CA2035959A1 - Peptide compositions and uses therefor - Google Patents

Abstract

ABSTRACT OF THE DISCLOSURE

A biologically active amphiphilic peptide which in accordance with an aspect of the present invention, includes one of the following basic structures X1 through X7, wherein:
X1 is -[R1-R2-R2-R3-R1-R2-R2]-n X2 is -[R2-R2-R3-R1-R2-R2-R1]-n;
X3 is -[R2-R3-R1-R2-R2-R1-R2]-n;
X4 is -[R3-R1-R2-R2-R1-R2-R2]-n;
X5 is -[R1-R2-R2-R1-R2-R2-R3]-n;
X6 is -[R2-R2-R1-R2-R2-R3-R1]-n; and X7 is -[R2-R1-R2-R2-R3-R1-R2]-n;
wherein R1 is a basic hydrophilic amino acid, R2 is a hydrophobic amino acid, R3 is a neutral hydrophilic, basic hydrophilic or hydrophobic amino acid and n is from 2 to 5.
Preferred peptides are of the following formulae:
(Lys Ile Ala Gly Lys Ile Ala)3-NH2 and (Lys Ile Ala Lys Ile Ala Gly)3-NH2 In another aspect of the prevent invention, there is provided a biologically active amphiphilic peptide which includes the following basic structure.
R1-R2-R2-R3-R4-R2-R2-R1-R2-R2-R2-R4-R2-R2, wherein R1, R2, and R3 are as hereinabove described, and R4 is a basic hydrophilic or hydrophobic amino acid.
Preferred peptides are of the following formulae:
and In yet another aspect of the present invention, there is provided a biologically active amphiphilic peptide including the following structural formula:
(Lys Ile Ala Lys Lys Ile Ala)n, wherein n is from 2 to 5.
In a further aspect of the present invention, there is provided a biologically active amphiphilic peptide selected from the group consisting of:
(SEQ ID NO:61)-NH2;
(SEQ ID NO:62)-NH2;
(SEQ ID NO:63)-NH2; and (SEQ ID NO:64)-NH2.
The peptides may be used in pharmaceutical compositions.

Description

203~959 NOVEL PEPTIDE COMPOSITIONS AND
USES l~ERE'EOR

This application i8 a continuatlon-in-part of application Serial No. 476,629, filed February 8, 1990.
Thls invention relates to biologically active peptides, and more particularly to novel biologically active peptldes and uces therefor.
In accordance with an aspect of the preqent invention, there i8 provided a biologically active amphiphilic peptide which includes one of the following baeic structures Xl through X7 wherein:
Xl i 8 _[Rl R2-R2-R3-Rl-R2-R2~_ ;
X2 i8 -lR2-R2-R3-Rl-R2 R2 Rl] n X3 is -[R2_R3-Rl-R2-R2 Rl 2] n X4 i~ -[R3_Rl-R2-R2-Rl R2 R21 n;
X5 i~ -[Rl-R2-R2-Rl-R2 R2 R3] n;
X6 1~ -[R2-R2-Rl-R2-R2-R3 Rll n;
X7 i~ -[R2_Rl-R2-R2-R3 Rl R2] n;
whereln Rl 1~ a baslc hydrophilic amino acid, R2 i~ a hydrophobic amino acld, R3 is a neutral hydrophilic or hydrophoblc amino acid, and n is from 2 to 5.
The ba~ic hydroph~lic amino acids include, but are not limited to Ly~, Arg, His, Orn, homoarginine (Har), 2, 4-diamino butyric acid (Dbu), and p-aminophenylalanine.

2~359~9 The hydrophobic amino acids include, but are not limited to Ala, Cy9, Phe, Gly, Ile, Leu, Met, Pro, Val, Trp, Tyr, norleucine (Nle), norvaline (Nva~, and cyclohexylalanine (Cha).
The neutral hydrophilic amino acid~ include, but are not limit~d to Asn, Gln, Ser and Thr.
In accordance with one embodiment, when the peptide includes the structure Xl, the peptide may include the following structure:
Yl-Xl, wherein Xl is as hereinabove de~cribed, and Y is:
(i) R2;
(ii) R2-R2;
(iii) Rl-R2-R2;
(iv) R3-Rl-R2 R2;
( ) 2 3 Rl R2 R2; or (vl) R2-R2-R3-Rl-R2-R2, wherein Rl, R2, and R3 are as herelnabove de~crlbed In accordance with another embodiment, when the peptide includes the structure Xl, the peptide may include the following structure:
Xl-Zl, wherein Xl is a~ hereinabove described, and Zl is:
(i) Rl;
(ii) Rl-R2;
(ili) R~ 2-R2;
(iv) Rl-R2 R2 R3;
(v) Rl-R2-R2-R3-Rl; or ~vi ) Rl-R2-R2-R3-Rl R2 -In accordance with yet another embodiment, the peptide may include the following structure:
(Yl)a-Xl-(Zl)b, wherein Yl and Zl are as previously defined, a lc 0 or 1, and b is 0 or 1.
When the peptide includes the structure X2, the peptide may include tho followlng structure:
Y2 ~ X2, wherein X2 is as hereinabove described, and Y2 i~:

203~9 ~i) Rl;
(ii) R2-Rl;
(iii) R2-R2-Rl;
( ) 1 2 R2 Rl;
(v) R3-Rl-R2-R2-R ; or (vl ) R2-R3-Rl-R2 R2 Rl -In another embodlment, the peptide may include the following ~tructure:
X2 ~ Z2 wherein X2 is as hereinabove described, and Z2 is:
(i) R2;
(ii) R2-R2;
(ili) R2-R2-R3;
(iv) R2~R2~R3 Rl;
(v) R2-R2-R3-Rl-R2; or (vl ) R2-R2-R3-Rl R2 R2 ' In accordanco with yet another embodiment, the peptide may include the following structure:
(Y2)a - X2 ~ (Z2)b~ wherein Y2 and Z2 are a~ proviously defined, a i~ O or 1, and b i~ O or 1.
In accordance wlth another embodiment, when the peptide include~ the ~tructure X3, the peptlde may include the following structure:
Y3 - X3 whereln X3 18 as herelnabove descrlbed, and Y3 i~:
(i) R2;
(li) Rl-R2;
(lli) R2-R1 R2;
(lv) R2-R2-Rl R2;
(v) Rl-R2-R2-Rl-R2; or (vl) R3-Rl-R2-R2-Rl-R2, wherein Rl, R2, and R3 are a~
hereinabove de~crlbed.
In accordanco with another embodlment, when the peptlde lnclude~ the ~tructure X3, the peptlde may lnclude the followlng structure:
X3 - Z3 wherein X3 i9 a9 hereinabove described, and Z3 is:

_4_ 20359~9 (i ) R2;
( i i ) R2-R3;
(ili) R2-R3-Rl;
( iv) R2-R3-Rl R2;
(v) R2-R3-Rl-R -R ; or (vi ) R2-R3-Rl-R2 R2 Rl, In accordance with yet another embodiment, the peptide may include the following structure:
(Y3)a ~ X3 ~ (Z3)b~ wherein Y and Z are a~ previously defined, a i~ O or 1, and b i~ O or 1.
In accordance with yet another em~odiment, when the peptide include~ the structure X4, the peptide may include the following structure:
Y4 - X4, wherein X4 i~ a~ herelnabove de~cribed, and Y4 i9:
(i) R2;
(li) R2-R2;
(iii) Rl-R2-R2;
(iv) R2-Rl-R2-R2;
~ v) R2-R2-Rl-R2-R2; or (vi) Rl-R2-R2-Rl-R2-R2, wherein Rl, R2 and R3 are as heroinabove described.
In accordance wlth another embodlment, when the peptlde include~ th- ~tructure X4, tho peptide may include the following ~tructure:
X4-Zg~ whereln, X4 i~ a~ herelnabove descrlbed, and Z4 i~:
(i) R3;
(il) R3-Rl;
(iii) R3-Rl-R2;
(iv) R3-Rl-R2 R2;
(v) R3 Rl R2 R2 Rl; or ( vl ) R3-Rl-R2-R2 Rl R2 -In accordance wlth yet another embodiment, the peptide may include the followlng ~tructure:

_5_ 203~9~9 (Y4)a~ X4 (Z4)b~ wherein X4 and Z4 are as previou~ly defined, a i8 0 or l, and b i9 0 or 1.
In accordance wlth a further embodlmQnt, when the peptlde includeq the structure X5, the peptide may include the following structure:
Y5-X5, wherein X5 i~ as hereinabove described, and Y5 i~:
(i) R3;
~i~) R2-R3;
(iil) R2-~2-R3;
(lv) Rl-R2-R2 R3;
( ) 2 Rl R2 R2 R3; or 2 2 1 R2 R2 R3~ wherein Rl, R2, and R3 are a~
hereinabove de~cribed.
In accordance with another embodlment, when the peptide includes structure X5, the peptide may lnclude the followlnq structure:
X5 - Z5 wherein X5 is as hereinabove described, and Z5 is:
(i) Rl;
(ii) Rl-R2;
(iii) Rl-R2-R2;
(iv) Rl-R2 R2 Rl;
(v) Rl-R2-R2-Rl-R2; or (vi ) Rl-R2-R2-Rl-R2 R2 ' In accordance with yet another embodlment, the peptide may include the followlng Jtructure:
(Y5)a~ X5 (Z5)b~ wherein X5 and Z5 are as previou~ly deflnod, a 18 0 or 1, and b 18 0 or 1.
In accordanco with a further embodiment, when the peptide includos the structuro X6, the peptlde may lnclude the following structure:
Y6 ~ X6 whereln X6 18 as herelnabove descrlbed, and Y6 is:
(1) Rl;
(il) R3-Rl;
(iil) R2-R3-Rl;

-6- 2~359~3 (iv) R2-R2~R3 R1;
(v) R1-R2-R2-R3-R ; or (vi) R2-R1-R2-R2-R3-R1, whereln R1, R2, and R are as hereinabove described.
In accordance with another embodiment, wh~n the peptide lncludes the structure X6, the peptide may include the following structure:
X6-Z6, wherein X6 is as hereinabove described, and Z6 is:
~1) R2;
(ii) R2-R2;
(iii) R2-R2-Rl;
(iv) R2-R2-R1 R2;
(v) R2-R2-R1-R2-R2; or (vi) R2-R2-R1-R2 R2 R3-In accordance with yet another embodiment, the peptide mayinclude the following structure:
(Y6)a- X6 (Z6~b' wherein Y6 and Z6 are as previously defined, a is 0 or 1, and b is 0 or 1.
In accordance with one embodiment, when the peptide include~
the structure X7, the peptide may include the structure Y7-X7, wherein X7 i9 a~ hereinabove de~cribed, and Y7 i8:
(i ) R2;
(li) Rl-R2;
(111) R3-Rl-R2;
(iv) R2-R3-Rl R2 (v) R2 R2 R3 R1 R2; or (vi) R1-R2-R2-R3-R1-R2, wherein R1, R2, and R3 are ag herelnabove described.
In accordance wlth a further embodlment, when the peptlde lncludes the structure X7, the peptlde may include the followinq ~tructure:
X7 - Z7 whereln X7 is as hereinabove descrlbed, and Z7 is:
(1) R2;
(ii) ~2 R1;

_7_ 2~3~9 (iii) R2-Rl-R2;
(iv) R2-Rl-R2 R2;
(v) R2-Rl-R -R -R ; or (vi) R2-Rl-R2-R2 R3 Rl-In accordance with yet another embodiment, the peptide may lnclude the following structure:
tY7)a~ X7 (Z7)b~ whereln Y7 and Z7 are as previou~ly defined, a i~ O or l, and b is Q or l.
The peptides and/or analogues or derivative~ thereof, may be C-terminal acid3 or amides.
In a preferred embodiment, n i8 3, and most preferably the peptide i~ of one of the following structure~ listed below and al80 listed in the accompanying sequence li~ting:
(Lys Ile Ala Gly Lys Ile Ala)3-NH2(SEQ ID NO: l) (Lys Ile Ala Lys Ile Ala Gly)3-NH2(SEQ ID NO: 2) ~Lys Ile Ala Gly Ly~ Ile Gly)3-NH2(SEQ ID NO: 3) ~Lys Leu Ala Gly Lys Leu Ala)3-NH2(SEQ ID NO: 4) (Lys Phe Ala Gly Lys Phe Ala)3-NH2(SEQ ID NO: 5) (Lys Ala Leu Ser Ly~ Ala Leu)3-NH2(SEQ ID NO: 6) (Lys 1eu Leu Lys Ala Leu Gly)3-NH2(SEQ ID NO: 7) (Lys Ala Ile Gly Lys Ala Ile)3-NH2(SEQ ID NO: ~) (Gly Ile Ala Lys Ile Ala Lys)3-NH2(SEQ ID NO: 9) (Lys Ile Ala Ly~ Ile Phe Cly)3-NH2(SEQ ID NO: lO) (Gly Ile Ala Arg Ile Ala Ly~)3-NH2(SEQ ID NO: ll) (Ly~ Phe Ala Arg Ile Ala Gly)3-NH2(SEQ ID NO: 12) (Gly Phe Ala Ly~ Ile Ala Ly~)3-NH2(SEQ ID NO: 13) (Lys Ile Ala Gly Orn Ile Ala~3-NH2(SEQ ID NO: 14) (Lys Ile Ala Arg Ile Ala Gly)3-NH2(SEQ ID NO: 15) (Orn Ile Ala Gly Lys Ile Ala)3-NH2(SEQ ID NO: 16) (Gly Ile Ala Arg Ile Phe Lys)3-NH2(SEQ ID NO: 17) (Lys Nle Ala Gly Lys Nle Ala)3-NH2(SEQ ID NO: 18) (Lys Nle Ala Gly Ly~ Ile Ala)3-NH2(SEQ ID NO: l9) (Ly8 Ile Ala Gly Lys Nle Ala)3-NH2(SEQ ID NO: 20) (Ly~ Nva Ala Gly Lys Nva Ala)3-NH2(SEQ ID NO: 21) 2~35959 (Lys Nva Ala Gly Ly~ Ile Ala)3-NH2(SEQ ID NO: 22) (Ly~ Leu Leu Ser Lys Leu Gly)3-NH2(sEQ ID NO: 23) (Ly~ Leu Leu Ser LYR Phe Gly)3-NH2(5EQ ID NO: 24) (Ly.~ Ile Ala Gly LY9 Nva Ala)3-NH2(5EQ ID NO: 25) (Hi~ Ile Ala Gly His Ile Ala)3-NH2(SEQ ID NO: 26) (Ala Gly LY9 Ile Ala Lys Ile)3-NH2(SEQ ID NO: 27) (Ile Ala Lys Ile Ala Cly Lys)3-NH2(SEQ ID NO: 28) (Lys Ile Ala Cly Ar~ Ile Ala)3-NH2(5EQ ID NO: 29) (Arg Ile Ala Cly Arg Ile Ala)3-NH2(SEQ ID NO: 30) (Lye Val Ala Cly Lys Ile Ala)3-NH2(SEQ ID NO: 31) (Ly~ Ile Ala Gly Lys Val Ala)3-NH2(SEQ ID NO: 32) (Ala Lys Ile Ala Gly Lys Ile)3-NH2(SEQ ID NO: 33) ~Orn Ile Ala Gly Orn Ile Ala)3-NH2(SEQ ID NO: 34) ~Lys Phe Ala Gly Lys Ile Ala)3-NH2(SEQ ID NO: 35) (Lys Ile Ala Gly Lys Phe Ala)3-NH2(SEQ ID NO: 36) (Lys Cha Ala Gly Lys Ile Ala)3-NH2(SEQ ID NO: 37) (Lys Nle Ala Lye Ile Ala Cly)3-NH2(SEQ ID NO: 38) (Arg lle Ala Cly Lys Ile Ala)3-NH2(SEQ ID NO: 39) ~Har Ile Ala Cly Har Ile Ala)3-NH2(5EQ ID NO: 40) (Xaa Ile Ala Gly Lys Il¢ Ala)3-NH2(SEQ ID NO: 41) ( Ly8 I le Ala Gly Xaa Ile Ala)3-HN2(SEQ ID NO: 42) In (SEQ ID NO:41) and (SEQ ID NO:42), Xaa is p-aminophonylalanine.

