇CO-BD2.20 (SEQ ID NO:3228), the Fmoc group was removed with 25% piperidine in DMF and the N-terminal was re-protected with an acetyl group with Ac₂O/DIEA (1:1, 20 molar excess) for 2 hours. The Mtt-protected amino group of the central Lys was then selectively exposed with 2% TFA in DCM (1.5 mL) for 15 minutes (three cycles of 5 min). The resulting product was reloaded into the synthesizer and the peptide sequence built from the Lys side-chain was completed with standard Fmoc SPPS methods. As shown in FIG. 15, the completed MH-STAMP M8(KH)-20 contained the side-chain peptide KH (Pseudomonas spp.-targeting, KKHRKHRKHRKH-GGG (SEQ ID NO:3229)), while in MH-STAMP M8(BL)-20 a peptide with no bacterial binding (data not shown), BL-1 (DAANEA-GGG), was utilized. BL(KH)-20 was constructed identically to M8(KH)-20, utilizing BL-1 in place of M8 (FIG. 15).

• TABLE 19
  MICs of MH-STAMPs and component peptides.

  MIC (μM)

  	P. aeruginosa	E. coli	K. pneumoniae	S. mutans	S. epidermidis	S. aureus

  BD2.20	14.4 ± 4.40	5.47 ± 1.41	2.98 ± 0.47	2.86 ± 0.60	5.11 ± 1.58	5.625 ± 1.29
  M8(KH)-20	11.95 ± 3.32	2.72 ± 0.59	3.13	6.25	3.13	5.64 ± 1.07
  M8(BL)-20	50	5.97 ± 0.94	6.88 ± 1.98	6.25	6.25	18.05 ± 6.58
  BL(KH)-20	27.5 ± 7.90	6.25	6.25	6.25	6.25	6.25
  Average MIC with standard deviation, n = 10 assays.

