CN114907447A - Antibacterial peptide - Google Patents
Antibacterial peptide Download PDFInfo
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- CN114907447A CN114907447A CN202210171227.7A CN202210171227A CN114907447A CN 114907447 A CN114907447 A CN 114907447A CN 202210171227 A CN202210171227 A CN 202210171227A CN 114907447 A CN114907447 A CN 114907447A
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/08—Linear peptides containing only normal peptide links having 12 to 20 amino acids
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
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- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change
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- Chemical Kinetics & Catalysis (AREA)
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- Proteomics, Peptides & Aminoacids (AREA)
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Abstract
The invention belongs to the field of biochemistry, and discloses an antibacterial peptide, which has the following components: (I) and an amino acid sequence as shown in any one of SEQ ID No. 1-SEQ ID No. 20; or (II), an amino acid sequence obtained by substituting, deleting and adding one or more amino acids in the amino acid sequence described in (I), or an amino acid sequence obtained by converting one or more amino acids in the amino acid sequence described in (I) into D-type amino acids, and the amino acid sequence has the same function with the amino acid sequence described in (I). The polypeptide has the characteristics of broad spectrum, high efficiency, safety and difficult drug resistance.
Description
Technical Field
The invention relates to the field of biochemistry, in particular to an antibacterial peptide.
Background
Bacterial infections are one of the most serious public health problems at present, and it is expected that 1000 million people die of bacterial infections every year 2050. The number of deaths outweighs cancer. The development of a new antibiotic drug needs 10-15 years, while the emergence of a drug-resistant bacterium only needs about 2 years, and the development of the new drug by continuing to use the antibiotic mechanism is more and more unable to keep up with the speed of drug resistance of bacteria. In addition, due to the adverse factors of high investment, low return, high approval threshold and the like, many enterprises are reluctant to invest and develop new antibiotics. If allowed to develop, humans will either not be available in the future. There is therefore a great need to develop new methods to accelerate the design and production of effective antibacterial agents, thereby limiting the spread of drug resistant pathogens.
Antimicrobial peptides (AMPs) are small molecular polypeptides which are encoded by organism specific genes and generated by external induction and consist of 5-100 amino acid residues and have antibacterial activity, are commonly present in animals, plants and microorganisms, and are important defense systems in organisms in the nature. The antibacterial peptide is usually rich in basic amino acids such as lysine, arginine and the like, has a certain amount of positive charges and is a cationic polypeptide. The antibacterial activity of the antibacterial peptide has the characteristics of high selectivity, quick sterilization, broad spectrum action and difficulty in forming resistance, so that the antibacterial peptide becomes an ideal candidate for researching and developing novel antibiotics. At present, the extraction of natural antibacterial peptide from organisms is one of the main approaches for the development of antibacterial peptide products.
In the 80's of the 20 th century, Boman et al, a swedish scientist, discovered and named the first antimicrobial peptide, cecropin, in the ancient ratio of silkworms. To date, as many as 3000 or more natural or synthetic antimicrobial peptides have been discovered and identified, but only 9 of them are actually drugged. Unfortunately, the drug-approved antimicrobial peptides are narrow spectrum antimicrobial peptides, the best known vancomycin, which is considered the "last line of defense" for antibiotics, is not effective against gram-negative bacteria. And bacteria resistant to vancomycin, such as vancomycin-resistant enterococci (VRE), have emerged due to overuse of antibiotics, creating concerns in the control of infectious diseases. Therefore, the development of new broad-spectrum antibacterial peptides has been very slow.
D1: the Tianjin medical professor thesis, "preliminary investigation of antibacterial action of Pennetatin-derived short peptide RR9 on Streptococcus oralis", fourth page records: we found that CPP, Penetratin and some of its analogues with good cell penetration actually have antibacterial activity; the scheme develops a short peptide RR9 based on the parent peptide Pennetratin, wherein the short peptide RR9 has 9 amino acids and has stronger antibacterial activity.
At the same time, D1 also discloses on page 16 that arginine (Arg) contributes significantly to antibacterial activity.
However, the parent peptide of Penetratin has 16 amino acids, and theoretically, the more positive charges, the more helices are more easily bound to the bacterial cell membrane to destroy the cell membrane, and if the helices are too short, the more helices are reduced, and the cell membrane destructive power is reduced sharply.
D2: CN201611036266.7 an antibacterial peptide based on cell-penetrating peptide Tat (49-57) and its synthesis method, the scheme carries out corresponding amino acid modification on cell-penetrating peptide Tat, and obtains polypeptide with more excellent antibacterial effect.
According to D2, altered Tat (YG), Tat (YY), Tat (FG) and Tat (FF) have better antibacterial activity, and the concentration of the polypeptide with the same antibacterial effect is mostly reduced to 25-50% of Tat (49-57).
Therefore, the technical problem that the present scheme was solved is: how to develop a new broad-spectrum antibacterial peptide.