In accordancs with anothor aspect of the present lnvention, there i~ provlded a blologlcally actlve amphiphilic peptide which include~ the followlng ba~ic ~tructure X14:
1 2 2 R3 R4 R2-R2-Rl-R2-R2-R2-R4-R2-R
wherein R1, R2, and R3 are as hareinabove descrlbed, and R4 18 a basic hydrophillc or hydrophoblc amlno ac1d, In accordance with one embodiment, the peptide may include the following 3tructure:
Y14-X14, wherein X14 18 as hereinabove descrlbed, and Yl4 is:

g ~i) R2;
( i l ) R2 -R;
( ~11 ) R4-R2-R2;
( iv ) R3 -R4-R2-R
(v) 2 3 R4 R2 R2;
( vi ) R2-R2-R3 -R4-R2-R2 ~ or (vii) Rl~R2~R2~R3~R4~R2-R2,Whereln Rl, R2, R3 and R4 herelnabove described.
In accordance with another embodlment, the peptlde may include the following ~tructure:
Xl4-Z14, wherein Xl4 i~ a~ hereinabove de~cribed and Z14 i9:
(i) Rl;
(ii) Rl-R2;
( iii ) Rl-R2-R2;
( iv) Rl-R2-R2 R3;
(v) Rl-R2-R2 R~ R4;
(vi ) Rl-R2-R2-R3 R4 R2;
( ) 1 2 R2 R3 R4 R2 R2, wherein Rl, R2, R3, and R4 are as herelnabove described.
In accordance with yet another embodiment the peptide may include the following structure:
(Y14)a-Xl4-(Zl4)b, wherein X and Y are as prevlously defined, a i8 0 or 1, and b is 0 or 1. In a preferred embodiment, the peptide has the ollowing ~tructural formula a~
indicatod in tho accompanying seguence listinq:
( SEQ ID NO: 43 ) -NH2 .
In another proferred embodiment, the peptide has the followlng ~tructural formula as indlcated in the accompanying sequence listlng:
( SEQ ID NO: 44 ) -NH2 .
In accordance with a further embodiment, the peptide has one o the following structural formulae a~ indlcated ln the accompanying sequence llsting:
~SEQ ID NO: 45)-NH2 -lo- 2~35~9 ( SEQ ID N0: 46)-NH2 (SEQ ID N0: 47)-NH2 (SEQ ID No: 48)-NH2 (SEQ ID No: 49)-N~2 (SE~ ID N0: 50)-NH2 ~SEQ ID N0: 51)-NH2 (SEQ ID N0: 52)-NH2 (SEQ ID N0: 53)-NH2 (SEQ ID N0: 54)-NH2 (SEQ ID N0: 55)-NH2 (SEQ ID N0: 56)-NH2 (SEQ ID N0: 57)-NH2 ~SEQ ID N0: 58)-NH2 (SEQ ID N0: 59)-NH2 In accordance with another aspect of the present invention, there is provided a biologically actlve amphiphilic peptide which includes the following structural formula:
-(Lys Ile Ala Ly~ Lys Ile Ala)-n wherein n i8 from 2 to 5.
Preferably, n i~ 3, and the peptide ha~ the followlng structural formula:
(Lys Ile Ala Lys Lys Ile Ala)3-NH2- tSEQ ID N0:60) In accordance with another a~pect of the pre~ent invention, there is provided a blologically actlve amphiphillc peptide selocted from the group conslstlnq of the following ~tructural formulae as given ln tho accompanying sequence listing:
(SEQ ID N0: 61)-NH2 (SEQ ID N0: 62)-NH2 (SEQ ID N0: 63)-NH2 (SEQ ID N0: 64)-NH2 In accordance wlth one embodlment, each of the amlno acid resldues contained in the peptlde~ is a D-amlno acld resldue or glyclne. Although the scope of thls particular embodlment is not to bo llmlted to any theoretlcal reasonlng, it is belleved that the above-mentloned peptides, when conslstlng entirely of D-amino -11- 2~35~3 acid or glycine re~idues, may have increflsed resistanc~ to proteolytic enzyme~ while retaininq their bioloqical actlvity.
Such peptide~ thus may be administered orally. Thus in accordance with a preferred embodiment, all of the amino acid re~idue~ are either D-amino acid or glycine residues or L-amino acld or qlycine residue~.
An amphiphilic peptide ia a peptide which includes both hydrophobic and hydrophilic peptide regions.
In gsneral, the peptides hereinabove described, and/or analogues or derivatives thereof are generally water soluble to a concentration of at least 2~ mg/ml at neutral pH in water. In addition, such peptides are non-hemolytic; i.e., they will not rupture blood cells at effective concentrations. In addition, the structure of such peptide provides for flexibility of the peptide molecule. When the peptide is placed in water, it does not a~sume an amphiphilic structure. When the peptide encounters an oily qurface or membrano, the peptide chain folds upon itself into a rod-like structure.
The peptlde~ and/or analogues or derivative~ thereof may be administered to a host; for example a human or non-human animal, in an amount effective to inhibit growth of a target cell, viruQ, or virally-infected cell. Thu~, for example, the peptides and/or analogues or derivative~ thereof may be used as antimicrobial agentJ, anti-viral agent~, antibiotics, anti-tumor agents, antipara~itic agonts, antifungal agent~, spermicldo~, a~ well as xhlblting oth-r bloactlv- unction~.
Th- term "antlmlcroblal" as u~ed herein means that the peptides of the present inventlon lnhlbit, prevent, or destroy the growth or prollferatlon of microbes such as bacteria, fungi, or the like.
The term "antibiotic" as u~ed horein mean~ that the peptides employed ln the present invention produce effects adverse to the normal blological functions of the non-host cell, tissue or organism, including death or destructlon and prevention of the 2~353~9 growth or prollferation of the non-host cell, ti~sue, or organi~m, when contacted with the peptides.
The term "spermicidal" as u~ed herein mean~ that the peptideq employed in the preqent invention, inhibit, prevent, or destroy the motility of sperm.
The term "antiviral" as used herein means that the peptides employed in the present invention inhibit, prevent, or destroy the growth or proliferation of viruses, or of virally-infected cells .
The term anti-tumor as used herein means that the peptide inhlbits the growth of or destroys tumors.
The term "antifungal" as used herein means that the peptides of the pro~ent invention may be used to inhibit the growth of or destroy fungi.
The term "antiparasitlc" as used herein means that the peptides of the present invention may be used to inhibit the growth of or de~troy parasltes.
The peptides may be admlnistered ln vivo or in vitro. The peptides also may be administered directly to a target cell, virus, or virally-infected cell, or the peptides may be administered systemically, The peptides of tho pre~ent invention have a broad range of potent antibiotic activity against a plurslity of microorganism~
includlng Gram-po~itive and Cram-negative bacterla, fungi, protozoa, and the like, as woll as parasites. The peptides of tho pre~ont inventlon allow a method for treating or controlling mlcrobial inectlon cau~ed by organisms which are sensitive to the peptlde~. Such troatment may comprise admini~tering to a ho~t organl~m or ti~ue su~ceptible to or affiliated w~th a mlcroblal infoction an antimicrobial amount of at least one of the peptide~.
Becauoe of the antlblotlc, antimicrobial, and antlviral proportios of the peptide~, they may al~o be used as -13- 2~3~9~9 pre~ervative~ or sterilants of material~ susceptible ~o microbial or viral contamination.
The peptide and/or d~rivativ~s or analogues thereof may be admini~tered in combination with a non-toxic pharmaceutical carrier or vehicle ~uch as a filler, non-toxic buffer, or physiologlcal qallne solution. Such pharmaceutical compositions may be used topically or systemically and may be in any suitable form ~uch as a liquid, solid, qeml-solld, injectable solution, tablet, ointment, lotlon, paste, capsule, or the like. The peptide compositlon~ may also be used in combination with ad~uvant~, protease inhibitors, or compatlble drugs where such a comblnation is ~een to be de~irable or advantageou-q in controlling infection caused by harmful microorganlsms including protozoa, viru~es, and the like, as well as by paraslte~.
The psptide(s) of the pre~ent invention may be administered to a host; in particular an animal, in an effective antibiotic and/or antl-tumor and/or anti-viral and/or anti-mlcroblal and/or anti-parasitlc and/or an antispermicidal amount.
Deponding on the use, a compo~ition in accordance with the invention will contaln an efective anti-microbial amount and/or an effective antispermlcldal amount and/or an effectlve anti-viral amount and/or an effective anti-tumor amount and/or an effective antibiotic amount and/or anti-para~itic amount of one or more of tho horelnabove doscrlbQd peptido~ which have ~uch activity.
Tho p-ptide o tho pre~ont invention may also be employed in promoting or ~timulating healing of a wound ln a ho~t.
The term "wound healing" a~ used herein includes various aspoct~ of tho would healing process.
The~e aspects include, but are not limited to, increased contraction of the wound, increa3ed depo~ition o connective tis~ue, as evidenced by, for example, increa~ed deposltion of collagen in tho wound, and increased tensile strength of the wound, i.e., the peptides increase wound breaking ~trength. The 2~3~9~9 peptidee of the present invention may also be employed so as to reverse the inhibition of wound healing caused by steroids such a~ cortl~one or by conditlons whlch compromlse or depress the immune system.
The peptides of the present invention may be used in the treatment of external burns and to treat and/or prevent skin and burn lnfections. In particular, the peptldes may be used to treat skin and burn infection~ caused by organisms such as, but not llmited to, P. aeruainosa and S. aureu~.
The peptides are also useful in the prevention or treatment of eye infection~. Such infections may be caused by bacteria such as, but not limited to, P. aeruainosa, S. aureus, and N.
aonorrhoeae, by fungi such as but not limlted to C. albicans and A. fumlqatus, by parasites such as but not limited to A.
castellani, or by viruses.
The peptides may also be effective in killing cysts, spores, or trophozoites of infection - causing organisms. Such organism~
include, but are not limited to Acanthamoeba which forms trophozoites or cyst~, C. albicans, which forms spores, and A.
fumiaatus, which form~ spores as well.
The peptido~ may al~o bo administored to plants ln an effective antimicroblal or antiviral or antiparasitic amount to prevent or treat microbial or viral or parasitic contamination thereof.
In ~eneral, the peptido is employed to provide peptide dosagas of from 0.1 mg. to 500 mg. per kilogram of host weight, whon admini~tered systemically. When administered topically, the peptide ls used in a concentration of from .05% to 10%.
The peptides may be produced by known techniques and obtained in substantially pure form. For example, the peptides may be synthesized on an automatic peptide syntheizer. Journal of the American Chemlcal SocietY, Vol. 85, pgR. 2149-54 (1963).
It is also possible to produce such peptides by genetic engineering techniques.

-15- 2~3~~59 In accordance with another embodiment, the peptides of the present invention may be employed in combination with a toxic ion for the purposes hereina~ove described.
A toxic ion i~ one which when introduced into a target cell, virus, or virally-infected call, inhibits and/or prevent~ and/or destroys the growth of the target cell, virus, or v~rally-infected cell.
Such a toxic ion is one which in the ab~ence of an ion channel forming peptide i8 unable to cross a natural or synthetic lipid membrane; ln particular a cell membrane, in sufficient amounts to affect a cell adversely.
The peptide and toxic ion may be administered as a single composition or in separate compo~itions, and the single or separate compositions may include additional materials, actives and/or lnactives, in addition to the peptide and toxic ion. As representatlve examples of toxlc ions whlch may be employed, there may be mentloned fluoride, peroxide, blcarbonate, and silver ion~.
The peptide and the toxic ion, whether admini~tered or prepared in a single compo~ition or in ~eparate compositions, are employed in amounts effective to inhibit and/or prevent and/or de~troy the growth of the target cell, virus, or virally-infected cell. In effect, the ion potentiates the action of the peptide, i.e., the amount o toxic lon i8 effectlve to reduce the mlnimum effectlve concentration of the peptide for inhlbiting growth of a target cell, viru~, or virally-infected cell.
Tho toxic ion, whon used topically, iB generally employed in a concentration of from 0.05% to 2.0%. When used systemically, the ion i~ genorally employed in an amount of from l to 10 mq.
per kg. of host welght. Peptide dosages may be withln the ranges hereinabove described.
It 1~ also to be understood that the peptlde and toxlc lon may be delivered or admlnlstered in dlfferent forms; for example, 2B3~9 the toxic ion may be adminiqtered orally, while the peptide may be admini~tered by IV or IP.
Aq representative examples of administering the peptide and toxic ion for topical or local adminiqtration, the peptide could be administered in an amount of up to about 1% weight to weight and the toxic ion delivered in an amount of about SOmM (about 0.1%). Alternatively, the toxic ion, in the form of a salt such a3 ~odium fluoride, could be administered orally in conjunction wlth systemic administration of the peptide. For axample, the peptide may be administered IV or IP to achieve a ~erum dose of 100 micrograms per milliliter (10 milligrams per kilogram) in con~unction with an oral dose of toxlc ion, in particular, sodium fluoride, of 10 meq per kilogram.
In accordance with another embodiment, the peptidec of the present invention may be administered to a host in combination with an antibiotic selected from the class conslsting of bacltracins, gramacidin, polymyxin, vancomycin, teichoplanin, aminoglycosides, hydrophobic antibiotics, penicillin~, monobactams, or derlvatives or analogues thereof.
The bacitracins, gramacidin, polymyxin, vancomycin, teichoplanin, and derivatives and analogues thereof, are a group of polypeptide antibiotics. A preferred bacitracin i8 bacitracin A.
Aminoglycoside antibiotics include tobramycin, kanamycin, amlkacin, the gentamicin~ (e.g., gentamicin Cl, gentamlcin C2, gentamlcln Cla), netllmlcln, kanamycin, and derivative~ and analoguo~ thoroof. The preferred aminoglycosides are tobramycin and the gontamlcln~. The aminoglycosides, and the bacitracins hereinabove described, tend to be hydrophilic and water-soluble.
Penicilllns which may be employed include, but are not limited to benzyl penlclllln, ampicillin, methicillin (dlmethoxyphenyl penlclllln), tlcarlclllln, ponlclllln V
(phenoxymethyl penicillin), oxacillin, cloxacillin, dicloxacillin, flucloxacillin, amoxicillin, and amldinocillin.