• Synthesis progression was monitored by the ninhydrin test, and completed peptides cleaved from the resin with 95% TFA utilizing appropriate scavengers, and precipitated in methyl tert-butyl ether. Purification and MH-STAMP quality was confirmed by HPLC (Waters, Milford, Mass.) using a linear gradient of increasing mobile phase (acetonitrile 10 to 90% in water with 0.1% TFA) and a Waters)(Bridge BEH 130 C18 column (4.6×100 mm, particle size 5 μm). Absorbance at 215 nm was utilized as the monitoring wavelength, though 260 and 280 nm were also collected. LC spectra were analyzed with MassLynx Software v.4.1 (Waters). Matrix-assisted laser desorption ionization (MALDI) mass spectroscopy was utilized to confirm correct peptide mass (Voyager System 4291, Applied Biosystems) (Anderson et al. (2008) Biotechnol Lett., 30: 813-818).
• MIC Assay
• Peptides were evaluated for basic antimicrobial activity by broth microdilution, as described previously (Eckert et al. (2006) Antimicrob Agents Chemother., 50: 3651-3657; Eckert et al. (2006) Antimicrob Agents Chemother., 50: 1480-1488). Briefly, ˜1×105 cfu/mL bacteria were diluted in TH (S. mutans), or Mueller-Hinton (MH) broth (all other organisms) and distributed to 96-well plates. Serially-diluted (2-fold) peptides were then added and the plates incubated at 37° C. for 18-24 h. Peptide MIC was determined as the concentration of peptide that completely inhibited organism growth when examined by eye (clear well). All experiments were conducted 10 times.
• Post-Antibiotic Effect Assay
• The activity and selectivity of MH-STAMPs after a 10 min incubation was determined by growth retardation experiments against targeted and untargeted bacteria in monocultures, as described previously (Id.). Cells from overnight cultures were diluted to ˜5×106 cfu/mL in MH (or TH with 1% sucrose for S. mutans), normalized by OD600 0.05-0.1 and seeded to 96-well plates. Cultures were then grown under the appropriate conditions for 2 h (3 h for S. mutans) prior to the addition of peptides for 10 min. Plates were then centrifuged at 3000×g for 5 min, the supernatants discarded, fresh medium returned (MH or TH without sucrose for S. mutans), and incubation resumed. Bacterial growth after treatment was then monitored over time by OD600.
• Microbial Population Shift Assay
• Mixed planktonic populations of P. aeruginosa, E. coli, S. epidermidis, and S. mutans were utilized to examine the potential of MH-STAMPs to direct species composition within a culture after treatment. Samples were prepared containing: ˜6×10⁴ cfu/mL S. mutans, ˜2×10⁴ cfu/mL E. coli, ˜2×104 cfu/mL S. epidermidis, and ˜0.5×10⁴ cfu/mL P. aeruginosa in BHI (mixed immediately before peptide addition). Peptide (10 μM) or mock-treatment (1×PBS) was then added and samples were incubated at 37° C. for 24 h under anaerobic conditions (80% N₂, 15% CO₂, 5% H₂). After incubation, samples were serially diluted (1:10) in 1×PBS and aliquots from each dilution were then spotted to agar plates selective for each species in the mixture: TH plus 800 μg/mL spectinomycin (S. mutans), LB plus 25 μg/mL ampicillin (P. aeruginosa), LB plus 200 μg/mL spectinomycin (E. coli), and mannitol salt agar (MSA, S. epidermidis) in order to quantitate survivors from each species. Plates were then incubated 37° C. under aerobic conditions (TH plates were incubated anaerobically) and colonies counted after 24 h to determine survivors. Expected colony morphologies were observed for each species when plated on selective media. Gram stains and direct microscopic observation (from select isolated colonies) were undertaken to confirm species identity (data not shown). The detection limit of the assay was 200 cfu/mL.
Results
• Design and Synthesis of Multi-Headed STAMPs
• We constructed a prototype MH-STAMP from the well-established targeting peptides KH (specific to Pseudomonas spp) and M8 (specific for Streptococcus mutans). The wide-spectrum antimicrobial peptide BD2.20 was utilized as the base AMP for all MH171 STAMP construction. BD2.20 is a novel synthetic AMP with a cationic and amphipathic residue arrangement, which has robust MICs against a variety of Gram-negative and Gram-positive organisms (Table 19). For the synthesis of MH-STMAP M8(KH)-20 (construct presented in FIG. 15), BD2.20 and a Lys (Mtt-protected side-chain) residue were joined via an activated alkane spacer, followed by addition of the M8 targeting peptide to the N-terminus of the product. Selective deprotection of the central Lys(Mtt) side chain was then undertaken and the KH targeting peptide attached. The correct molecular mass (4888.79) and ˜90% purity was confirmed by HPLC and MALDI mass spectrometry (FIG. 16).
• The non-binding “blank” targeting peptide BL-1 was incorporated into the synthesis scheme in place of KH or M8 to construct variant MH-STAMPs possessing a single functional targeting head: M8(BL)-20 and BL(KH)-20. The correct MW and acceptable purity were observed for these MH-STAMPs (FIG. 15, data not shown).
• General Antimicrobial Activity of Multi-Head Constructs
• After synthesis, the completed MH-STAMPs were evaluated for general antimicrobial activity by MIC against a panel of bacteria. As shown in Table 19, the MH-STAMP constructs M8(KH)-20, BL(KH)-20, and M8(BL)-20 were found to have similar activity profiles to that of BD2.20 for the organisms examined (less than two titration steps in 10-fold difference). Additionally, we observed a difference in general susceptibility between P. aeruginosa and the other organisms tested, suggesting this bacterium is more resistant to BD2.20. Overall, these data indicate that the addition of the targeting domains to the base sequence was tolerated and did not completely inhibit the activity of the antimicrobial peptide.
• Peptide selectivity could not be determined utilizing these methods, as STAMPs and their parent AMP molecules often display similar MICs, but have radically different antimicrobial kinetics and selectivity due to increased specific-killing mediated by the targeting regions (Id.). Therefore, we performed different experiments to test for antimicrobial selectivity and functional MH-STAMP construction.
• Selectivity and Post-Antibiotic Effect of MH-STAMP Constructs
• MH-STAMP antimicrobial kinetics was ascertained utilizing a variation of the classical post-antibiotic effect assay, which measures the ability of an agent to affect an organism's growth after a short exposure period. Monocultures of WI-STAMP-targeted and untargeted organisms were exposed to M8(KH)-20, M8(BL)-20, BL(KH)-20, or unmodified BD2.20, then allowed to recover. As shown in FIG. 17A, S. mutans growth was effectively retarded by M8-containing constructs (M8(KH)-20, M8(BL)-20), but was not altered by a MH-STAMP construct lacking this region (BL(KH)-20). Similarly, the growth of the other targeted bacterium, P. aeruginosa, was inhibited in a KH-dependant manner (FIG. 17B). In comparison, the non-targeted bacteria E. coli, S. aureus, and S. epidermidis were not inhibited by treatment with any MH-STAMP and were only inhibited by the base antimicrobial peptide BD2.20, which displayed robust antimicrobial activity against all examined strains. These results indicate that MH-STAMPs containing KH or M8 targeting domains have activity against P. aeruginosa or S. mutans, respectively, and not other bacteria. Furthermore, replacement of the targeting region with a non-binding peptide abolishes specific activity.