-1~- 2~3~g59 Preferred penicillins which may be employed ar~ b~nzyl penicillin and ampicillin. A preferred monobactam which may he employed is aztreonam.
Aq representative examples of hydrophobic antibiotic~ which may be used in the present invention, there may be mentioned macrolides such as erythromycln, roxythromycin, clarithromycin, etc.; 9-N-alkyl derivative~ of erythromycin; midecamycin acetate;
azithromycin; flurithromycin; rifabutin: rokitamycin; a 6-0-methyl erythromycin A known a~ TE-031 (Tai~ho); rifapentine;
benzypiperazinyl rifamycins ~uch as CCP-7040, CGP-5909, CGP-279353 (Ciba-Geigy); an erythromycin A derivative with a cyclic carbamate fùsed to the Cll/Cl~ position of a macrolide ring known as A-62514 (Abbott); AC-7230 (Toyo Jozo);
bsnzoxazinorifamycin; difficidin; dirithromycin; a 3-N-plperdinomethylzalno methyl rifamycin SV known as FCE-22250 (Farmitalla); M-ll9-a (Klrln Brewery); a 6-0-methyl-1-4i'-0-car~amoyl erythromycln known as A-63075 (Abbott); 3-formylrifamycln SV-hydrazone~ with diazabicycloalkyl sids chain~ ~uch as CCP-27557 and CGP-2986 (Ciba-Geigy); and 16-membered macrollde~ havlng a 3-0-alpha-L-cladinosyl moiety, Ruch as 3-0-alpha-L-cladino~yldeepoxy ro~aramicin; tylosins and acyl demycinosyl tylo~lns.
In addltion to the macrolldes hereinabove described, rlfamycln, carbenlclllln, and nafclllln may be employed as well.
Other antlbiotlc~ which may be used (whether or not hydrophoblc) are antlblotic~ which sre 50-S rlbo~oms inhibitors such a~ llncomycin; cllndamycin; and chloramphenicol; etc.;
antlbiotlcs which havo a large lipid like lactone ring, ~uch aR
myJtatin; plmarlcln, etc.
The peptlde and antlbiotlc may be admlnqtered by dlrect admlnistratlon to a target coll or by ~y~temic or topical admini~tration to a host whlch lncludes tho target coll, in order to prevent, destroy or lnhiblt the growth of a target cell.
Targot cells whoqe growth may be prevented, inhibited, or 2~3~g -la-de~troyed by the admini~tration of the peptide~ and antibiotic include Cram-po~itive and Gram-negative bacteria as well ac fungal cells.
The antibiotic, such as those hereinabove de~cribed, or derivative~ or analogues thereof, when used topically, is qenerally employed in a concetration of about 0.1% to about 10%.
When u~ed systemically, the antibiotic or derivative or analogue thereof ~8 qenerally employed in an amount of from 1.25 mg. to about 45 mg. per kg. of host weight per day. Peptide dosageq may bo those a~ hereinabove described.
As representative exmple~ of administering the peptide and antibiotic for topical or local administration, the peptide could be admnistered ln an amount of from about 0.1% to about 10%
woight to weight, and the antibiotic is delivered ln an amount of from about 0.1% to about 10% welght to welght.
In accordance with another embodlment, the peptides of the present lnvention may be adminiqtered ln comblnation wlth an antlparasltic agent or an antifungal agent.
Antiparasitic agent~ which may be employed include, but are not limited to, anti-protozoan agents. Examples of specific anti-parasitic agents which may be employed include, but are not limited to, pentamidine isethionate, and propamldlne isethlonate (Brolene).
Anti-fungal agents which may be employed include, but are not limited to, ketoconazole. It i9 also to be underqtood that certain anti-para~ltlc agents may al~o have anti-fungal activity, and that certa1n anti-fungal agents may have anti-para~itic activity.
In accordance with another embodiment, the peptide~ of the present inventlon may be administered in combinatlon with an antibiotic which inhibits DNA gyrase, which is an enzymo lnvolved ln the formatlon of bonds between indlvidual colling strands of replicatlng bacterial DNA. Thus, DNA gyrase is neces~ary for the normal replication of bacterial DNA, and, therefore, antibiotics 2 ~ ;S 9 which inhibit DNA gyrase inhibit the normal replication of bacterlal DNA.
Example~ of antibiotic~ which inhibit DNA gyrase include nalidixic acid, oxolinic acid, cinoxacin, and quinolone antibiotic~ which include ciprofloxacin, norf].oxacin, ofloxacin, enoxacin, pefloxacin, lomefloxacin, fleroxacin, tosulfloxacin, temafloxacin, and rufloxacin.
In accordance wlth another embodlment, the peptldes of the present invention may be admlni~tered for the purpose hereinabove de~crlbed in comblnation wlth other biologically active amphlphilic peptlde~, or in combination with ion channeL-forming protein~.
Examples of biologically active amphiphilic peptide~ which may be employed in combination wlth the peptide~ of the present inventlon lnclude magalnln peptldes, PCLa peptlde~, XPF peptldes, CPE peptide~, cecropins and sarcotoxlns.
A magalnln peptlde 1J elther a magainln such a~ maqa~nin I, II, or III or an analogue or derivative thereof.
The magalnln peptide~ generally include at least fourteen amlno acids. A magalnin peptide preferably has 22 or 23 amino acids.
As representative example~ of such magainin peptldes, there may be mentioned peptide~ having the following peptide sequences a~ llsted in the accompanying sequence ll~tlng:
(a) (NH2) (SEQ ID. NO: 65)(0H) or (NH2) (Magalnin I) (b) (NH2) (SEQ ID. NO: 66)(0H) or (NH2) (Magalnin II) (c) (NH2) (SEQ ID. NO. 67)(OH) or (NH2) (Magainin III) The following are example~ of peptide derivatives or analogues:
(d) (NH2) (SEQ ID. NO: 6a) (OH) or (NH2) (e) (NH2) (SEQ ID. NO: 69) (OH) or (NH2) -20- 2~35959 (f) (NH~) (SEQ ID. NO: 70) (OH) or (NH2) Maqainin peptides are described in Proc. Natl. Acad. Sci., Vol. 84, pg~. 5449-53 (Auq. 87). The term "magainin peptides~' as used herein refers to the magainin peptides as well a~
derivatives and analogue~ thereof including but not limited to the repre~entative derivatives and analogue~.
A PGLa peptide i8 either PCLa or an analogue or derivative thereof.
The PCLa peptides generally include at least seventeen amino acids and may include as many a~ forty amino acid~.
An XPF peptide i~ either X~F or an analogue or derivative thereof. The XPF peptides generally include at least nineteen amino acids and may lnclude up to forty amino acids.
A~ representative examplo~ of PG~a and XPF peptides, there may be mentioned the following peptide ~equences as well as appropriate analogue~ and derivatives thereof:
PGLa: (SEQ ID NO: 71) (NH2) XPF: (SEQ ID NO: 72) A review of XPF and PG~a can bs found in Hoffman, et al., EMBO J., 2:711-714 (1983); Andreu, et al., J. Biochem, 149:531-535 (1985); Gibson, et al., J. ~iol. Chem., 261:
5341-5349 (1986); and Glovanninl, et al., 8iochem J., 243:113-120 (19~7).
A CPF peptide i~ either a CPF peptide or an analogue or derlvative thereof. In general, a CPF peptide doe~ not include more than 40 amino acld~.
Repre~ontatlve example~ of CPF peptide~ which may be employed ln comblnatlon with the peptldes of the pre~ent lnvention, ~ome of which have been de~cribed in the literature, include the following ~equences:
~ I) (SEQ ID NO: 73) (II) (SEQ ID ~0: 74) (III) (SEQ ID NO: 75) (IV) (SEQ ID NO: 76) (V) (SEQ ID N0: 77) (VI~ (SEQ ID N0: 78) (VII) (SEQ ID N0: 79) (VIII) (SEQ ID N0: aO) (IX) (SEQ ID N0: 81) (X) (SEQ ID N0: 82) (XI) (SEQ ID N0: 83) (XII) (SEQ ID N0: 84) (XIII) (SEQ ID N0: 85) The above i9 expressed as single letter code for amino acid~.
A review of the CPF peptides can be found in Richter, K., Egger, R., and Kreil (1986) J. Biol. Chem. 261, 3676-3680;
Wakabayashi, T. Kato, H., and Tachibaba, S. (1985) Nucleic Acids Re~earch 13, 1817-1828; Gibson, B.W., Poulter, L., William~, D.R., and Maggio, J.E. (19~6) J. Biol. Chem. 261, 5341-5349.
The term cecropins includes the ba~lc ~tructure as well as analogue~ and derivatives thereof. The cecropins and analogues and derivatives thereof are described in Ann. Rev. Microbiol.
l9a7, Vol. 41, pages 103-26, in particular page 108, and in Christen~en, et al., PNAS Vol. 85, pgs. 5072-76, which are hereby incorporated by reference.
The term sarcotoxins includes the basic materials as well as analo~ues and derivatlve~ thereof. The sarcotoxinq and analo~ues and derivatlves thereof are described in Molecular Entomology, page~ 369-78, ln partlcular page 375, Alan R. liss, Inc. ~19~7), whlch 1~ horeby lncorporated by reference.
Ion channel-formlng proteins or peptldes which may be employed in comblnation wlth the peptlde~ of the pre~ent invention lnclude defensins, also known as human neutrophil antimlcroblal poptides (HNP), major basic protein (MaP) of eoslnophil~, bacterlcldal permeabillty-lncreaslng proteln (~PI), and a pore-formlng cytotoxln called varlously perforln, cytolysln, or pore-forming protein. Defensins are descrlbed in 203~9~9 -~2-Selsted, et al., J. Clin. Invest., Vol. 76, pgs. 1436-1439 ( 19~5 ) . MBP proteins are described in Wasmoen, et al., J. Biol.
Chem., Vol. 263, pg~ 12559-12563. (1988). BPI proteins are de~cri~ed in Ooi, et al, J. Biol. Chem., Vol. 262, pgs.
14891-14894 ( 1987). Perforin is de~cribed in Henkart, et al., J.
E;XD, Med., 160: 75 (19B4), and in Podack, et al., J. ~x~. Med., 160:695 (1984). The above artlcles are hereby lncoroporated by reforence.
The term lon channel-forming protein~ lnclude~ the basic structures of the lon-forming protein~ a~ well as analogue~ and derivatives.
The invention will now be further described with respect to the following examples; however, the scope of the present inventlon is not to be limited thereby.
Example 1 - Antlbacterial Assav The procedure for the following antibacterial as~ay is ba~ed upon the guidelines of the National Commlttee for Clinlcal Laboratory Standard~, Document M7-T2, Volume 8, No. 8, 1988.
Stock solution~ of the following Peptides (SEQ ID N0: 1) through (SEQ ID NO: 64) in accordance wlth the present invention are preparod at a concentratlon of 512 ~g/ml ln sterile deion~zed distilled water and storod at -70C.
Peptide (lA) is of tho same ~tructural formula ao Peptide (SEQ ID NO: 1), except that oach amlno acid re~idue 1`~ a D-amlno acld reJ{duo.
The ~tock peptlde oolutlon i9 dlluted in ~erlal dllutlons (1:2) down the well~ of a mlcrotlter plate 80 that the flnal concentratlons of poptido~ in the wells are 0.25, 0.50, 1, 2, 4, 8, 16, 32, 64, 128, and 256 ~g/ml. 1-5 X 105 CFUs/ml of either S. aureus ATCC 25923, E. coli ATCC 25922, or P. aerualno~a ATCC
27853 were added to the woll~ ln ull strength Muoller Hlnton broth ~BBL 11443) from a mld-log culture. The inoculum 18 standarlzed spectrophotometrlcally at 600nm and 18 verlfled by colony counts. Tho plate~ are lncubated for 16-20 hour~ at 37C, -23- 2~3~9~

and the minimal inhibitory concentration (MIC) for each peptide iQ determined. Minimal inhibitory concentration i~ defined as the lowe~t concentratlon of peptide whlch produce~ a clear well in the microtiter plate. The result~ are given in Table I below.
For purpose~ of explanation of Table I below, S i9 the M~C
of the peptide again~t S.aureus, P ls the MIC of the peptide against P.aeru~inosa, and E i9 the MIC of the peptide against E.col~.
.
TABLE I
MIC (~ml) S P E
(SEQ ID N0:1) 4,8 16,32 2,4 (lA) 2,4 32 2 (SEQ ~D N0:2) 8,16 64 2,4 (SEQ ID N0:3) 256 64 32 (SEQ ID NO:4) 16 32 8 (SEQ ID N0:5) 32 32 4,16 ~SEQ ID N0:6) 128 256 256 (SEQ ID NO:7) 128 >256 256 (SEQ ID NO:8) 8 12B 16 (SEQ ID NO:9) 16 32 8,16 (SEQ ID NO:10) 32 >256 64 (SEQ ID N0:11) 16,32 64,128 8 (SEQ ID NO:12) 32 16,32 8 (SEQ ID NO:13) 32 64 16 (SEQ ID NO:14) 32 64 16 (SEQ ID N0:15) 4,8 8 4,8 (SEQ ID N0:16) 16 32 4 ~SEQ ID N0:17) 16 64 16 (SEQ ID N0:18) 4,8 32,64 4 (SEQ ID N0:19) 16 64 4,8 (SEQ ID N0:20) 8 32 2,4 (SEQ ID N0:21) 128,256 128 32 (SEQ ID N0:22) 128 128 8 -24- 2~359~

(SEQ ID NO:23) 32,64 64 32 (SEQ ID N0:24) 32 64 32 (SEQ ID NO:25) 128 128 16 (SEQ ID NO:26) 128 >256 256 (SEQ ID N0:27) 32 64 4 (SEQ ID NO:28) 128 128 32 (S~Q ID N0:29) 32 64,128 8 (SEQ ID N0:30) 16 64,128 8 (SEQ ID N0:31) 2S6 256 32 (SEQ ID NO:32) 64,128 128 32 (SEQ ID N0:33) 64 128 4 ~SEQ ID NO:34) 32 64 8 ~SEQ ID N0:35) 32 128 8,16 ~SEQ ID N0:36) 32 64 8,16 (SEQ ID NO:37) 4,8 16,32 2,4 (SEQ ID N0:38) 8 16 2 ~SEQ ID NO:39) 16 64,128 8 (SEQ ID N0:40) 4,8 32,64 4 ~SEQ ID N0:41) 64 >256 12B
(SEQ ID NO:42~ 16 256 64 (SEQ ID N0:43) 4 8 2 (SEQ ID NO:44) 16 64 4 (SEQ ID N0:45) 16 64 8 (SEQ ID N0:46) 4 32,64 4 (SEQ ID N0:47) 4,8 128 8 (SEQ ID NO:48) 32 16 4,8 (SEQ ID N0:49) 64 64 8 (SEQ ID NO:50) 2,4 32 2 (SEQ ID N0:51) 16 32 8,16 (SEQ ID N0:52) 16 64 4 (SEQ ID N0:53) 16 32 4 (SEQ ID NO: 54) 16 32 4 (SEQ ID NO:55) B 32 2,4 (SEQ ID N0:56) 4 64 4,8 2~3~9~9 -2s-(SEQ ID N0:57) 8 128 4,8 ~SEQ ID N0:58) 8 128 8 (SEQ ID N0:59) 16 32 2 (SEQ ID N0:60) 4 16 4 (SEQ ID N0:61) 32 12a,256 8,16 (SEQ ID No:62) 16 128 a (SEQ ID N0:63) 16 128 4,8 (SEQ ID N0:64) 16,32 32,64 8,16 ExamPle 2 - AntiDarasitic Assav Logarlthmic phase axenic culture~ of Acanthamoeba polYphaqa trophozoites were grown at 30C in fluid ppyg medium (2%
proteose-peptone; O.S% yeast extract; 0.5% glucose; pH 7.2).
Cell~ were counted uslng a Coulter counter, and added to fresh ppyg medium to give a cell concentration of approximately 10,000 amoebas/ml. Cell suspensions were then tran~ferred to Corninq ~issue culture flasks (25 cm3) to which either Peptide (SEQ ID
N0:1) or Peptlde (SEQ ID N0:43) had been added to appropriate concentrations, wlth each fla~k containinq lOml of medium. The flasks were lncubated at 30C. 0.5ml samples were removed from the flasks, generally over a 5-day period, for countlnq in a Coulter Counter.
For determination of Mlnimum Inhibltory Concentration (MIC) and Minimum Amoebicidal Concentration (MAC) of the trophozoites, the contents of appropriate fla~ks were centrifuged, wa~hed free of "old" medium and peptide with dilute ~aline, re~uspended in re~h ppyg medium, and transferred to Corning ti~sue culture tube~ (16 X 125mm). Tho tubes were lncubated at 30C, and examined at dsily intervals for qrowth of amoebas. Minimum Amoeblcidal ConcQntrstion i~ defined is the minimum concentration of peptide nece~sary to klll the trophozoite~, The re~ult~ aro glven in Table II bolow.