• Ability of MH-STAMPs to Direct a “Population Shift” within a Mixed Species Population
• We hypothesized that potential MH-STAMP dual-functionality could affect a particular set of bacteria within a mixed population, thereby promoting the outgrowth of non-targeted organisms and “shifting” the constituent makeup. To examine this possibility, defined mixed populations of planktonic cells were treated continuously and the make-up of the community examined after 24 h. As shown in FIG. 18, treatment with the wide spectrum AMP BD2.20 resulted in a significant loss of recoverable cfu/mL after 24 h from all species in the mixture. Treatment with M8(KH)-20 was found to alter this pattern; we observed ˜1×10⁵ cfu/mL surviving E. coli and S. epidermidis, but did not recover S. mutans or P. aeruginosa cfu/mL. In BL(KH)-20 treated samples, P. aeruginosa cfu/mL were not observed, though we recovered higher than input cfu/mL from S. mutans and unchanged numbers of S. epidermidis and E. coli. In samples exposed to M8(BL)-20, S. mutans recoverable cfu/mL were greatly reduced compared to input cfu/mL, while other species were not affected or affected to a lesser extent. Interestingly, these results suggest that M8(KH)-20, M8(BL)-20, and BL(KH)-20 retain their ability to affect organisms recognized by the targeting regions present, even within a mixed population of bacteria.
Discussion
• Our results indicate that we have successfully constructed a STAMP with dual antimicrobial specificities controlled by the targeting peptides present in the molecule; KH for Pseudomonas spp, M8 for S. mutans. In a closed multi-species system (FIG. 18), the dual specificity of M8(KH)-20 was readily discernable: the population of the culture “shifted” away from targeted organisms after MH-STAMP treatment. The targeted bacteria were eliminated and the population of untargeted organisms increased, to varying degrees, above-input cfu/mL. Additionally, interruption of KH or M8 in the MH-STAMP construct with the non-binding peptide BL-1 resulted in the expected elimination of only one targeted species. These results support the hypothesis that functional MH-STAMPs could be constructed from a wide-spectrum AMP base.
• The emergence of metagenomics and the development of more sensitive molecular diagnostics has driven an increase in the understanding of human-associated microbial ecologies and host-microbe interactions (Aas et al. (2005) J Clin Microbiol., 43: 5721-5732; Boman (2000) Immunol Rev., 173: 5-16; Kreth et al. (2005) J Bacteria, 187: 7193-7203). At mucosal surfaces, it has become clear that our bodies harbor an abundance of residential flora which may impact innate and humoral immunity, nutrient availability, protection against pathogens, and even host physiology (Metges (2000) J Nutr., 130: 1857S-64; Sears (2005) Anaerobe, 11: 247-251; Lievin-Le et al. (2006) Clin Microbiol Rev., 19: 315-337; DiBaise et al. (2008) Mayo Clinic Proceedings 83: 460-469). Furthermore, findings have indicated that shifts in the diversity of normal flora are associated with negative clinical consequences; for example the overgrowth of S. mutans in the oral cavity during cariogenesis (linked to the uptake of sucrose) or the antibiotic-assisted colonization of the intestine by Clostridium difficle (Loesche (1986) Microbiol Rev., 50: 353-380; Gould and McDonald (2998) Crit Care 12: 203). Other population shifts may be linked to axilla odor (Corynebacteria spp) (Leyden et al. (1981) J Invest Dermatol., 77: 413-416; Elsner (2006) Curr Probl Dermatol., 33: 35-41), or even host obesity. Given the quantity and diversity of microbes present, pathogenesis at mucosal surfaces is not likely to be associated with the overgrowth of a single strain or species. More often, it is a population shift resulting in the predominance of two or more species; for example the persistence of Burkholderia cepacia and P. aeruginosa in cystic fibrosis airway or Treponema denticola and Porphymonas gingivalis and other “red cluster” organisms in gingivitis (Govan and Deretic (1996) Microbiol Rev., 60: 539-574; Paster et al. (2001) J Bacteriol., 183: 3770-3783). In many cases (such as the latter) these species may have only distant phylogenetic relationships and display differential susceptibilities to antibiotic therapies resulting in persistent disease progression despite treatment (Schlessinger (1988) Clin Microbiol Rev., 1: 54-59; Tresse et al. (1997) J Antimicrob Chemother., 40: 419-421). Currently, available treatments for infections of mucosal surfaces are largely non-specific (traditional small-molecule antibiotics, mechanical removal), and thus are not effective in retaining flora or shifting the constituent balance back to a health-associated composition (Keene and Shklair (1974) J Dent Res., 53: 1295). There is a need for a therapeutic treatment that can selectively target multiple pathogens, regardless of their phylogenetic relationship, and MH-STAMPs can help achieve this goal.
• In monoculture experiments (FIG. 17), our results suggest that M8 or KH inclusion in the MH-STAMP drove activity towards S. mutans or P. aeruginosa, but also that the presence of a targeting domain reduced the activity of the parent AMP BD2.20 against untargeted organisms. In contrast, the results of our MIC assays (Table 19) indicate little difference in activity between BD2.20 and any MH-STAMP. Against untargeted organisms, the M8 and KH regions are likely to have a negative, but not completely inhibitory, impact on BD2.20 activity. Given the long duration of activity and the lower inoculum size in the MIC assay (compared with experiments in FIG. 17), it is likely that all BD2.20-containing peptides could reach equal levels of growth inhibition, despite large and target-specific differences in antimicrobial speed. This pattern of results was also observed when comparing MICs of targeted and untargeted organisms utilizing STAMPs against S. mutans and Pseudomonas mendocina (Eckert et al. (2006) Antimicrob Agents Chemother., 50: 3651-3657; Eckert et al. (2006) Antimicrob Agents Chemother., 50: 1480-1488).
• Although more rigorous studies and a more medically relevant combination of pathogen targets is desirable, these findings indicate that it is possible to design an antimicrobial peptide-based therapeutic with multiple and defined fidelities in vitro. MH-STAMPs may help improve human health through the promotion of healthy microbial constituencies.
Example 2 Synthesis of Peptide—Porphyrin Conjugate