~03~3~9 TABLE II
AntiParasitic ActivitY Aq~inqt Acanthamoeba po 1 Yphaqa TroDhozoites Peptide MIC MAC
(SEQ ID N0:1) 20 25 ( SEQ ID NO: 43 ) 25 40 The peptides of the pre~ent invention, whether administered alone or ln combinatlon with agents such as toxic ions, antlbotlcs, or other biologlcally active peptides or proteins as hereinabove described, may be employed in a wide variety of pharmaceutical compoqition3 in combination with a non-toxic pharmaceutlcal carrier or vehicle such as a flller, non-toxic buffer, or physlological ~aline solution. Such pharmaceutical compositions may be used topically or sy~temically and may be in any sultable form ~uch as a liquid, solid, semi-solid, injectable solutlon, tablet, olntment, lotion, paste, capsule or the like.
The peptide and/or agent as hereinabove described may also be uJed in combinatlon with adjuvant~, protea~e inhibitor~, or compatible drugs where such a combinatlon is seen to be desirable or advantageous in controlling infection caused by harmful microorganisms including protozoa, virusea, parasltes, fungi, and the llke.
The peptide may be administerd to a host in particular an anlmal, in an effectlve antibiotic and/or anti-tumor and/or antiviral and/or antlmlcroblal and/or antlspermicidal and/or antifungal and/or antlparasltic amount, or in an amount effective to stlmulate wound heallng in a host The peptides may be admlnlsterd either alone or ln comblnatlon wlth a toxlc lon, antibiotic, or ion channel formlng peptlde or protein as hereinabove descrlbed. When the peptlde is admlnistered ln combination with a toxlc lon, the activity of the peptide 19 potentiated.

203~3.~i~

When the peptide is admini~tered in combination with an agent a~ hereinabove described, it i~ possible to administer the peptide and agent in separate forms. For example, the agent may be administered systemlcally and the peptide may be admlnistered topically When the peptide is adminltered toplcally, lt may be administered in comblnation with a water-~oluble vehicle, ~aid water-qoluhle vehlcle belng in the form of an ointment, cream, lotion, paste or the like. Examples of water-soluble vehicles which may be employed include, but are not limited to, glycols, ~uch as polyethylene qlycol, hydroxycellulose, and KY Jelly. The water-soluble vehicle is preferably free of an oily substance.
The peptide may also be employed in combination with a toxic ion as hereinabove de~cribed in the form of an oral compo~ition for oral hygiene. Such a composition may be incorporated into a wlde variety of compo~ition~ and materials used for oral hygiene purpo~eE, which include, but are not limited to, toothpastes, mouthwashes, tooth gels, and tooth powders. Such composition may thus be used to treat or prevent perlodontal disease, to prevent or reduce plaque, and/or to prevent or treat or reduce dental caries. The peptide and toxic ion may be used to inhibit, prevent, or destroy the growth of StreDtococcus mutans, which is associated with dental caries and periodontal disease.
Numerou~ modlficatlons and varlatlon~ of the pre~ent invention ar~ po~clblo ln llght of the above teachings and, thoroforo, wlthin tho ~cope of the accompanying claims, the invontion may be practiced other than as particularly described.

2~3~9~9 SEQUENCE LISTING

(1) GENERAL ~NFORMATION:
(i) APPLICANT: Berkowitz, ~arry A.
Kari, U. Pra~ad Maloy, W. Lee (ii) TITLE OF INVENTION: Novel Peptide Compositions and U~e~ Therefore (11i) NUMBER OF SEQUENCES: 85 (iv) CORRESPONDENCE ADDRESS:

(A) ADDRESSEE: Carella, Byrne, Bain, Gilfillan, Cecchi & Stewart (B) STREET: 6 Becker Farm Road (C) CITY: Ro~eland (D) STATE: New Jersey (E) COUNTRY: USA
(F) ZIP: 07068 (v) COMPUTER READABLE FORM:
(A) MEDIUM TYPE: 3.5 inch diskette (B) COMPUTER: IBM PS/2 (C) OPERATING SYSTEM: PC-DOS
(D) SOFTWARE: DW4.V2 (vll) PRIOR APPLICATION DATA:
(A) APPLICATION NUMBER: US 07476629 (B) FILING DATE: 08-FEB-1990 2~3~

(viii) ATTORNEY/ACENT INFORMATION:
(A) NAME: Olstein, Elliot M.
(B) REGISTRATION NUMBER: 24,025 (C) REFERENCE/DOCKET NUMBER: 421250-122 (ix) TELECOMMUNICATION INFORMATION:
(A) TELEPHONE: 201-994-1700 (B) TELEFAX: 201-994-1744 (2) INFORMATION FOR SEQ ID NO:l ~i) SEQUENCE CHARACTERISTICS
~A) LENGTH: 21 amlno acids ~B) TYPE: amino acid ~D) TOPOLOGY: llnear (li) MOLECULE TYPE: peptide (ix) FEATURE:
(D) OTHER INFORMATION: amlde-terminated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:l:
Lys Ile Ala Gly Lys Ile Ala Ly~ Ile Ala Gly Ly~ Ile Ala Lys Ile Ala Cly Ly~ Ile Ala (2) INFORMATION FOR SEQ ID NO:2 (1) SEQUENCE CHARACTERISTICS:
(A) LENGTH: 21 amino acld~
(B) TYPE: amino acid (D) TOPOLOGY: llnear (ii) MOLECULE TYPE: peptide (ix) FEATURE:
(~) OTHER INFORMATION: amide-terminated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:2:
Ly~ Ile Ala Ly~ Ile Ala Cly Lys Ile Ala Ly~ Ile Ala Gly Lys Ile Ala Lys ~le Ala Gly (2) INFORMATION FOR SEQ ID NO:3 (i) SEQUENCE CHARACTERISTICS:
(A) LEN~TH: 21 amino acid~
(B) TYPE: amino acid (D) TOPOLOCY: linear (il) MOLECULE TYPE: peptido (ix) FEATURE:
(D) OTHER INFORMATION: am1de-terminated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:3:
Ly~ Ile Ala Gly Ly~ Ilo Cly Ly~ Ile Ala Cly Lys Ile Gly Ly~ Ile A1A Cly Ly~ Ilo ~ly (2) INFO~MATION FOR SEQ ID NO:4 ~i) SEQUENCE CHARACTERISTICS
(A) LENCTH: 21 amlno acld~
(B) TYPE: amino acld (D) TOPOLOCY: l,near (ii) MOLECULE TYPE: peptide 2~3~

(ix) ~EATURE:
(D) OTHER INFORMATION: amide-terminated txl) SEQUENCE DESCRI PT I ON: SEQ ~D NO:4:
Ly~ Leu Ala Gly Ly~ Leu Ala Lys Leu Ala Gly Ly~ Leu Ala Ly~ Leu Ala Gly Lys Leu Ala (2) INFORMATION FOR SEQ ID NO:5 (1) SEQUENCE CHARACTERISTICS
(A) LENGTH: 21 amlno aclds (B) TYPE: amino acid (D) TOPOLOCY: linear (il) MOLECULE TYPE: peptlde (ix) FEATURE:
(D) OTHER INFORMATION: amide-terminated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:5:
Ly~ Pho Ala ~ly Lys Phe Ala Ly~ Phe Ala aly Lys Phe Ala Lys Phe Ala Gly Lys Phe Ala (2) INFORMATION EOR SEQ ID NO:6 (i) SEQUENCE C~ARACTE~ISTICS
(A) LENCTH: 21 amino acids ( B ) TYPE: ~mlno acld (D) TOPOLOGY: linear 2~3~9 (ii) MOLECULE TYPE: peptide (ix) FEATURE:
(D) OTHER INFORMATION: amide-terminated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:6:
Lys Ala Leu Ser Lya Ala Leu Lys Ala Leu 5er Lys Ala Leu Ly~ Ala Leu Ser Lys Ala Leu (2) INFORMATION FOR SEQ ID NO:7 (~ SEQUENCE CHARACTERISTICS
~A) LENGTH: 21 amlno aclds (B) TYPE: amino acld (D) TOPOLOGY: llnear (ii) MOLECVLE TYPE: peptlde (~x) FEATURE:
(D) OTHER INFORMATION: amide-terminated (xl) SEQUENCE DESCRI PT I ON: SEQ ID NO:7:
Ly~ Leu Leu Ly Ala Leu Cly Ly~ Leu Leu Ly~ Ala Le~ Gly Ly~ Leu Leu LYB Ala Leu Gly (2) INFORMATION FOR SEQ ID NO:a (1) SEQUEN OE CHARACTERISTICS
(A) LENGTH: 21 amino aclds (B) TYPE: amino acld _33_ 203~9:~9 (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE:
(D) OTHER INFORMATION: am~de-terminated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:~:
Lyo Ala Ilo Cly Lys Ala Ile Lys Ala Ile Gly Lyo Ala Ile Lys Ala Ile Gly Lys Ala Ile (2) INFORMATION FOR SEQ ID NO:9 (1) SEQUENCE CHARACTERISTICS
(A3 LENGTH: 21 smino acids (B) TYPE: amlno acid tD) TOPOLOCY: linear (ii) MOLECULE TYPE: peptido (ix) FEATURE~
(D) OTHER INFORMATION: amide-torminated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:9:
Cly Ilo Ala Lyo Ilo Ala Lya Cly Ilo Ala Lys Ilo Ala Ly~ Cly Ile Ala Ly~ Ile Ala Lys ~2) INFORMATION FOR SEQ ID NO:10 (i) SEQUENCE CHARACTERISTICS

_34_ 2~3~9 (A) LENGTH: 21 amlno acid~
(8) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE:
(D) OTHER INFORMA.ION: amide-terminated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:10: ys Ile Ala Lys Ile Phe Gly Ly~ Ile Ala 10 y~ Phe Cly Lys Ile Ala Lys Ile Phe 2 ly 2) INFORMATION FOR SEQ ID NO:ll (1) SEQUENCE CHARACTERISTICS
(A) LENCTH: 21 amlno acid~
(B~ TYPE: amino acid (D) TOPOLOCY: llnear (ii) MOLECULE TYPE: peptide (1x) FEATURE:
(D) OTHER INFORMATION: amide-termlnated (xl) SEQUENCE DESCRIPTION: SEQ ID NO:ll: ly Ile Ala Arg Ile Ala Lys Cly Ile Ala 10 rg Ilo Ala Ly~ Gly Ilo Ala Arg Ile Ala lS 20 y~

(2) INEORMATION FOR SEQ ID NO:12 _35_ 2~3~359 (i) SEQUENCE CHARACTER-STICS
(A) LENGTH: 21 amino acid~
(B) TYPE: amino acid (D) TOPOLOCY: linear (ii) MOLECULE T~PE: peptide (ix) FEATURE:
(D) OTHER INFORMATION: amide-terminated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:12: y~ Phe Ala Arg Ile Ala Gly Lys Phe Ala S 10 rg Ilo Ala Cly Lys Phe Ala Arg Ile Ala 20 ly 2) INFORMATION FOR SEQ ID NO:13 (i) SEQUENCE CHARACTERISTICS
(A) LENGTH: 21 amino acids (B) TYPE: amlno acid (D) TOPOLOGY: linear (il) MOLECULE TYPE: peptide ~ix) FEATURE:
(D) OTHER INFORMATION: amide-torminated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:13: ly Phe Ala Lys Ile Ala LYB Gly Phe Ala 10 y~ Ila Ala Ly~ Gly Phe Ala Ly~ Ile Ala Ly8 -36- 203~939 (2~ INEORMATION FOR SEQ ID NO:14 (i) SEQUENCE CHARACTERIST~CS
(A? LENGTH: 21 amino acid~
(~) TYPE: amino acid (D) TOPOLOGY: linear (il) MOLECULE TYPE: peptlde (ix) FEATURE:
(D) OTHER INFORMATION: amide-terminated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:14: y~ Ile Ala Gly Orn Ile Ala Ly~ Ile Ala 10 ly Orn Ile Ala Lys Ile Ala Gly Orn Ile 20 la 2) INFORMATION FOR SEQ ID NO:15 (i) SEQUENCE C~ARACTERISTICS
(A) LENCTH: 21 amlno acid~
( B ) TYPE: amino acid (D) TOPOLOCY: llnear (ii) MOLECULE TYPE: peptide (lx) EEATURE:
(D) OTHER INFORMATION: amide-terminated (xl) SEQUENCE DESCRIPTION: SEQ ID NO:15: ys Ile Ala Arg Ile Ala Gly Lys Ile Ala 10 rg Ile Ala Gly Lys Ile Ala Arg Ile Ala S 20 ly _37_ 2~3~959 (2) INFORMATION FOR SEQ ID NO:15 (i) SEQUENCE C~ARACTERISTICS
(A) LENGTH: 21 amino acids (B) TYPE: ~mino acid (D) TOPOLOCY: linear (ii) MOLECULE TYPE: peptlde (ix) FEATURE:
(D) OTHER INFORMATION: amide-terminated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:16:
Orn Ilq Ala Gly Lys Ile Ala Orn Ile Ala Gly Ly~ Ile Ala Orn Il~ Ala Gly Ly~ Ile Ala (2) INFORMATION FOR SEQ ID NO:17 (i) SEQUENCE CHARACTERISTICS
(A) LENGTH: 21 amino acid~
~B) TYPE: amlno acid (D) TOPOLOGY: linear (il) MOLECULE TYPE: peptide (lx) FEATURE:
(D) OTHE~ INFORMATION: amlde-terminated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:17:
Gly Ile Ala Arg Ile Phe Ly~ Gly Ile Ala _3~_ 2~3J3~

Arg Ile Phe Lys Gly Ile Ala Arg Ile Phe Ly~
(2) INFORMATICN FOR SEQ ID NO:18 (i) SEQUENCE CHARACTERISTICS
(A) LENGTH: 21 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide ( i x ) FEATURE:
(D) OTHER INFORMATION: amide-terminated ~xi) SEQUENCE DESCRIPTION: SEQ ID NO:18:
Ly~ Nle Ala Gly Lys Nle Ala Lys Nle Ala Cly Ly~ Nl~ Ala Lys Nls Ala Gly Ly~ Nle Ala (2) INFORMATION FOR SEQ ID NO:l9 (i) SEQUENC~ CHARACTERISTICS
(A) LENGTH: 21 amino acid~
(B) TYPE: amino acid (D) TOPOLOCY: lln~ar (ii) MOLECULE TYPE: peptld~