• The mixture of coupling reagent HATU (5 eq. excess, 10 mg) and purpurin-18 (MW 564, 5 eq excess, 15 mg) in 600 mL dry dichloromethane (DCM):DMF:dimethylsulphoxide (DMSO) (1:1:1 (v/v)) was added to the peptide resin (1 molar equivalent, 15 mg) which was swelled by placing in minimal DMF for 30 min prior to reaction. 26 μL (10 molar equivalents) DIPEA was then added to the reaction flask to initiate the reaction. The reaction mixture was protected with argon and stirred at room temperature for 3 h.
• After finishing, the reaction mixture was then passed down a sintered glass filtered vial and extensively washed with DMF and DCM to remove all waste reagents. The resin was then dried overnight in vacuum, and cleaved with 1 ml of trifluoroacetic acid (TFA)/thioanisole/water/EDT (10/0.5/0.5/025) for 2 hr at room temperature, and the cleavage solution was precipitated with 10 mL methyl-tert butyl ether. The precipitate was washed twice with the same amount of ether.
Example 3 Synthesis of Peptide—CSA Conjugate
• To the fully protected peptide (solution of B43-GGG (FIDSFIRSF-GGG, 0.025 mmol) and tri-Boc-CSA-15 (0.0125 mol) in 300 μL DMF, DCC (7.7 mg), HOBt (5.1 mg) and 13 μL DIEA were added in iced-bath. After stirred at room temperature for four days, the reaction mixture was poured into 5 ml water and extracted with chloroform (5×3 mL). The CHCl₃ extract was evaporated under vacuum and dried in a lyophilizer overnight. The dried CHCl₃ extracts was then dissolved in 1 mL DCM followed by added 1 mL of TFA in iced-bath. The reaction mixture was further stirred at room temperature for 2 hours and precipitated with methyl tert-butyl ether (10 mL). The precipitate was further washed once with the same amount ether and dried in vacuum.
Example 4 STAMPs Against Corynebacterium jeikeium and Streptococcus mutans
• This example illustrates the development of STAMPs to selectively target and reduce or eliminate Streptococcus mutans (dental caries) or Corynebacterium jeikeium (body odor, opportunistic infections) from mixed microbial populations.
• Axilla odor is caused by overgrowth of, and metabolite production from, Corynebacterium spp, which replaces Staphylococcus and Micrococcus spp associated with less odor. Current hygiene (soaps, antibiotics, antiseptics, disinfectants) practices remove all bacteria, allowing the ratio of Corynebacteria to normal flora to remain high during regrowth. Deodorants and anti-perspirants are temporary solutions that hide or even exacerbate the problem.
• S. mutans is the major etiological agent of dental caries. Current methods (tooth brushing, antiseptic mouthrinses) to treat cariogenesis have focused on complete bacterial removal, i.e., elimination of S. mutans and other harmless oral bacteria. Caries have persisted despite these methods, and in many cases, S. mutans can become the dominant organism in the mouth. Several S. mutans and acid-targeted approaches (probiotic replacement, saliva pH adjustment) are under development, but none have shown clinical efficacy.
• This example describes a number of STAMPs that preferentially or selectively reduce or eliminate S. mutans and/or Corynebacterium spp from mixed populations.
• Several lead STAMPs with specific activity against Corynebacterium jeikeium are also disclosed herein.
• The STAMPs described herein comprise functional regions within a peptide molecule or a chemical conjugate. These regions include a targeting region comprising one or more targeting moieties (e.g., targeting peptides), a linker, and one or more killing moieties (e.g., antimicrobial peptides (AMPs), porphyrins, etc.).
• The STAMPs function through the targeting region, which selectively accumulates STAMPs, and therefore killing regions, on or in proximity to the microorganism of interest. Other flora are not recognized by the targeting region, and therefore avoid or have reduced STAMP accumulation and cellular damage.
• In certain embodiments, STAMPs against oral S. mutans are best applied formulated in a mouthrinse, toothpaste, cream, gel, or adhesive strip, and in certain preferably embodiments, are provided in a formulation that comprises 0.5 to 2.5×PBS (or other salt) and other ingredients commonly found in oral healthcare formulations (e.g., mouthrinse formulations). Certain illustrative formulations are shown in Table 20.
• During the course of evaluating STAMPs, antimicrobial peptides (AMPs), and binding peptides for desired activity, it was discovered that certain formulations can attenuate or promote peptide activity, as compared to activity levels in a default buffer system (1×PBS). In some cases, 1×PBS may provide the best level of activity. Below are a number of formulations that alter, or may alter, peptide or STAMP activity. For complex buffer systems, assume the base solvent is water unless otherwise stated.
• Formulation 1 (1×PBS, pH 7.4): 136.8 mM NaCl, 2.68 mM KCl, 1.01 mM Na₂HPO₄, and 1.37 mM KH₂PO₄.
• Formulation 2 (HEPES/CTAB): 20 mM HEPES (4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid), 150 mM NaCl, 1 mM MgCl₂, and 0.1% CTAB (Cetyl trimethylammonium bromide).
• Formulation 3 (TRIS/CTAB): 20 mM Tris (tris(hydroxymethyl)aminomethane), pH 7.5, 150 mM NaCl, 1 mM MgCl₂, and 0.1% CTAB.
• Formulation 4: 20 mM HEPES.
• Formulation 5: 20 mM Tris, pH 7.5.
• Formulation 6: 0.2% CTAB.
• Formulation 7: 1% Glycerol.
• Formulation 8: 1% Pluronic F108 (nonionic surfactant: α-Hydro-.omega.-hydroxypoly(oxyethylene)poly(oxypropylene)poly(oxyethylene) block copolymer).
• Formulation 9: 1% Pluronic F123 (Poly(ethylene glycol)-block-poly(propylene glycol)-block-poly(ethylene glycol), average M_n ˜5,800).
• Formulation 10: 1% Pluronic F17R4 (Poly(propylene glycol)-block-poly(ethylene glycol)-block-poly(propylene glycol), average M_n ˜2,700).
• Formulation 11: 1% to 7% PEG400.
• Formulation 12: 50 mM Urea.
• Formulation 13: 10 mM AOT (Sodium bis(2-ethylhexyl) sulfosuccinate).
• Formulation 14: 0.5-0.1% Tween 20 (nonionic detergent, also known as polysorbate 20 or PEG(20)sorbitan monolauratesorbitan monolaurate).
• Formulation 15: 0.5-0.1% Tween 80 (nonionic surfactant, C₆₄H₁₂₄O₂₆, also known as polyoxyethylene (20) sorbitan monooleate, (x)-sorbitan mono-9-octadecenoate poly(oxy-1,2-ethanediyl), or POE (20) sorbitan monooleate).
• Formulation 16: 5-10% Ethanol.
• Formulation 17: 20% Glycerin.
• Formulation 18: 20% Sorbitol.
• Formulation 19: 10% Glycerin/10% Sorbitol.
• Formulation 20: 0.1% SLS (Sodium lauryl sulfate).
• Formulation 21: 1% Pluronic F127 (nonionic surfactant: α-Hydro-.omega.-hydroxypoly(oxyethylene)poly(oxypropylene)poly(oxyethylene) block copolymer).
• Formulation 21: 0.1% Tween 20 (nonionic detergent, also known as Polysorbate 20, or PEG(20)sorbitan monolaurate).
• Formulation 21: 10% PG (phospholipid gel).
• Mouthrinse neat solution #1 (made in 1×PBS): 7% ETOH, 20% Glycerin, 7% PEG 400, and 1% PLURONIC® F127.
• Mouthrinse neat solution #2 (made in 1×PBS): 7% ETOH, 20% Sorbitol, 7% PEG 400, and 1% PLURONIC® F127.
• Mouthrinse neat solution #3 (made in 1×PBS): 7% ETOH, 20% Glycerin and 7% PEG 400.
• Mouthrinse neat solution #4 (made in 1×PBS): 7% ETOH, 20% Sorbitol and 7% PEG 400.
• Other illustrative, but not limiting, mouthrinse formulations are shown in Table 20.