(ix) FEATURE:
(D) OTHER INFORMATION: amide-termlnated _39_ 2~5~9 (xi) SEQUENCE DESCRIPT~ON: SEQ ~D NO:l9: ys Nle Ala Gly Ly~ Ile Ala Lys Nle Ala 10 ly Lys Ile Ala Lys Nle Ala Gly Lys Ile 20 la (2J INFORMATION FOR SEQ ID NO:20 ~1) SEQUENCE CHARACTERISTICS
(A) LENGTH- 21 amino acid~
~B) TYPE: amlno acid (D) TOPOLOGY: llnear (li) MOLECULE TYPE: peptlde (ix~ FEATURE:
(D) OTHER INFORMATION: amlde-terminated (xl) SEQUENCE DESCR~PTION: SEQ ID NO:20: y~ Ile Ala Gly Ly~ Nle Ala Ly~ Ile Ala 10 ly Ly~ Nle Ala Ly~ Ile Ala Gly Lys Nle 20 la 2) INFORMATION FOR SEQ ID NO:21 (1) SEQUENCE CHARACTERISTICS
(A) LENGTH: 21 amino aclds TYPE: amlno acld ~D) TOPOLOGY: llnear (ii) MOLECULE TYPE: peptide ~x) FEATURE:
(D) OTHER INFORMATION: amide-termlnated _40_ 2~3 ;~9 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:21: ys Nva Ala Cly Lys Nva Ala Ly~ Nva Ala 10 ly Ly~ Nva Ala Ly~ Nva Ala Gly Ly~ Nva 1~ 20 la 2) INFORMATION FOR SEQ ID NO:22 ~i) SEQUENCE CHARACTERISTICS
(A) LENGTH: 21 amino acid~
(B) TYPE: amino acid (D) TOPOLOGY: linear (ii~ MOLECULE TYPE: peptlde (ix) FEATURE:
(D) OTHER INFORMATION: amide-terminated ~xl) SEQUENCE DESCRIPTION: SEQ ID NO:22: y~ Nva Ala Gly Lys Ile Ala Lys Nva Ala 10 ly Lys Il~ Ala Lys Nva Ala Gly Ly3 Nva 20 la (2) INFORMATION FOR SEQ ID NO:23 (1) SEQUENCE CHARACTERISTICS
(A) LENGTH: 21 amlno acid~
~B) m E: amino acld (D) TOPOLOGY: llnoar (l~) MOLECULE TYPE: p~ptldo (lx) FEATURE:
(D) OTHER INFORMATION: amldo-termlna~ed -41- 203~9 ~xi) SEQUENCE DESCRIPTION: SEQ ID NO:23: y~ Leu Leu 5er Ly~ Leu Cly Lys Leu Leu 10 er LyY Leu Gly Ly~ Leu Leu Ser Lys Leu 20 ly 2~ rNFORMATION FOR SEQ ID NO:24 (i) SEQUENCE CHARACTERISTICS
~A) LENCTH: 21 amino acids (8) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE:
(D) OTHER INFORMATION: amide-terminated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:24: y~ Leu Leu Ser Lys Pho Gly Lys Leu Leu 10 er Lys Phe Gly Lys Leu Leu Ser Ly~ Phe 20 ly (2) INFORMATION FOR SEQ ID NO:25 (i) SEQUENCE CHARACTERISTICS
(A) LENCTH: 21 amino ncid~
(L) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE:
(D) OTHER INFORMATION: amide-terminated 2~3~g~9 (xi~ SEQUENCE DESCR~PTION: SEQ ID NO:25:
Lys Ile Al~ Gly Lys Nva Ala Lys Ile Ala Gly Ly~ N~ Ala Ly~ Ile Ala Gly Ly~ Nva Ala (2) INFO~'ATION FOR SEQ ID NO:26 ~i) SJQUENCE CHARACTERISTICS
(P) LENGTH: 21 amlno acid~
(~) TYPE: amino ac~d (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE:
(D) OTHER INFORMATION: amide-terminated ~xi) SEQUENCE DESCRIPTION: SEQ ID NO:26:
His Ile Ala Cly His Ilo Ala Hi~ Ile Ala Gly His Ile Ala Hi~ Ile Ala Gly Hi~
Ala (2) INFORMATION FOR SEQ ID NO:27 (i) SEQUENCE CHARACTERISTICS
(A) LENGTH: 21 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (il) MOLECULE TYPE: poptide (ix) FEATURE:
(D) OT~ER INFORMATION: amide-terminated 2 0 3 ~ 9 , 9 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:27:
Ala Gly Ly8 I le Ala Ly~ lle Ala Cly Ly~

Ile Ala Ly~ Ile Ala Gly Ly~ Ile Ala Lys Ile (2) INEORMATION FOR SEQ ID NO:28 (1) SEQUENCE CHARACTERISTICS
(A) LENCTH: 21 amino acid~
(B) TYPE: amino acld (D) TOPOLOGY: llnear (ii) MOLECULE TYPE: peptide (lx) FEATURE:
(D) OTHER INFORMATION: amide-termlnated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:28:
Ilo Ala Ly~ Ile Ala Cly Lys Ile Ala Ly8 Ile Ala Gly Lys Ile Ala Ly~ Ile Ala Gly Ly~
(2) INFORMATION FOR SEQ ID NO:29 (1) SEQUENCE CHARACTERISTICS
(A) LENCTH: 21 amino acid~
(L) TYPE: amlno acid (D) TOPOLOGY: llnear ~li) MOLECULE TYPE: peptlde (lx) FEATURE:
(D) OTHER INFORMATION: amide-terminated _44_ ~3~

( x i ) S EQUENCE DE SC RIPTION: SEQ ID NO:29:
Ly~ Ile Ala Gly Arg Ile Ala Lys Ile Ala Cly Arg Ile Ala Lys Ile Ala Gly Arg Ile Ala ~2) INEORMATION FOR SEQ ID NO:30 (1) SEQUENCE CHARACTERISTICS
(A) LENGTH: 21 amino acid~
(B) TYPE: amino acld (D) TOPOLOGY: linear (11) MOLECULE TYPE: peptide (ix) FEATURE:
(D) OTHER INFORMATION: amlde-terminated (xl) SEQUENCE DESCRIPTION: SEQ ID NO:30:
Arg Ilo Ala Gly Arg Ile Ala Arg Ile Ala Gly Arg Ile Ala Arg Ile Ala Gly Arg Ile Ala (2) INFORMATION EOR SEQ ID NO:31 (i) SEQUENCE CHARACTERISTICS
(A) LENOTH: 21 amino acld~
(a) TYPE: amlno acid tD) TOPOLOGY: linoar (11) MOLECULE TYPE: peptlde (1x) FEATURE:
(D) OTHER INFORMATION: amldo-termlnated ~3'~-9~ ~

(xi) SEQUENCE DESCRIPTION: SEQ ID NO:31:
Ly~ Val Ala Gly Ly~ Ile Ala Ly~ Val Ala Cly Ly~ Ile Ala Ly-~ Val Ala Gly Ly~ Ile Ala (2) INFORMATION FOR SEQ ID NO:32 (i) SEQUENCE CHARACTERISTICS
(A) LENGTH: 21 amino acid~
(B) TYPE: amlno acld (D) TOPOLOGY: linear (1i) MOLECULE TYPE: peptide (lx) FEATURE:
~D) OTHER INFORMATION: amlde-terminated (xl) SEQUENCE DESCRIPTION: SEQ ID NO:32:
Ly~ Ile Ala Gly Ly~ Val Ala Ly~ Ile Ala Gly Ly~ Val Ala Lya I 18 Ala Cly Lys Val Ala (2) INFORMATION FOR SEQ ID NO:33 (1) SEQUENCE CHARACTERISTICS
(A) LENGTH: 21 amlno acld~
1 B ) TYPE: amino acld (D) TOPOLOGY: llnear (11) MOLECULE TYPE: peptide (ix) FEAT~RE:
(D) OTHER INFORMATION: amide-terminated 2~3~9 (xi) SEQUENCE D~SCRIPTrON: SEQ ID NO:33:
Ala Lys I le Ala Gly Lys Ile Ala Lys I le Ala Gly Ly~ Ile Ala Lys Ile Ala Gly Lys Ile ~2) INFORMATION FOR SEQ ID NO:34 ~1) SEQUENCE CHARACTERISTICS
~A) LENGTH: 21 amino acids ~B) TYPE: amino acid (D) TOPOLOGY: linear (il) MOLECULE TYPE: peptide (ix) FEATURE:
(D) OTHER INFORMATION: amlde-terminatod (xi) SEQUENCE DESCRIPTION: SEQ ID NO:34:
Orn Ilo Ala Gly Orn Ilo Ala Orn Ilo Ala Gly Orn Ile Ala Orn Ile Ala Gly Orn Ile Ala (2) INFORMATION FOR SEQ ID NO:35 (i) SEQUENCE CHARACTERISTICS
(A) LENGTH: 21 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear ( 11 ) MOLE;CULE TYPE: p~ptid~

(ix) FEATU~E:

_47_ 2~

(D) OTHER INFORMATION: amide-terminated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:35:
Lya Phe Ala Gly Lys Ile Ala Lys Phe Ala Gly Lys Il~ Ala Ly~ Phe Ala Cly Lys Ile Ala (2) INFORMATION FOR SEQ ID NO:36 11) SEQUENCE CHARACTERISTICS
(A) LENGTH: 21 amino acid~
(a) TYPE: amino acid (D) TOPOLOGY: linear (li) MOLECULE TYPE: p~ptide ( i x ) FEATURE:
(D) OTHER INFORMATION: amlde-terminated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:36:
Lya Ilo Ala Cly Lys Phe Ala Lys Ile Ala Cly Ly- Pho Ala Ly~ Ilo Ala Gly Lya Ph~
Ala (2) INFORMATION FOR SEQ ID NO:37 (1) SEQUENCE CHARACTERISTICS
(A) LENGTH: 21 amino acida (B) TYPE: amino acid (D) TOPOLOCY: llnear (li) MOLECULE TYPE: peptide 2~35959 ~ix) ~EATURE:
~D) OTHER INFORMATION: amide-terminated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:37:
Ly~ Cha Ala Gly Lys Ile Ala Lys Cha Ala Gly Lys Ile Ala Ly~ Cha Ala Cly Lys r le Ala (2) INFORMATION FOR SEQ ID NO:38 (1) SEQUENCE CHARACTERISTICS
(A) LENCTH: 21 amino acid~
(B) TYPE: amino acid (D) TOPOLOCY: linear (ii) MOLECULE TYPE: peptido ( 1 x ~ FEATURE:
(D) OTXER INFORMATION: amide-terMinated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:38:
Ly~ Nle Ala Lys Ile Ala Cly Lys Nle Ala Ly~ I le Ala Gly LYJ Nle Ala Lys Ile Ala aly ~2) INFORMATION FOR SEQ ID NO:39 (~) SEQUENCE CXARACTERISTICS:
(A) LE~CT~: 21 amino aclds ~B) TYPE: amino acld (D) TOPOLOGY: linear 2~3~

(ii) MOLECULE TYPE: peptide (ix) FEATURE:
(D) OTHER INFORMATION: amlde-termlnated (xi) SEQUENCE DESCRIPTION: SEQ lD NO:39:
Arq Ile Ala Gly Lys Ile Ala Arg Ile Ala Cly Ly~ Ile Ala Arg Ile Ala Gly Ly~ Ile Ala (2) INFORMATION FOR SEQ ID NO:40 ~i) SEQUENCE CHARACTERISTICS:
(A) LENCTH: 21 amino acids ~B) TYPE: amino acid (D) TOPOLOGY: linear (li) MOLECULE TYPE: peptide ~ix) FEATURE:
~D) OTHER INFO~MATION: amlde-termlnated ~xl) SEQUENCE DESCRIP~ION: SEQ ID NO:40:
Har Ile Ala Cly Har Ilo Ala Har Ile Ala Cly Har Ile Ala Har Ile Ala Cly Har Ile Ala (2) INFORMATI ON FOR SEQ I D NO: 41 ( 1 ) SEQUENCE CHA~ACTERISTICS:
(A) LENCTH: 21 amlno acids ~B) TYPE: amlno acld 203~

(D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptlde (ix) FEATURE: amide-terminated, Xaa is p-aminophenylalanine (xl~ SEQUENCE DESCRIPTION: SEQ ID NO:41:
Xaa Ile Ala Gly Ly~ Ile Ala Xaa Ile Ala Cly Lys Ile Ala Xaa Ile Ala Cly Ly~ Ile Ala (2) INFORMATION FOR SEQ ID NO:42 (i) SEQUENCE CHARACTERISTICS:
(A) LENCTH: 21 amlno aclds ~i3) TYPE: amlno acid (D) TOPOLOCY: l1near (ii) MOLECULE TYPE: peptido (ix) FEATURE: amide-terminated, Xaa is p-aminophenylalanine (xi) SEQUENCE DESCRIPTION: SEQ ID NO:42:
Lys Ile Ala Cly Xaa Ile Ala Lys Ile Ala Cly Xaa Ile Ala Lys Ile Ala Gly Xaa Ilo Ala (2) INFORMATION FOR SEQ ID NO:43 (i) SEQUENCE C~ARACTERISTICS
(A) LENCTH: 21 amino acid~
(B) TYPE: amlno acld -51- 2~3~9~

(D) TOPOLOG~: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE:
(D) OTHER INFORMATION: amide-terminated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:43:
Ly~ Leu Ala Ser Lys Ala Gly Lys Ile Ala Gly Lys Ile Ala Lys Val Ala Leu Lys Ala Leu (2) INFORMATION FOR SEQ ID NO:44 (i) SEQUENCE CHARACTERISTICS
(A) LENGTH: 21 amino acid3 (B) TYPE: amino acid (D) TOPOLOCY: llnear (ii) MOLECULE TYPE: peptlde (ix) FEATURE:
(D) OTHER INFORMATION: amide-terminated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:44:
Ly~ Ile Ala Cly Lys Ils Ala Lys Ile Ala Cly Orn Ile Ala Lys Ile Ala Cly Lys Ile Ala (2) INFORMATION FOR SEQ ID NO:45 (i) SEQUENCE CHARACTERISTICS
(A) LENGTH: 21 amino acids (B) TYPE: amino acid 2~3~9~
(D~ TOPOLOCY: linear (11) MOLECULE TYPE: peptlde ( i x ) FEATURE:
(D~ OTHER INFORMATION: amlde-terminated (xl) SEQUENCE DESCRIPTION: SEQ ID NO:45: y~ Ilc Ala Cly Lys Ile Ala Ly~ Ile Ala 10 ly Arg Ile Ala Ly~ Ile Ala Cly Ly~ Ile 20 la (2) INFORMATION FOR SEQ ID NO:46 (1) SEQUENCE CHARACTERISTICS
(A) LENGTH: 21 amino acid~
(B) TYPE: amino acld (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (lx) FEATURE~
(D) OTHER INFORMATION: amlde-termlnated (xl) SEQUENCE DESCRIPTION: SEQ ID NO:46: y~ Ile Ala Gly Ly~ Ile Ala Ly~ Ile Ala 10 ly Nle Ilo Ala Ly~ Ile Ala Cly Ly~ Ile 20 la 2) INFORMATION FOR SEQ ID NO:47 (i) SEQUENCE CHARACTERISTICS
(A) LENCTH: 21 amlno acid~

-53~ a 9 5 ~

( B ~ TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: p~ptlde (ix) FEATURE:
(D) OTHER INFORMATION: amlde-terminated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:47:
Ly~ Ile Ala Gly Lys Ile Ala Lys Ile Ala Gly Nva Ile Ala Ly~ Ile Ala Gly Lys Ile Ala (2) INFORMATION FOR SEQ ID NO:48 (i) SEQUENCE CHARACTERISTICS
(A~ LENGTH: 21 amino acids (B) TYPE: amlno acid (D) TOPOLOGY: linear (il) MOLECULE TYPE: peptido (ix) FEATURE:
(D) Ol~ER INFORMATION: amlde-termlnatod (xi) SEQUENCE DESCRIPTION: SEQ ID NO:48:
Lys Pho Ala Gly Lys Phe Ala Ly~ Phe Ala Gly Orn Phe Ala Lys Phe Ala Gly Lys Phe Ala (2) INFORMATION FOR SEQ ID NO:49 (1) SEQUENCE CHARACTERISTICS