• TABLE 20
  Illustrative mouthrinse formulations.

  Rinse#	ETOH	Glycerin	PEG400	F127	Water1	Fluoride

  1	5	22.5	7	1	64.5	187.5
  2	6	25	1	0	68	0
  3	6	20	7	0	67	0
  4	6	20	1	1	72	0
  5	7	25	7	0	61	0
  6	7	20	1	0	72	0
  7	7	20	7	0	66	250
  8	5	20	7	1	67	0
  9	6.472	21.139	5.361	0.722	66.306	250
  10	7	22.5	1	0	69.5	250
  11	5	25	1	0	69	250
  12	7	20	7	0	66	250
  13	5	20	1	1	73	250
  14	5	25	7	0.5	62.5	250
  15	7	25	1	0.5	66.5	250
  16	7	25	7	1	60	250
  17	5	25	7	0.5	62.5	0
  18	7	20	1	1	71	250
  19	6	25	1	1	67	250
  20	7	25	7	1	60	125
  21	5	25	1	0	69	250
  22	5	20	1.5	0.5	73	0
  23	7	20	1	1	71	250
  24	6	20	1	0	73	250
  25	5	22.333	3.778	0.444	68.444	125
  26	7	25	1	1	66	0
  27	6	25	7	0	62	250
  28	7	20	7	1	65	0
  29	7	25	4	1	63	62.5
  30	5	25	4	0	66	0
  31	5	25	1	1	68	0
  32	7	25	7	1	60	0
  33	7	22.5	4	0.5	66	0
  34	5	20	4.5	0	70.5	250
  35	5	23	1	0	71	62.5
  36	6	20	1	1	72	0
  37	5	20	7	1	67	250
  38	7	20	1	0	72	0
  39	5	25	4	1	65	250
  40	5	22.5	7	0	65.5	0
  n1	7	20	7	1	65	0
  n2	7	20%	7	1	65	0
  		Sorbitol
  n3	7	20	7	0	66	0
  n4	7	20%	7	0	66	0
  		Sorbitol
  11xPBS can be substituted for water

• In certain embodiments, Corynebacterium-specific STAMPs are formulated in any number of creams, nanoemulsions, lipid micelles, aqueous or no-aqueous gels, sprays, soaps or roll-on bars, or other products used for axilla or other hygiene.
• STAMP-mediated selective antimicrobial activity can result in preservation of the normal flora at the oral or axilla mucosal surface, resulting in protective colonization and the conversion of a harmful flora to a beneficial one. Recurrence of pathogen overgrowth would be reduced, which also limits the amount and frequency (and therefore cost) of STAMP delivery. STAMPs allow for “surgical” antimicrobial precision, which limits antimicrobial resistance evolution as well due to the general mechanism of cell membrane damage mediated by the killing region.
• A number of anti-S. mutans STAMPs (see Table 21) and anti-C. jeikeium STAMPs have been designed and tested, some in formulations. All show potent selective activity against their bacterial targets in vitro, including against biofilm forms. When tested, STAMPs have little cytotoxicity against cell lines in vitro.

• TABLE 21
  Illustrative anti-S. mutans STAMPs. Single underline is
  binding peptide. Double underline is antimicrobial
  peptide (AMP). No underline is linker. *indicates
  optionally protected (e.g., amidated) C terminal.

  STAMP	Amino Acid Sequence	SEQ ID NO
  2_1G2	FIKHFIHRFGGGKNLRIIRKGIHIIKKY*	3230
  C16AF5	TFFRLFNRSFTQALGKGGGFLKFLKKFFKKLKY*	3231
  1845L621	KFINGVLSQFVLERKPYPKLFKFLRKHLL*	3232
  1903-21	NIFEYFLEGGGKLFKFLRKHLL*	3233

• TABLE 22
  Illustrative anti-C. jeikeium STAMPs. Single underline is
  binding peptide. Double underline is antimicrobial peptide
  (AMP). No underline is linker. *indicates optionally protected
  (e.g., amidated) C terminal.

  STAMP	Amino Acid Sequence	SEQ ID NO
  2038L6CAM	GKAKPYQVRQVLRAVDKLETRRKKGGRPYPGWR	3234
  135	LIKKILRVFKGL*
  1619-	SKRGRKRKDRRKKKANHGKRPNSGGGGWRLIKKI	3235
  CAM135	LRVFKGL*
  1599-BD2.16	YSKTLHFADGGGKILKFLFKKVF*	3236
  1619-BD2.16	SKRGRKRKDRRKKKANHGKRPNSGGGKILKFLFK	3237
  	KVF*
  1904-BD2.16	GSVIKKRRKRMSKKKHRKMLRRTRVQRRKLGKG	3238
  	GGKILKFLFKKVF*

• It was a surprising discovery that certain anti-S. mutans STAMPs required a salt in the formulation (e.g., PBS) for optimum activity. Thus, for example, the anti-S. mutans STAMP C16G2 (TFFRLFNRSFTQALGKGGGKNLRIIRKGIHIIKKY*, SEQ ID NO:2) comprising the TFFRLFNRSFTQALGK (SEQ ID NO:1) attached to the antimicrobial peptide (AMP) KNLRIIRKGIHIIKKY (SEQ ID NO: 3080) by a peptide linker (GGG) was substantially inactive in water-based salt-free buffers and nanoemulsions, but was active in a phosphate buffered saline (PBS) formulation. Suitable PBS formulations ranged from 0.5×PBS to about 2.5×PBS with an activity optimum at about 1×PBS. Similar results are believed to obtain for other anti-S. mutans STAMPS as well as a number of other STAMPs. In certain embodiments STAMP stability in solution was improved by inclusion of fluoride in mouthrinse.
Example 5 Photodynamic Therapy Targeted Against Streptococcus mutans
• Dental caries (tooth decay) is one of the most prevalent and costly infectious diseases in the United States. Currently, the annual expenditures on dental services exceed $85 billion, with the majority of these costs attributable to dental caries and its sequelae (www.ada.org/). The oral cavity harbors a complex microbial community consisting of over 600 different non-harmful/commensal microbial species together with a limited number of pathogenic bacteria, including the major etiological agent of dental caries, Streptococcus mutans. Once established, S. mutans generates acid during the fermentation of dietary sugars, which causes the demineralization of tooth structure and inhibits the growth of non-pathogenic commensal bacteria within the same microbial niche. Despite diligent use of broad-spectrum antimicrobial compounds and tooth brushing, S. mutans persists within the oral cavity and causes repeated cycles of cariogenesis. Current “remove all, kill-all” approaches have shown limited efficacy, since a “cleaned” tooth surface provides an equal opportunity for commensal as well as pathogenic bacteria to re-colonize in the non-sterile environment of the oral cavity. To address this shortcoming, we have constructed and evaluated a light-activated S. mutans-selective antimicrobial agent. C16-RB, constructed via conjugation of the S. mutans competence-stimulating peptide to the photodynamic dye rose bengal, displays robust anti-S. mutans activity in vitro under blue exposure from a handheld dental curing light. C16-RB has reduced activity against other oral streptococci under mixed biofilm conditions and has limited cytotoxicity in vitro.
• To develop a method of selectively eliminating S. mutans from a dental biofilm so that beneficial species exert a protective colonization effect and long-term protection from S. mutans re-colonization can be attained we created a novel class of targeted antimicrobials, known as specifically-targeted antimicrobial peptides, or STAMPs. STAMPs consist of functionally independent, yet conjoined, domains within a linear peptide sequence; a targeting region and an antimicrobial region. The targeting region, which binds specifically to a bacterial species of interest, delivers the killing portion of the molecule that consists of a normally wide-spectrum antimicrobial peptide. Previously, we successfully designed STAMPs against S. mutans by taking advantage of the competence stimulating pheromone (CSP) peptide produced by this organism that has demonstrated S. mutans-specific recognition. STAMPs synthesized with portions of CSP as targeting domains were capable of specific antimicrobial activity against S. mutans, and not other oral streptococci or non-cariogenic organisms in biofilms.
• We hypothesized that targeted killing might be achieved through the use of non-peptide antimicrobial molecules, such as porphyrins or dyes utilized in PDT. Here we present the proof-of-principle construction and in vitro efficacy of the targeted, peptide-guided, photodynamic molecule C16-RB. C16-RB displays S. mutans selective antimicrobial activity upon blue light activation with limited activity against non-cariogenic oral streptococci and epithelial cells.
Materials and Methods
• Synthesis of C16-RB
• All amino acids, synthesis resins and reagents were peptide synthesis grade (Anaspec, San Jose, Calif.; Fisher Scientific). To construct our C16-RB conjugate, conventional 9-fluorenylmethoxy carbonyl (Fmoc) solid-phase methodology was employed to synthesize the CSP_C16 peptide and attach the succinate and PEG linkers, utilizing double coupling cycles in N-hdroxybenzotrazole, HBTU (O-benzotriazole-N,N,N,N-tetramethyl-uronium hexafluoro-phosphate) and diisopropyl ethylamine (DIEA), with dimethylformamide (DMF) and N-methylpyrrolidone (NMP) as solvents, as described previously. The peptide resin (1 molar equivalent, 15 mg) was then swollen in DMF for 30 min prior to attachment of the PEG terminal amide group to the carboxyl lactone in RB (FIG. 19B). This reaction was carried out in a mixture of 2-(7-Aza-1H-benzotriazole-1-yl)-1,1,3,3-tetramethyluronium hexafluorophosphate (HATU, 5-molar excess) in dichloromethane (DCM):DMF:dimethylsulphoxide (DMSO) (1:1:1 (v/v)). Ten molar equivalents of DIEA were added to the reaction flask to initiate the reaction, which was protected with argon and stirred at room temperature for 5 h. After completion, the reaction mixture was passed down sintered glass filtered vial and extensively washed with DMF and DCM to remove all waste reagents. The resin was then dried overnight in vacuum, and cleaved with 1 mL of trifluoroacetic acid (TFA)/thioanisole/water/EDT (10/0.5/0.5/025) for 2 hr at room temperature. The cleavage solution was precipitated with 10 mL methyl-tert butyl ether, and the precipitate was washed twice with the same amount of ether. The crude product was purified via preparative-level HPLC (Source 15RPC column, ACTA purifier, Amersham) and eluted with gradient acetonitrile/water from 10 to 35% in 10 min, which was increased to 90% over 8 min before finally being washed 15 min with 95% acetonitrile.
• C16-RB was purified further to >90% and the molecular mass confirmed via LC/MS, utilizing increasing hydrophobicity gradient of acetonitrile in water with 0.01% TFA as described above (Waters X-bridge BEH 130 C18 column, 4.6×100 mm, particle size 5 μm, Waters 3100 system). LC spectra were analyzed with MassLynx Softward v. 4.1 (Waters). C16-RB mass (3118.0) was confirmed by electrospray ionization (ESI) mass spectroscopy in linear, positive ion mode. The final product was lyophilized and protected from light at all times. C16-RB was soluble in 50% methanol.
• Bacterial and Cellular Growth
• Streptococcus oralis ATCC 10557, Streptococcus gordonii (Challis), Streptococcus sanguinis (NY101), Streptococcus mitis ATCC 903, Streptococcus salivarius ATCC 13419 and S. mutans wild-type UA140 and JM11 (spectinomycin-resistant) strains were grown in Todd-Hewitt (TH) broth 37° C. in an anaerobic atmosphere of 80% N₂, 10% CO₂, and 10% H₂. BHK-21 (ATCC CRL-10) fibroblasts were propagated in DMEM with 10% FBS, 1 mM sodium pyruvate, 100 units/mL penicillin G, and 100 μg/mL streptomycin at 37° C. with 5% CO₂. Cells were detached with 0.25% trypsin and subcultured as recommended by the supplier.
• Photodynamic Antimicrobial Assays Against Biofilms