_54_ 2~3~59 (A) LENGTH: 21 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE:
(D) OTHER INFORMATION: amide-terminated (xi~ SEQUENCE DESCRIPTION: SEQ ID NO:49:
Ly~ I le Ala Cly Lys Phe Ala Ly~ Ile Ala Cly Orn Phe Ala Lys Ile Ala Gly Lys Phe Ala (2) INFORMATION FOR SEQ ID NO:50 (i~ SEQUENCE CHARACTERISTICS
(A) LENGTH: 21 amlno acid~
(B) TYPE: amino acid (D) TOPOLOGY: linoar (ii) MOLECULE TYPE: peptido (ix) FEATURE:
(D) OTHER INFORMATION: amide-terminated (xl) SEQUENCE DESCRIPTION: SEQ ID NO:50:
Lys Ile Als Gly Ly~ Nle Ala Ly~ Ile Ala Cly Orn Nlo Ala Lys Ile Ala Cly Lys Nle Ala _55_ 2~35~59 (2) INFORMATION FOR SEQ ID NO:51:
(1) SEQUENCE CHARACTERISTICS
(A) LENaTH: 21 amlno acid~
(8) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (lx) FEATURE:
(D) OTHER INFORMATION: amide-termianted (xi) SEQUENCE DESCRIPTION: SEQ ID NO:51:
Ly~ Met Ala Ser Ly~ Ala Gly Ly~ Ile Ala Gly Ly~ Ile Ala Ly~ Val Ala Leu Ly~ Ala Leu (2) INFORMATION FOR SEQ ID NO:52:
(i) SEQUENCE CHARACTERISTICS
(A) LENGTH: 21 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptlde (ix) FEATURE:
(D) OTHER INFORMATION: amide-terminated (xl) SEQUENCE DESCRIPTION5 SEQ ID NO:52 Ly~ Ala Ser Ly~ Ala Gly Ly~ Ile Ala Oly Ly~ Ile Ala Ly~ Val Ala Leu Ly~ Ala Leu 2 3 3 ~ 9 s~, (2~ INFORMATION FOR SEQ ID NO:53:
(i) SEQUENCE CHARACTE~ISTICS
(A) LENGTH: 21 amino acid~
(B) TYPE: amino acld (D) TOPOLOCY- linear (11) MOLECULE TYPE: peptlde (ix) FEATURE:
(D) OTHER INFORMATION: amide-terminated (xi) SEQUENCE DESCRIPTION: SEO ID NO:53:
Ly~ Ile Ala Ser Ly~ Ala Gly Ly~ Nle Ala Gly Lys Ile Ala Lys Val Ala Leu LYB Ala Leu (2) INFORMAT I ON FOR SEQ ID NO:54:
(i) SEQUENCE CHARACTERISTICS
(A) LENCT~: 21 amlno acids (B) TYPE: amino ac~d (D) TOPOLOGY: llnear (ii) MOLECULE TYPE: poptlde (lx) FEATURE: .
(D) OTHER INEORMATION: amide-terminated (xl) SEQUENCE DESCRIPTION: SEQ ID NO:54:
Ly8 Lou Ala Ser Lys Ala Gly Ly~ Nle Ala _57_ 2~35~9 Gly Ly~ r le Ala Lys Val Ala Leu Lys Ala Leu (2) IN~ORMATION FOR SEQ ID NO:55:
(i) SEQUENCE CHARACTERISTICS
(A) LENGTH: 21 amlno acld~
(B) TYPE: amino acid ~D) TOPOLOGY: Linear (il) MOLECULE TYPE: peptide (ix) FEATURE:
(D) OTHER INFORMATION: amide-terminated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:55:
Lys Nle Ala Ser Lys Ala Gly Ly~ Nle Ala Gly Ly~ Ilo Ala Ly~ Val Ala Leu Lys Ala Leu ~2) INFORMATION FOR SEQ ID NO:56 (1) SEQUENCE CHARACTERISTICS:
( A ) LENG~H: 21 amino acid~
(B) m E: amino acld (D) TOPOLOGY: linear (11) MOLECULE m E: peptlde (lx) FEATURE:
(D) OTHER INFORMATION: amlde-terminated, Xaa i~
p-amlnophenylalanlne.

(xl) SEQUENCE DESCRIPTION: SEQ ID NO:56:

2 ~ 3 ~ 9 3 9 Ly~ Ile Ala Gly Ly-q Ile Ala Ly~ Ile Ala Gly Xaa Ile Ala Lys Ile Ala Cly Lys Ile Ala (2) INFO~MATION FOR SEQ ID NO:57 (i) SEQUENCE CHARACTERISTICS:
(A) LENGTH: 21 amlno acid~
(B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE:
(D) OTHER INFORMATION: amide-terminated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:57:
Ly~ Ile Ala Cly Ala Ile Ala Ly~ Ile Ala 5 . 10 Cly Ly~ Ile Ala Lys ILe Ala Gly Lys Ile Ala (2) INFORMATION FOR SEQ ID NO:5B
(i) SEQUENCE CHARACTERISTICS:
(A) LENGTH: 21 amino acld~
(B) TYPE: amino acid (D) TOPOLOCY: llnear (li) MOLECULE TYPE: pept1de (ix) FEATURE:
(D) OTHER INFORMATION: amlde-termi~ated 203~ ~9 _59_ ~xi) SEQUENCE DESCRIPTION: SEQ ID NO:58:
Lys Ile Ala Cly Lys I le Ala Ly~ Ile Ala Cly Ala Ile Ala Ly~ I le Ala Gly Ly~ Ile Ala ~2) INFORMATION FOR SEQ ID NO:59 (i) SEQUENCE CHARACTERISTICS:
(A) LENCTH: 21 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (lx) FEATURE:
(D) OTHER INFORMATION: amide-terminated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:59:
Lys Ile Ala Gly Lys Ile Ala Lys Ile Ala Gly Ly~ Ile Ala Ly~ Ile Ala Gly Ala Ile Ala (2) INFORMATION FOR SEQ ID NO:60 (1) SEQUENCE CHARACTERISTICS
(A) LENGTH: 21 amlno acids (B) TYPE: amino acid (D) TOPOLOGY: linear (li) MOLECULE TYPE: peptlde (ix) FEATURE:

2~3~5~

(D) OTHER INEORMATION: amide-terminated (xi) SEQU~NCE DESCRIPTION: SQ ~D NO:60:
Lys Ile Ala Lys Ly8 I le Ala Ly~ I le Ala Lys Ly~ Ile Ala Lys Iie Ala Ly~ Lys Ile Ala ~2) INFORMATION FOR SEQ ID NO:61 (i) SEQUENCE CHARACTERISTICS
(A) LENCTH: 21 amino acid~
(B) TYPE: amino acid (D) TOPOLOGY: linear (il) MOLECULE TYPE: peptlde (lx) FEATURE:
(D) OTHER INFORMATION: amlde-termlnated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:61:
Ala Ilo Ala Gly Lys Ile Ala Lys Ile Ala Gly Ly~ Ilo Ala Lys Ilo Ala Gly Ly~ Ile Ala (2) INFORMATION FOR SEQ ID NO:62 (i) SEQUENCE CHARACTERISTICS
(A~ LENGTH: 21 amino ac~ds (B) TYPE: amino acld (D) TOPOLOGY: linoar (11) MOLECULE TYPE: peptlde (lx) FEATURE:

2~3a9~9 (D) OTHER INFORMATION: amide-terminated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:62:
Ly~ I le Ala Cly Lys I le Ala Ala Ile Ala Gly Lys Ile Ala Lys Ile Ala Gly Lys ~le Ala ~2) INFORMATION FOR SEQ ID NO:63 ~i) SEQUENCE CHARACTERISTICS
(A) LENGTH: 21 amino acids (B) TYPE: amino acid (D) TOPOLOGY: llnear (1i) MOLECULE TYPE: peptide (ix) FEATURE:
(D) OTHER INFORMATION: amide-terminated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:63:
Lys Ile Ala Gly Lys Ile Ala Ly~ Ile Ala Gly Ly~ Ile Ala Ala Ilo Ala Cly Ly~ Ile Ala (2) INFORMATION FOR SEQ ID NO:64 (i) SEQUENCE CHARACTERISTICS
(A) LENGTH: 21 amino acid~
~B) TYPE: amino acid (D) TOPOLOGY: linear (11) MOLECULE TYPE: peptide (ix) FEATURE:

203 ~3~

(D) OTHER INFORMATION: amide-terminated (xi) SEQUENCE DESCRIPTION: SEQ ID NO:64:
Gly Met Ala Ser Lys Ala Gly Lys Ile Ala Cly Lys Ile Ala Lys Val Ala Leu Lys Ala Leu ~2) INFORMATION FOR SEQ ID NO:65 (i) SEQUENCE CHARACTERISTICS
(A) LENGTH: 23 amlno acld 9 (B) TYPE: amino acid (D~ TOPOLOGY: linoar (ii) MOLECULE TYPE: poptido ~lx) FEATURE:
~A) NAME/KEY: Magainin I peptide.
~D) OTHER INFORMATION: amide- or carboxy- termlnated ~x) PUBLICATION INFORMATION:
(A) AUTHOR: Za~loff, Michael ~C) JOURNAL: Proceedlna~ of the National Academv of Sclence~
(D) VOLUME: 84 (F) PAGE5: 5449-5453 (C) DATE: AUC - 1987 (H) DOCUMENT NUMBER: US 4810777 (I) FILINC DATE: 04-MAR-1987 ~J) PU~LICATION DATE: 07-MAR-1989 ~3~9 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:65 Gly Ile Gly Ly~ Phe Leu His Ser Ala Gly Ly~ Phe ~ly Lys Ala Phe Val ~ly Glu I le Met Lyq Ser ~2) INFORMATION FOR SEQ ID NO:66 (i) SEQUENCE CHARACTERISTICS
(A) LENGTH: 23 amino acld~
( 8 ) TYPE: amino acid (D) TOPOLOGY: linear (il) MOLECULE TYPE: peptide (ix) FEATURE:
(A) NAME/KEY: Magalnln II peptlde.
~D) OTHER INFORMATION: amlde- or carboxy- terminated (x) PUBLICATION INFORMATION:
(A) AUTHOR: Zasloff, Michael ~C) JOURNAL: Proceedlnas of the National AcademY
of Sclence~
~D) VOLUME: 84 ~F) PAGES: 5449-5453 ~G) DATE: AUG - l9a7 ~H) DOCUMENT NUMBER: US 4810777 (I) FILINC DATE: 04-MAR-1987 ~J) PUBLICATION DATE: 07-MAR-1989 ~xl) SEQUENCE DESCRIPTION: SEQ ID NO:66 Gly Ile Gly Lys Phe Leu Hl~ Ser Ala Ly~

2 ~ Y ~) ~

Lys Phe Gly Lys Ala Phe Val Gly Glu Ile Met A~n Ser (2) INFORMATION FOR SEQ ID NO:67 (i) S~QUENCE CHARACTERISTICS
(A) LENCTH: 22 amlno acld~
(~) TYPE: amino acld (D) TOPOLOGY: linear (il) MOLECULE TYPE: peptide (ix) FEATURE:
(A) NAME/KEY: Magainin III peptide.
(D) OTHER INFORMATION: amide- or carboxy- terminated (x) PUBLICATION INFORMATION:
(A) AUTHOR: Zasloff, Michael (C) JOURNAL: Proceodina~ of the Natlonal AcademY
of Sciences (D) VOLUME: 84 (F) PAGES: 5449-5453 (G) DATE: AUG - 1987 (H) DOCUMENT NUMBER: US 4810777 (I) FILING DATE: 04-MAR-1987 (J) PUBLICATION DATE: 07-MAR-1989 (xl) SEQUENCE DESCRIPTION: SEQ ID NO:67:
Cly Ilo Cly Ly~ Pho Leu Hi~ Sor Ala Lys Ly~ Pho Gly Ly~ Ala Pho Val Cly Glu Ile Met Asn ~33~95~

(2) INFORMAT~ON FOR SEQ ID NO:68 (i) SEQUENCE CHARACTERISTICS
(A) LEN~TH: 22 amlno acids (B) TYPE: amino acid (D) TOPOLOCY: linear ~ii) MOLECULE TYPE: peptide (~x~ FEATURE:
(A) NAME/KEY: magainln peptide.
(D) OTHER INFORMATION: amlde- or carboxy- termlnated (x) PUBLICATION INFORMATION:
(A) AUTHOR: Za~loff, Michael (C) JOURNAL: Proceedlna~ of the Natlonal AcademY
of Sci~nces (D) VOLUME: 84 (F) PACES: 5449-5453 (G) DATE: AUG - 1987 (H) DOCUMENT NUM8ER: US 4810777 (I) FILING DATE: 04-MAR-1987 (J) PUBLICATION DATE: 07-MAR-1989 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:68:
Il~ Gly Lys Ph~ L~u Hi~ Ser Ala Ly~ Ly~
Pho Cly Ly~ Ala Phe Val Oly Glu Ilo M~t A~n S~r (2) INFORMATION FOR SEQ ID NO:69 (1) SEQUENCE CHARACTERISTICS
(A~ LENGTH: 21 amino acld~
~B) TYPE: amino acid 2~3~3~9 (D) TOPOLOGY: linear ~ii) MOLECULE TYPE: peptide (lx) FEATURE:
(A) NAM~/KE'f: magainin peptide.
(D) OTHER INFORMATION: amlde- or carboxy- terminated (x) PUBLICATION INFORMATION:
(A) AUTHOR: Za~loff, Michael ~C) JOURNAL: Proceedin~ of the National AcademY
of Scienceq (D) VOLUME: 84 (F) PAGES: 5449-5453 (G) DATE: AUG - 1987 (H) DOCUMENT NUMBER: US 4810777 (I) FILING DATE: 04-MAR-1987 (J) PUBLICATION DATE: 07-MAR-1989 (xi) SEQUENCE D~SCRIPTION: SEQ ID NO:69:
Gly Lys Phe Leu Hi~ Ser Ala Lys Lys Phe Gly Lys Ala Phe Val Gly Glu Ile Met A~n lS 20 Ser ~2) INFORMATION FOR SEQ ID NO:70 ~1) SEQUENCE CHARACTERISTICS
~A) LENGTH: 20 amino acid~
(B) TYPE: am~no acid (D) TOPOLOGY: linear ~ii) MOLECULE TYPE: peptide 2 ~ ~ ~ 9 (ix) F~ATURE:
(A) NAME/KEY: magainin peptide.
(D) OTHER INFORMATION: amide- or carboxy~ termi~ated ~x) PUBLICATION INFORMATION:
~A~ AUTHOR: Za~loff, Michael ~C) JOURNAL: Proceedinq~ of the National AcademY
of Sc_enceJ
(D) VOLUME: 84 ~F) PAGES: 5449-5453 (G) DATE: AUG - 1987 ~H) DOCUMENT NUMBER: US ~810777 (I) FILIN5 DATE: 04-MAR-1987 (J) PU8LICATION DATE: 07-MAR-1989 ~xi) SEQUENCE DESCRIPTION: SEQ ID NO:70:
Ly~ Phe Leu His Ser Ala Ly~ Lys Phe Gly Ly~ Ala Phe Val Gly Glu Ile Met A~n Ser (2~ INFORMATION FOR SEQ ID NO:71 (i) SEQUENCE CHARACTERISTICS
~A) LENGTH: 21 amino acid~
~a) TYPE: amlno acid (D) TOPOLOGY: llnear (11) MOLECULE TYPE: peptide (ix) FEATURE:
(A) NAME/KEY: PGLa peptide.
(D) OTHER INEORMATION: amlde-terminated (x) PU8LICATION INFORMATION:

203~59 -6a-(A) AUTHOR: Hoffman, et al.
(C) JOURNAL: EMBO J.
(D) VOLUME: 2 (~) PAGES: 711-714 (C) DATE: 1983 (A) AUTHOR: Andreu, et al.
(C) JOURNAL: Journal of Biochemi~trY
(D) VOLUME: 149 (F) PAGES: 531-535 (G) DATE: 1985 ~A) AUTHOR: Clbson, et al.
(C) JOURNAL: J. Biol. Chem.
(D) VOLUME: 261 (F) PAGES: 5341-5349 (C) DATE: 1986 (A) AUTHOR: Giovannini, et al.
(C) JOURNAL: Biochem J.
( D ) VOLUME: 2 43 (F) PAGES: 113-120 (G) DATE: 1987 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:71:
Gly Met Ala Sor Ly~ Ala Gly Ala Ile Ala Cly Ly~ Ile Ala Ly~ Val Ala Lou Lyq Ala Leu (2) INFORMATION FOR SEQ ID NO:72 (1) SEQUENCE CHARACTERISTICS
( A ) LENGTH: 2 5 amino acid~
( B ) TYPE: amlno acid (D) TOPOLOGY: linear 2~35959 (ii) MOLECULE TYPE: peptlde (ix) FEATURE:
(A) NAME/KEY: XPF peptlde.