• To evaluate C16-RB against monoculture biofilms, S. mutans UA140 was grown overnight in TH prior to inoculation for biofilm formation. For biofilms, 1:5000 dilution of overnight culture was made into TH with 1% sucrose in 2 mL centrifuge tubes (200 μL volume) and grown 24 h under anaerobic conditions. After incubation, biofilms were treated for 5 min with 5 or 25 μM C16-RB or 5 μM RB in 1×PBS, or PBS alone, followed by removal of supernatant and exposure to 5 min blue light (emission 400-550 nm, power 400 mW/cm²) from an Astralis 7 (Ivoclar Vivodent, Austria) handheld LED commonly used as a dental curing light. The light source was suspended 4 cm from the tube bottom (even with the mouth of the tube). A duplicate set of samples were left covered to serve as dark controls. After treatment, biofilms were mechanically disrupted and plated to determine cfu/mL.
• To gauge C16-RB selectivity for S. mutans, similar assays were conducted against multispecies biofilms. Mixed biofilms were seeded by diluting (1:5000) a mixture of equal parts S. oralis, S. gordonii, S. mitis, S. sanguinis, S. salivarius, and S. mutans JM11 (made from overnight cultures) into TH with 1% sucrose, 1% glucose, and 1% mannose. Biofilms were incubated and treated as described above with the addition of vitamin C or potassium gluconate. After the addition of agent and 5 min incubation, biofilms were washed 1× with 1×PBS prior to light exposure. After PDT and biofilm disruption, survivors were plated on TH, and TH supplemented with 800 μg/mL spectinomycin, which allowed for quantitation of surviving total oral streptococci and surviving S. mutans, respectively.
• Evaluation of C16-RB Cytotoxicity
• The effect of RB and C16-RB on human fibroblasts was ascertained by utilizing the Promega CellTiterGlo assay, as described by the manufacturer. Briefly, fibroblasts were grown to confluence, detached, and seeded to ˜5,000 cells per well in a 96-well opaque walled, clear bottom 96-well plate (Nunc International). For long-term dark toxicity, cells were allowed to attach to for 18 h before the culture medium was replaced with medium plus serially-diluted RB or C16-RB (200 μM to 390 nM) or medium alone. After 18-24 h, equal volume Cell Titer Glo reagent was added to each well and mixed. Luciferace activity was then quantified to measure cell viability (Varian Fluorometer in Biolumenescence mode). To measure cytotoxicity after RB or C16-RB light exposure, cells were seeded at ˜10,000 cells per well and allowed to attach for 4 h. Cell growth medium was then replaced with RB or C16-RB containing medium, prior to exposure (a single well at a time) with blue light (400 mW/cm²) suspended ˜3 cm from the well bottom. After exposure, cultures were disrupted with Cell Titer Glo and luciferase activity quantitated as above.
Results
• Design of Photodynamic Peptide-Dye Conjugate
• For the targeting peptide component of the chimeric molecule, we selected a shortened derivative of S. mutans CSP, CSP_C16 (sequence: TFFRLFNRSFTQALGK). CSP_C16 has been utilized successfully as a STAMP targeting peptide in several constructs, and demonstrates selective binding to S. mutans and not other non-cariogenic bacteria. For the photodynamic dye, we selected rose bengal (RB, FIG. 19A), a xanthene dye with a demonstrated record of safety as a diagnostic tool in optometry. Unlike TBO or methylene blue, RB is not recognized by efflux pumps, and has shown robust activity against a variety of bacteria in vitro in the presence of green or blue light (max absorption ˜549 nm), and can be activated by a handheld dental curing LED.
• C16-RB Synthesis
• As shown in FIG. 19B, RB was attached to the N-terminus of CSP_C16 through a succinate/PEG linker to construct the C16-RB molecule. Conventional solid-phase peptide methods were utilized to synthesize CSP_C16, followed by linker and RB coupling prior to cleavage from the resin. After cleavage, C16-RB was repeatedly purified by LC/MS prior to evaluation. As shown in FIG. 20, over 95% purity was achieved with the expected mass species observed. The lactone ring in RB was opened as a result of CSP_C16 attachment. However, we hypothesized that the conjugate would retain enough singlet-oxygen generating activity for a proof-of-principle demonstration, as other xanthene dyes with activity lack this ring.
• C16-RB Efficacy Against Single-Species S. mutans Biofilms
• After synthesis, the basic photosensitization potential of C16-RB was assessed by challenging mature single-species S. mutans biofilms (grown 24 h) with C16-RB or unmodified RB, followed by blue emission from a dental curing light. As shown in FIG. 21, potent antimicrobial activity was observed in cultures exposed to C16-RB or RB and blue light: a reduction in over 3 log_in from input cfu/mL at 5 or 25 μM In contrast, appreciable decreases in cfu/mL were not observed in S. mutans treated with blue light alone, or 5 μM RB or C16-RB dark controls. Modest dark toxicity was observed in samples treated with 25 μM C16-RB. Overall, these results indicate that the peptide-dye conjugate is active against S. mutans and at roughly similar levels to the parental RB molecule.
• Selective PDT Against Multi-Species Biofilms
• C16-RB was next evaluated for selectivity in mixed cultures containing S. mutans and non-cariogenic oral streptococci that compete for the same niche on the tooth surface. We utilized mixed biofilms of S. mutans transformed with spectinomycin resistance (strain JM11, Merritt, et al., 2005), plus S. oralis, S. gordonii, S. mitis, S. sanguinis, and S. salivarius. The mixed cultures were grown 24 and then treated with RB or C16-RB as indicated, plus potassium gluconate to minimize killing of untargeted bacteria by reducing the superoxide-producing activity of the free C16-RB not bound to S. mutans. Ethanol treatment served as an indiscriminant killing control. As shown in FIG. 21, RB alone exhibited strong indiscriminant photodynamic antimicrobial effects against S. mutans and non-S. mutans in the mixed biofilm system (ratio of surviving S. mutans:non-cariogenic streptococci cfu ˜1). In contrast, C16-RB displayed specific photodynamic activity towards S. mutans, and not the other oral streptococci examined, as reflected in the low ratio of recovered S. mutans to other streptococci. These results suggest C16-RB has antimicrobial activity in the presence of blue light that is specific for S. mutans and dependent on the CSP_C16 targeting peptide.
• Cytotoxicity Against Eukaryotic Cells
• Given the demonstrated PDT potential of RB-C16, experiments were conducted to examine the cytotoxicity for this conjugate and RB alone. IC₅₀s were obtained for BHK cells exposed C16-RB, RB, or Melittin B (positive control for cytotoxicity), with and without blue light exposure. As shown in Table 23, cytotoxicity was noted for cells exposed to Melittin B at the lowest peptide dilution tested at either 5 min or 24 h, with or without light (IC₅₀<1.56 while light-dependent toxicity was observed only for RB-treated samples. No photo-associated toxicity was noted in BHK cells treated with C16-RB, though modest light-independent cytotoxicity (IC₅₀=90 μM) was detected after 24 h of exposure. These results suggest that C16-RB is not toxic to BHK cells after illumination, and displays mild toxic effects (when compared to Melittin B) after 24 h exposure.