(x) PUBLICATION INFORMATION:
(A) AUTHOR: Hoffman, et al.l (C) JOURNAL: EM80 J.
(D) VOLUME: 2 ~F) PACES: 711-714 (G) DATE: 1983 (A) AUTHOR: Andreu, et al.
(C) JOURNAL: Journal of Biochemi~trY
(D) VOLUME: 149 ~F) PACES: 531-535 (C) DATE: 1985 (A~ AUTHOR: Glbson, et al.
(C~ JOURNAL: J. 3101. Chem.
(D) VOLUME: 2 61 (F) PAGES: 5341-5349 (G) DATE: 1986 (A) AUTHOR: Gi ovannl ni, e t al.
(C) JOURNAL: Blochem J .
( D ) VOLUME: 2 43 (F) PACES: 113-120 (G) DATE: 1987 (xi) SEQUENCE DE SCR I PT I ON: SEQ ID NO:72:
Cly Trp Ala Ser Ly~ I le aly Cln Thr Leu Gly Ly8 Ilo Ala Ly8 Val Gly Leu Ly~ Clu Leu I le Gln Pro Lys 2~3~59 ~o--(2) INFORMATION FOR SEQ ~D NO:73 (i) SEQUENCE CHARACTERISTICS
(A) LENGTH: 27 amino acid~
(B) TYPE: amino acid (D) TOPOLOCY: linear (ii) MOLECULE TYPE: peptide (lx) FEATURE:
(A) NAME/KEY: CPF peptide.
(D) OTHER INFORMATION: amide- or carboxy- terminated (x~ PUBLICATION INFORMATION:
(A) AUTHOR: Richter, K.
Egger, R.
Kreil (C) JOURNAL: J. Biol. Chem.
(D) VOLUME: 261 (F) PACES: 3676-3680 (G) DATE: 1986 (A) AUTHOR: Wakabaya~hi, T.
Kato, ~.
Tachibaba, S.
(C) JOURNAL: Nucleic Acid~ Research (D~ VOLUME: 13 (F) PAGES: 1817-1B2B
(C) DATE: 1985 ~A) AUTHOR: Gib~on, B.W.
Poulter, L.
William~, D.H.
Maggio, J.E.
(C) JOURNAL: J. Biol. Chem.
(D) VOLUME: 261 (F) PAGES: 5341-5349 2~353~9 (G) DATE: 1986 (H) DOCUMENT NUMBER: WO90/04407 (I) FILING DATE: 16-OCT-1989 (J) PUBLICATION DATE: 03-MAY-l99O

(xl) SEQUENCE DESCRIPTION: SEQ rD NO:73:
Gly Phe Cly Ser Phe Leu Cly Leu Ala Leu Lys Al~ Ala Leu Lys Ile Cly Ala A~n Ala Leu Gly Gly Ala Pro Gln Gln (2) INFORMATION FOR SEQ ID NO:74 (i) SEQUENCE CHARACTERISTICS
(A) LENCTH: 27 amino acid~
(B) TYPE: amino acid (D) TOPOLOCY: linear (ii) MOLECULE TYPE: peptide (lx) FEATURE-(A) NAME/KEY: CPF peptlde.
(D) OTHER INFORMATION: amide- or carboxy- terminated (x) PUBLICATION INFORMATION:
(A) AUTHOR: Richter, K
Egger, R.
Kreil (C) JOU~NAL: J. 8iol. Chem.
(D) VOLUME: 261 ( F ~ PAGES: 3 67 6- 3 680 (G) DATE: 1986 (A) AUTHOR: Wakabayashl, T.

20~9~

Kato, H.
Tachibaba, S.
(C) JOURNAL: Nucleic Acid~_Research (D) VOLUME: 13 (F) PAGES: 1817-1828 (G) DATE: 1985 ~A) AUTHOR: Cib~on, B.W.
Poulter, L.
William~, D.H.
Maggio, J.E.
(C) JOURNAL: J. Blol. Chem.
(D) VOLUME: 261 (F) PAGES: 5341-5349 (C) DATE: 1986 (H) DOCUMENT NUM8ER: WO90/04497 (I) FILING DATE: 16-OCT-1989 (J) PUBLICATION DATE: 03-MAY-1990 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:74 Gly Leu Ala Ser Phe Leu Gly Ly~ Ala Leu Lys Ala Cly Leu Ly~ Ile Gly Ala ~i9 Leu Leu Gly Cly Ala Pro Gln Gln (2) INFORMATION FOR SEQ ID NO:75 (1) SEQUENCE CHARACTERISTICS
(A) LENGTH: 27 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide _73_ 233~959 (ix) FEATURE:
(A) NAME/~EY: CP~ peptide.
(D) OTHER INFORMATION: amide- or carboxy- terminated (x) PUBL~CATrON INFORMATION:
(A) AUTHOR: Richter, K.
Egger, R.
Kreil (C) JOURNAL: J. Biol. Chem.
(D) VOLUME: 261 (F) PAGES: 3676-36~30 (G) DATE: 1986 (A) AUTHOR: Wakabaya~hi, T.
Kato, H.
Tachibaba, S.
(C) JOURNAL: Nucleic Acid~ Research (D) VOLUME: 13 (F) PACES: 1817-1828 (G) DATE: 1985 (A) AUTHOR: Cibson, B.W.
Poulter, L.
Williams, D.H.
Magqio, J.E.
(C) JOURNAL: J. Biol. Chem.
(D) VOLUME: 261 (~) PAGES: 5341-5349 (C) DATE: 1986 (H) DOCUMENT NUMBER: W090/04407 (I) FILINC DATE: 16-OCT-1989 (J) PUBLICATION DATE: 03-MAY-1990 (xl) SEQUENCE DESCRIPTION: SEQ ID NO:75:
Gly Leu Ala Ser Leu Leu Cly Ly~ Ala Leu _74_ 2~3~9~9 Lys Ala Cly Leu Lys Ile Gly Thr His Phe Leu Gly Gly Ala Pro Gln Gln ~2) rNFORMATION FOR SEQ ID NO:76 ~i) SEQUENCE CHARACTERISTICS
~A) LENGTH: 27 amlno acids (B~ TYPE: amino acld (D) TOPOLOCY: linear (11) MOLECULE TYPE: peptide (lx) FEATURE:
(A) NAME/KEY: CPF peptlde.
(D) OTHER INFORMATION: amlde- or carboxy- terminated (x) PUBLICATION INFORMATION:
(A) AUTHOR: Rlchter, K.
Eg~er, R.
Krell (C) JOURNAL: J. 8101. Chem.
(D) VOLUME: 261 (F) PAGES: 3676-3680 (G) DATE: 1986 (A) AUTHOR: Wakabaya~hl, T.
Kato, H.
Tachlbaba, S.
(C) JOURNAL: Nuclelc Acids Research (D) VOLUME: 13 (F) PAGES: 1817-1828 (G) DATE: 1985 (A) AUTHOR: Glbson, B.W.
Poulter, L.

_75_ 2~3~9~9 Williams, D.H.
Maggio, J.E.
~C) JOURNAL: J. B~ol_. Chem.
(D) VOLUME: 261 (F) PAGES: 5341-53~9 (G) DATE: 1986 (H) DOCUMENT NUM~ER: W090/04407 (I) FILINC DATE: 16-OCT-1989 (J) PUBLICATION DATE: 03-MAY-l99O

(xi) SEQUENCE DESCRIPTION: SEQ ID NO:76:
Gly Leu Ala Ser Leu Leu Gly Lys Ala Leu Ly~ Ala Thr Leu Lys Ile Gly Thr His Phe Leu Cly Gly Ala Pro Gln ~ln (2) INFORMATION EOR SEQ ID NO:77 (i) SEQUENCE CHARACTERISTICS
(A) LENGTH: 27 amino acid3 (B) TYPE: amino acid (D) TOPO~OGY: linear (ll) MOLECULE TYPE: peptide (ix) FEATURE:
(A) NAME/KEY: CPF peptide.
(D) OTHER INFORMATION: amide- or carboxy- terminated (x) PUBLICATION INFO~MATION:
(A) AUTHO~: Rlchter, K.
Egger, R.
Kreil -76- 2~3~9~

(C) JOURNAL: J. Biol. Chem.
(D) VOLUME: 261 (F) PAGES: 3676-3680 (C.) DATE: 1986 (A) AUTHOR: Wakabayashi, T.
Kato, H.
Tachib~ba, S.
(C) JOURNAL: Nuclelc Acids Research (D) VOLUME: 13 (F) PAGES: lB17-1828 (G) DATE: 1985 (A) AUTHOR: Gib~on, B.W.
Poulter, L.
Wllliam~, D.H.
Maggio, J.~.
(C) JOURNAL: J. 8iol. Chem.
(D) VOLUME: 261 (F) PAGES: 5341-5349 (G) DATE: 1986 (H) DOCUMENT NUMBER: WO90/04407 (I) FILING DATE: 1600CT-1989 (J) PUBLICATION DATE: 03-MAY-l99O

(xi) SEQUENCE DESCRI PT ION: SEQ ID NO:77:
Gly Phe Ala Sor Phe Leu G1y Ly~ Ala Leu Ly~ Ala Ala Lou Lys I le Gly Ala AJn Met Lou Gly Gly Thr Pro Gln Gln ~2) INFORMATION FOR SEQ ID NO:78 (i) SEQUENCE CHARACTERISTICS
(A) LENCTH: 27 amino acids -77- 203.~9~9 (B) TYPE: amino acid (D) TOPOLOCY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE:
(A) NAME/KEY: CPF peptide.
(D) OTHER INFORMATION: amide- or carboxy- terminated (x) PU~LICATION INFORMATION:
(A) AUTHOR: Richter, K.
Egger, R.
Krell (C) JOURNAL: J. 8101. Chem.
(D) VOLUME: 261 (F) PAGES: 3676-3680 (G) DATE: 1986 (A) AUTHOR: Wakabayashi, T.
Kato, H.
Tachibaba, S.
(C) JOURNAL: Nucleic Acids Research (D) VOLUME: 13 (F) PAGES: 1817-1828 (G) DATE: 1985 (A) AUTHOR: Glbson, 8.W.
Poulter, L.
Wllliams, D.H.
Magglo, J.E.
(C) JOURNAL: J. Blol. Chem.
(D) VOLUME: 261 (F) PAGES: 5341-5349 (G) DATE: 1986 (H) DOCUMENT NUMBER: WO90/04407 (I) FILING DATE: 16-OCT-1989 -78- 2~3J9-~9 (J~ PUBLICATION DATE: 03-MAY-l99O

(xi) SEQU~NCE DESCRIPTION: SEQ ID NO:7~:
Cly Phe Cly Ser Phe Leu Cly Ly~ Ala Leu Ly~ Ala Ala Leu t,yq Ile Cly Ala Acn Ala Leu Cly Gly Ala Pro Gln Gln (2) INFORMATION FOR SEQ ID NO:79 (i) SEQUENCE CHARACTERISTICS
(A) LENGTH: 27 amino acids (B) TYPE: amino acld ~D) TOPOLO~Y: llnear (li) MOLECULE TYPE: peptlde ~lx) FEATURE:
~A) NAME/KEY: CPF peptide.
~D) OTHER INFORMATION: amlde- or carboxy- terminated (x) PUBLICATION INFORMATION:
~A) AUTHOR: Richter, K.
Egger, R.
Krell (C) JOURNAL: J. Biol. Chem.
(D) VOLUME: 26l (F) PAGES: 3676-3680 (G) DATE: 1986 (A) AUI'HOR: Wakabayashl, T.
Kato, H.
Tachibaba, S.
(C) JOURNAL: Nucleic Aclds Research (D) VOLU~.E: 13 _79_ ~3~59 ( F) PACES: 1817-1828 (G) D~TE: 1985 (A) AUTHOR: Gibson, ~.W.
Poulter, L.
Williams, D.H.
Maggio, J.E.
(C) JOURNAL: J. Blol. Chem.
(D) VOLUME: 261 (F) PACES: 5341-5349 (G) DATE: 1986 (H) DOCUMENT NUMBER: W090/04407 (I) FILING DATE: 16-OCT-1989 (J) PUBLICATION DATE: 03-MAY-1990 (xl) SEQUENCE DESCRIPTION: SEQ ID N0:79:
Gly Phe Gly Ser Phe Leu Gly Ly~ Ala Leu Ly~ Ala Ala Leu Ly~ Ile Cly Ala A~n Ala Leu Gly Gly Ser Pro G.n Cln (2) INFORMATION FOR SEQ ID NO:80 (i) SEQUENCE C~ARACTERISTICS
(A) LENGTH: 27 amino acid~
(B) TYPE: amino acld ~D) TOPOLOGY: llnear (li) MOLECULE TYPE: peptide (ix) FEATURE:
(A) NAME/~EY: CPF peptlde.
(D) O~HER INFORMATION: amide- or carboxy- termlnated ~ ~ 3 ~

(x) PUBLICATION INFORMATION:
(A) AUTHOR: Richter, K.
Egger, R.
Kreil (C) JOURNAL: J. Biol. Chem.
(D) VOLUME: 261 (E) PAGES: 3676-3680 (C) DATE: 1986 (A) AUTHO~: Wakabayashl, T.
Kato, H.
Tachibaba, S.
(C) JOURNAL: Nucleic Acids Research (D) VOLUME: 13 (F) PAGES: 1817-la28 (G) DATE: 1985 (A) AUTHOR: Glb~on, B.W.
Poulter, L.
William~, D.H.
Magglo, J.E.
(C) JOURNAL: J. Biol. Chem.
(D) VOLUME: 261 (F~ PAGES: 5341-5349 (G) DATE: 1986 (H) DOCUMENT NUMBER: WO90/04407 (I) FILING DATE: 16-OCT-1989 (J) PUBLICATION DATE: 03-MAY-l99O

(xl) SEQUENCE DESCRIPTION: SEQ ID NO:80:
Gly Ph~ Ala Ser Phe Leu Gly Ly~ Ala Leu Ly~ Als Ala Leu By~ Ile Cly Ala A~n Leu Leu Gly Gly Thr Pro Gln Cln ~5 2~3~9~9 (2) INFORMATION FOR SEQ ID NO 81 (i) SEQUENCE CHARACTERISTICS
(A) LENGTH: 27 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE:
(A) NAME/KEY: CPF peptide.
(D) OTHER INFORMATION: amide- or carboxy- terminated (x) PUBLICATION INFORMATION:
(A) AUTHOR: Richter, K.
E~ger, R
Kreil (C) JOURNAL: J. Blol. Chem.
(D) VOLUME: 261 (F) PAGES: 3676-3680 ~G) DATE: 1986 (A) AUTHOR: Wakabayashi, T.
Kato, H.
Tachibaba, S.
(C) JOURNAL: Nucleic Acids Research (D) VOLUME: 13 (F) PAGES: 1817-1828 (G) DATE: 1985 (A) AUTHOR: Cib~on, B.W.
Poulter, L.
William~, D.H.
Magglo, J.E.
(C) JOURNAL: J. alol. Chem.
(D) VOLUME: 261 (F) PAGES: 5341-5349 -82- 2~3~9~9 (C) DATE: 1986 ~xi) SEQUENCE DESCRIPTION: SEQ ID NO:~l:
Cly Phe Ala Se~ Phe Leu Gly Ly~ Ala Leu Lys Ala Ala Leu Lys Ile Cly Ala Asn Ala Leu Gly Gly Ala Pro Gln Gln (2) INFORMATION FOR SEQ ID NO:82 (i) SEQUENCE CHARACTERISTICS
(A) LENCTH: 27 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE:
(A) NAME/KEY: CPF peptide.
(D) OTHER INFORMATION: amide- or carboxy- terminated (x) PUBLICATION INFORMATION:
(A) AUTHOR: Richter, K.
Egger, R.
Kreil (C) JOURNAL: J. Biol. Chem.
(D) VOLUME: 261 (F) PAGES: 3676-36~30 (C) DATE: 1986 (A) AUTHOR: Wakabaya~hi, T.
Kato, H.
Tachibaba, S.
(C) JOURNAL: Nuclelc Acid9 Research (D) VOLUME: 13 (F) PAGES: 1817-1828 ~ 3 ~ 3 9 ~G) DATE: 1985 ~A) AUTHOR: Cib~on, B.W.
Poulter, L.
Williams, D.H.
Maggio, J.E.
(C) JOURNAL: J. 3iol. Chem.
(D) VOLUME: 261 (Fl PACES: 5341-5349 (G) DATE: 1986 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:82:
Gly Phe Ala Ser Phe Leu Cly Lys Ala Leu Lys Ala Ala Leu Lys Ile Cly Ala Asn Met Leu Cly Gly Ala Pro Cln Cln (2) INFORMATION FOR SEQ ID NO:~33 (i) SEQUENCE CHARACTERISTICS
(A) LENGTH: 27 amino acid~
~B) TYPE: amino acid (D) TOPOLOGY: linoar (ii) MOLECULE TYPE: peptide (lx) FEATURE:
~A) NAME/KEY: CPF poptld~.
(D) OTHrER INEORMATION: amide- or carboxy- terminated (x) PUBLICATION INFORMATION:
(A) AUTHOR: Rlchter, K.
Eg~or, R.
Kreil -a4- 2~3~9~9 (C) JOURNAL: J. Biol Chem.
(D) VOLUME: 261 (F) PAGES: 3676-3680 (G) DATE: 1986 (A) AUTHOR: Waka~ayashi, T.
Kato, H.
Tachibaba, S.
(C) JOURNAL: Nucleic Acid~ Re~earch (D) VOLUME: 13 (F) PAGES: 1817-1828 (C) DATE: 1985 (A) AUTHOR: Clb~on, ~.W.
Poulter, L.
Williams, D.H.
Maggio, J.E.
(C) JOURNAL: J. Biol. Chem.
~D) VOLUME: 261 (F) PAGES: 5341-5349 (C) DATE: 1986 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:83:
Cly Phe Gly Ser Phe Leu Gly Lys Ala Leu Ly~ Ala Ala Lou Lys Ile Cly Ala AAn Ala Leu Gly Cly Ser Lou Gln Gln (2) INFORMATION FOR SEQ ID NO:84 (1) SEQUENCE CHARACTERISTICS
(A) LENGTH: 27 amino acid~
(B) TYPE: amino acid (D) TOPOLOGY: linear (li) MOLECULE TYPE: peptide ~3~9 -~5-(ix) FEATURE:
(A) NAME/KEY: CPF peptide.
(D) OTHER INFORMATION: amide- or carboxy- terminated (x) PUBLICATION INFORMATION:
(A) AUTROR: Richter, ~.
Egqer, R.
Krell (C) JOURNAL: J. Biol. Chem.
tD) VOLUME: 261 (F) PAGES: 3676-3680 (C) DATE: 1986 (A) AUTHOR: Wakabayashi, T.
Kato, H.
Tachlbaba, S.
(C) JOURNAL: Nucl~ic Aclds Research (D) VOLUME: 13 (F) PAGES: 1817-1828 (G) DATE: 1985 (A) AUTHOR: Glb~on, 8.W.
Poulter, L.
William~, D.H.
Magglo, J.E.
(C) JOURNAL: J. 81Ol. Chem.
(D) VOLUME: 261 (F) PAGES 5341-5349 (G) DATE: 1986 (xl) SEQUENCE DESCRIPTION: SEQ ID NO:84:
Gly Pho Cly Ser Phe Leu Gly Lys Ala Leu Lys A1A Cly Leu Lys Ile Gly Thr Asn Phe Leu Gly Gly Ala Pro Gln Gln 2~3~9~9 -a6-(2) INFORMATION FOR SEQ ID NO:85 ~i) SEQUENCE CHARACTERISTICS
(A) LENGTH: 27 amino acids ( B ) TYPE: amino acid (D) TOPOLOCY: linear (ll) MOLECULE TYPE: peptide (ix) FEATURE:
(A) NAME/KEY: CPF peptide.
(D) OTHER INFORMATION: amide- or carboxy- terminated (x) PUBLICATION INFORMATIO~:
(A) AUTHOR: Richt~r, K
Egger, R.
Kreil (C) JOURNAL: J. Biol. Chem.
~D) VOLUME: 261 (F) PAGES: 3676-3680 (G) DATE: 1986 (A) AUTHOR: Wakabayashl, T.
Kato, H.
Tachlbaba, S.
(C) JOURNAL: Nucleic Acids Research (D) VOLUME: 13 (F) PACES: 1~17-1828 (G) DATE: 19~5 (A) AUTHOR: Clbson, B.W.
Poulter, L.
Willlams, D.H.
Maggio, J.E.
(C) JOURNAL: J. Blol. Chem.

(D) VOLUME: 261 (F) PAGES: 5341-5349 -87- 2a359~9 (G) DATE: 1986 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:85:
Gly Leu Ala Ser Leu Leu Gly Lyc Ala Leu Ly~ Ala Ala Leu Ly~ Ile Cly Ala A~n Ala Leu Cly Gly Ser Pro Gln Cln

Claims (52)

1. A biologically active amphiphilic peptide, said peptide including one of the following basic structures X1 through X7, wherein X1 is -[R1-R2-R2-R3-R1-R2-R2]n, X2 is -[R2-R2-R3-R1-R2-R2-R1]n;
X3 is -[R2-R3-R1-R2-R2-R1-R2]n;
X4 is -[R3-R1-R2-R2-R1-R2-R2]n;
X5 is -[R1-R2-R2-R1-R2-R2-R3]n;
X6 is -[R2-R2-R1-R2-R2-R3-R1]n; and X7 is -[R2-R1-R2-R2-R3-R1-R2]n;
wherein R1 is a basic hydrophilic amino acid, R2 is a hydrophobic amino acid, R3 is a neutral hydrophilic or hydrophobic amino acid, and n is from 2 to 5.

2. The peptide of Claim 1 wherein n is 3.

3. The peptide of Claim 2 wherein said peptide has the following structural formula:
(Lys Ile Ala Gly Lys Ile Ala)3-NH2

4. The peptide of Claim 2 wherein said peptide has the following structural formula:
(Lys Ile Ala Lys Ile Ala Gly)3-NH2

5. A composition comprising the peptide of Claim l, and a pharmaceutical carrier.

6. The composition of Claim 5 wherein said peptide is present in an amount effective to inhibit growth of a target cell.

7. A process for inhibiting growth of a target cell, virus, or virally-infected cell, comprising:
administering a biologically active amphiphilic peptide, said peptide including one of the following basic structures X1 through X7, wherein:
X1 is -[R1-R2-R2-R3-R1-R2-R2]-n, X2 is -[R2-R2-R3-R1-R2-R2-R1]-n;
X3 is -[R2-R3-R1-R2-R2-R1-R2]-n;

X4 is -[R3-R1-R2-R2-R1-R2-R2]-n;
X5 is -[R1-R2-R2-R1-R2-R2-R3]-n;
X6 is -[R2-R2-R1-R2-R2-R3-R1]-n;
X7 is -[R2-R1-R2-R2-R3-R1-R2]-n;
wherein R1 is a basic hydrophilic amino acid, R2 is a hydrophobic amino acid, R3 is a neutral hydrophilic, basic hydrophilic, or hydrophobic amino acid, and n is from 2 to 5.

8 The process of Claim 7 wherein n is 3.

9. The process of Claim 8 wherein said peptide has the following structural formula:
(Lys Ile Ala Gly Lys Ile Ala)3-NH2.

10. The process of Claim 8 wherein said peptide has the following structural formula:
(Lys Ile Ala Lys Ile Ala Gly)3-NH2.

11. The process of Claim 7 wherein said administering is to an animal host in an effective anti-tumor amount.

12. The process of Claim 7 wherein said administering is to an animal host in an effective anti-viral amount.

13. The process of Claim 7 wherein said administering is to an animal host in an effective antimicrobial amount.

14. The process of Claim 7 wherein said administering is to an animal host in an effective anti-parasitic amount.

15. The process of Claim 7 wherein said administering is to an animal host in an effective antibiotic amount.

16. The process of Claim 7 wherein said administering is to an animal host in an effective anti-spermicidal amount.

17. The process of Claim 7 wherein said administering is to an animal host in an amount effective in treating healing of a wound in said animal host.

18. A biologically active amphiphilic peptide, said peptide including the following basic structure: X14:
R1-R2-R2-R3-R4-R2-R2-R1-R2-R2-R2-R4-R2-R2, wherein R1 is a basic hydrophilic amino acid, R2 is a hydrophobic amino acid, R3 is a neutral hydrophilic or a hydrophobic amino acid, and R4 is a basic hydrophilic or hydrophobic amino acid.

19. The peptide of Claim 26 wherein the peptide includes the following structure:
Y14-X14, wherein X14 is the basic peptide structure of Claim 18, and Y14 is:
(i) R2;
(ii) R2-R2;
(iii) R4-R2-R2;
(iv) R3-R4-R2-R2;
(v) R2-R3-R4-R2-R2;
(vi) R2-R2-R3-R4-R2-R2; or (vii) R1-R2-R2-R3-R4-R2-R2.

20. The peptide of Claim 18 wherein the peptide includes the following structure:
X14-Z14, wherein X14 is the basic peptide structure of Claim 18 and Z14 is:
(i) R1;
(ii) R1-R2;
(iii) R1-R2-R2;
(iv) R1-R2-R2-R3;
(v) R1-R2-R2-R3-R4;
(vi) R1-R2-R2-R3-R4-R2; or (vii) Rl-R2-R2-R3-R4-R2-R2.

21. The peptide of Claim 18 wherein the peptide includes the following basic structure:
(Y14)a-(X14)-(Z14)b, wherein Y14 and Z14 are as previuosly described in Claims 19 and 20, a is 0 or 1 and b is 0 or 1.

22. The peptide of Claim 21 wherein said peptide has the following structural formula:

23. The peptide of Claim 21 wherein said peptide has the following structural formula:

24. A composition comprising the peptide of Claim 18 and a pharmaceutical carrier.

25. The composition of Claim 24 wherein said peptide is present in an amount effective to inhibit growth of a target cell.

26. A process for inhibiting growth of a target cell, virus, or virally-infected cell, comprising:
administering a biologically active amphiphilic peptide, said peptide including the following basic structure X14:
R1-R2-R2-R3-R4-R2-R2-R1-R2-R2-R2-R4-R2 R2-, basic hydrophilic amino acid, R2 is a hydrophobic amino acid, R3 is a neutral hydrophilic or hydrophobic amino acid, and R4 is a basic hydrophilic or hydrophobic amino acid.

27. The process of Claim 26 wherein the peptide includes the following structure:
Y14-X14, wherein X14 is the basic peptide structure of Claim 29, and Y14 18:
(i) R2;
(ii) R2-R2;
(iii) R4-R2-R2;
(iv) R3-R4-R2-R2;
(v) R2-R3-R4-R2-R2;
(vi) R2-R2-R3-R4-R2-R2; or (vii) R1-R2-R2-R3-R4 R2-R2.

28. The process of Claim 26 wherein the peptide includes the following structure:

X14-Z14, wherein X14 is the basic peptide structure of Claim

29, and Z14 is:
(i) R1;
(ii) R1-R2;
(iii) R1-R2-R2;
(iv) R1-R2-R2-R3;
(v) R1-R2-R2-R3-R4;
(vi) R1-R2-R2-R3-R4-R2; or (vii) R1-R2-R2-R3-R4-R2-R2.
29. The process of Claim 26 wherein the peptide includes the following basic structure:
(Y14)a-X14-(Z14)b, wherein Y14 and Z14 are as previously defined in Claims 27 and 28, and a is 0 or 1, and b is 0 or 1.

30. The process of Claim 29 wherein said peptide has the following structural formula

31. The peptide of Claim 29 wherein said peptide has the following structural formula:

32. The process of Claim 26 wherein said administering is to an animal host in an effective anti-tumor amount.

33. The process of Claim 26 wherein said administering is to an animal host in an effective anti-viral amount.

34. The process of Claim 26 wherein said administering is to an animal host in an effective antimicrobial amount.

35. The process of Claim 26 wherein said administering is to an animal host in an effective anti-parasitic amount.

36. The process of Claim 26 wherein said administering is to an animal host in an effective antibiotic amount.

37. The process of Claim 26 wherein said administering is to an animal host in an effective anti-spermicidal amount.

38. The process of Claim 26 wherein said administering i-to an animal host in an amount effective in treating a wound in said animal host.

39. The peptide of Claim 1 wherein each amino acid residue is a D-amino acid residue or glycine.

40. The peptide of Claim 18 wherein each amino acid residue is a D-amino acid residue or glycine.

41. A biologically active amphiphilic peptide including the following structural formula:
(Lys Ile Ala Lys Lys Ile Ala)n, wherein n is from 2 to 5.

42. The peptide of Claim 41 wherein said peptide has the following structural formula:
(Lys Ile Ala Lys Lys Ile Ala)3-NH2.

43. A process for inhibiting growth of a target cell, virus, or virally-infected cell, comprising:
administering to a host the biologically active amphiphilic peptide of Claim 41, said peptide being administered in an amount effective in inhibiting growth of a target cell, virus, or virally-infected cell in a host.

44. The process of Claim 43 wherein said administering 1 to an animal host is an effective anti-tumor amount.

45. The process of Claim 43 wherein said administering is to an animal host in an effective anti-viral amount.

46. The process of Claim 43 wherein said administering is to an animal host in an effective anti-microbial amount.

47. The process of Claim 43 wherein said administering is to an animal host in an effective anti-parasitic amount.

48. The process of Claim 43 wherein said administering 1 to an animal host in an effective antibiotic amount.

49. The process of Claim 43 wherein said administering is to an animal host in an effective anti-spermicidal amount.

50. The process of Claim 43 wherein said administering is to an animal host in an amount effective in treating or healing a wound in said animal host.

51. A biologically active amphiphilic peptide selected from the group consisting of:
(SEQ ID NO:61)-NH2 (SEQ ID NO:62)-NH2 (SEQ ID NO:63)-NH2; and (SEQ ID NO:64)-NH2.

52. A process for inhibiting growth of a target cell, virus, or virally-infected cell, comprising:
administering a biologically active amphiphilic peptide, said peptide selected from the group consisting of:
(SEQ ID NO:61)-NH2 (SEQ ID NO:62)-NH2 (SEQ ID NO:63)-NH2; and (SEQ ID NO:64)-NH2.