• TABLE 23
  Cytotoxicity of RB and C16-RB compounds.

  	IC50 (μM)
  	BHK

  	5 min dark:
  	RB-C16	>100
  	RB	>100
  	Melittin B	<1.56
  	5 min w/blue light:
  	RB-C16	>100
  	RB	40
  	Melittin B	<1.56
  	24 h dark
  	RB-C16	55
  	RB	90
  	Melittin B	<1.56

• It is understood that the examples and embodiments described herein are for illustrative purposes only and that various modifications or changes in light thereof will be suggested to persons skilled in the art and are to be included within the spirit and purview of this application and scope of the appended claims. All publications, patents, and patent applications cited herein are hereby incorporated by reference in their entirety for all purposes.

Claims (32)

1. A chimeric construct, said construct comprising:

an effector attached to a peptide targeting moiety comprising an amino acid sequence found in Table 3 and/or Table 12.

2-5. (canceled)

6. The chimeric construct of claim 1, wherein said effector comprises a moiety selected from the group consisting of an antimicrobial peptide, an antibiotic, a ligand, a lipid or liposome, an agent that physically disrupts the extracellular matrix within a community of microorganisms, and a polymeric particle.

7. The chimeric construct of claim 1, wherein said effector comprises an antimicrobial peptide comprising an amino acid sequence found in Table 4, and/or Table 5, and/or Table 14, and/or Table 15.

8-12. (canceled)

13. The chimeric construct of claim 1, wherein said targeting moiety is chemically conjugated to said effector.

14. The chimeric construct of claim 13, wherein said targeting moiety is chemically conjugated to said effector via a linker.

15. The chimeric construct of claim 13, wherein said targeting moiety is chemically conjugated to said effector via a linker comprising a polyethylene glycol (PEG).

16. The chimeric construct of claim 13, wherein said targeting moiety is chemically conjugated to said effector via a non-peptide linker found in Table 16.

17. The chimeric construct of claim 1, wherein said targeting moiety is linked directly to said effector.

18. The chimeric construct of claim 1, wherein said targeting moiety is linked to said effector via a peptide linkage.

19. The chimeric construct of claim 18, wherein said effector comprises an antimicrobial peptide and said construct is a fusion protein.

20. The chimeric construct of claim 18, wherein said targeting moiety is attached to said effector by a peptide linker comprising or consisting of an amino acid sequence found in Table 16.

21-26. (canceled)

27. A pharmaceutical composition comprising a chimeric construct of claim 1 in a pharmaceutically acceptable carrier.

28.-29. (canceled)

30. An antimicrobial composition effective to kill or to inhibit the growth and/or of a microorganism and/or the formation and/or maintenance of a biofilm, said composition comprising one or more isolated antimicrobial peptides, the amino acid sequences of said peptides comprising one or more sequences selected from the amino acid sequences listed in Table 4 and/or Table 5.

31.-55. (canceled)

56. The composition of claim 30, wherein said peptides comprise all “L” amino acids.

57. The composition of claim 30, wherein said peptides comprise all “D” amino acids.

58. (canceled)

59. The composition of claim 30, wherein said peptides are β peptides.

60. The composition of claim 30, wherein said peptides comprise one or more protecting groups.

61-65. (canceled)

66. A method of killing and/or inhibiting the growth and/or proliferation of a microorganism, said method comprising contacting said microorganism with a chimeric construct of claim 1.

67-80. (canceled)

81. A method of detecting a bacterium and/or a bacterial film, said method comprising:

contacting said bacterium or bacterial film with a composition comprising a detectable label attached to a targeting peptide comprising one or more amino acid sequences found Table 3 and/or Table 12; and

detecting said detectable label wherein the quantity and/or location of said detectable label is an indicator of the presence of said bacterium and/or bacterial film.

82-83. (canceled)

84. A composition comprising a photosensitizing agent attached to a targeting peptide comprising an amino acid sequence of a peptide found in Table 3 and/or Table 12.

85-90. (canceled)

91. A method of inhibiting the growth or proliferation of a microorganism or a biofilm, said method comprising contacting said microorganism or biofilm with a composition of claim 84.

92-112. (canceled)

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