Disclosure of Invention
The invention aims to provide an antibacterial peptide which has the characteristics of broad spectrum, high efficiency, safety and difficult drug resistance.
In order to achieve the purpose, the invention provides the following technical scheme: an antimicrobial peptide having:
(I) and an amino acid sequence as shown in any one of SEQ ID No. 1-SEQ ID No. 20;
or
(II) an amino acid sequence obtained by substituting, deleting and adding one or more amino acids in the amino acid sequence described in (I) or an amino acid sequence obtained by converting one or more amino acids in the amino acid sequence described in (I) into D-type amino acids, and the amino acid sequence has the same function with the amino acid sequence described in (I).
The D-form amino acid is an amino acid artificially synthesized by D-form glyceraldehyde, and the amino acid of this type has similar biological and chemical properties to the amino acid sequence before conversion, as widely verified by those skilled in the art. Therefore, in the present invention, any sequence obtained by converting an amino acid into a D-form amino acid and having the characteristics described in the present invention is within the scope of the present invention.
Compared with the prior art, the invention has the beneficial effects that:
the antibacterial peptide has an inhibiting effect on gram-positive bacteria and gram-negative bacteria.
Polypeptide molecules are purified by a high-phase liquid chromatography to obtain a pure product, the pure product can realize effective bacteriostasis at a lower concentration, the bacteriostasis effect of certain antibacterial peptides (such as P2-9) and a glycopeptide named as vancomycin with the last line of defense of human is in the same order of magnitude, and compared with the vancomycin which can only treat gram-positive bacterial infection, the antibacterial peptide has the advantage of broad-spectrum antibacterial property.
Drawings
FIG. 1 is a hemolytic diagram of the antimicrobial peptide series 1 of the performance test 2 of the present invention;
FIG. 2 is a hemolytic diagram of the antimicrobial peptide series 2 of Performance test 2 of the present invention;
FIG. 3 is a SEM image of cells of performance test 3 of the present invention;
FIG. 4 is a confocal map of performance test 4 of the present invention;
FIG. 5 is a flow chart of Performance test 4 of the present invention;
FIG. 6 shows the resistance pattern of the polypeptides P2, P5, P2-10 and the control antibiotic ciprofloxacin.
Detailed Description
The technical solutions in the embodiments of the present invention will be clearly and completely described below with reference to the drawings in the embodiments of the present invention, and it is obvious that the described embodiments are only a part of the embodiments of the present invention, and not all of the embodiments. All other embodiments, which can be obtained by a person skilled in the art without making any creative effort based on the embodiments in the present invention, belong to the protection scope of the present invention.
Description of polypeptide Synthesis
The polypeptides of the present invention were synthesized by commercial companies.
Description of the reagents
Reagents used in the examples: mueller Hinton Broth (MH) medium, Tris, NaCl, human erythrocytes, Triton-X100, 2.5% glutaraldehyde, PBS, ethanol, PI dye, Hoechst dye are all conventional materials available from the market.
By the design of the applicant, hundreds of polypeptides prepared by entrusted commercial companies are screened, 80 polypeptides with possibly better performance are reserved, and 30 polypeptides are subjected to further performance verification.
The sequence of 30 polypeptides is shown in SEQ ID No. 1-SEQ ID No. 30;
the sequence of the parent peptide of Penetratin is shown in SEQ ID No. 30.
Specific information of SEQ ID Nos. 1 to 30 can be found in Table 1 below.
The performance verification is referred to the following performance tests 1-4.
TABLE 1 sequence information of the polypeptides
Performance test 1: evaluation of antibacterial Properties of antibacterial peptides
The antibacterial peptide powder is dissolved in sterile water to prepare a mother solution of 20 mg/mL. Add 100. mu.L (190. mu.L in the first well) of 5X 10 per well in 96-well plates 5 CFU/mL Mueller Hinton Broth (MH) medium of bacteria, the last well was an empty medium control without bacteria. mu.L of the polypeptide stock solution was added to the first well and diluted down sequentially by two-fold dilution to give polypeptide solutions with final concentrations of 0.97, 1.95, 3.9, 7.8, 15.6, 31.25, 62.5, 125, 250, 500 and 1000. mu.g/mL, three replicates per concentration. The 96-well plate was sealed with a sealing film and incubated at 37 ℃ for 20 hours. And detecting the light absorption value of each pore plate at 600nm by using a microplate reader. The bacteria used in the test of the present invention were 5 kinds in total, among them, gram-negative3 kinds of bacteria, namely Escherichia coli (e.coli), Pseudomonas aeruginosa (p.aeruginosa), Klebsiella pneumoniae (k.pneumoniae); the 2 gram-positive bacteria are Staphylococcus aureus (S. aureus) and Methicillin-resistant Staphylococcus aureus (MRSA), respectively.
The test results can be referred to in table 2 below.
Table 2 antibacterial property test results
Performance test 2: hemolytic evaluation of polypeptide molecules
Human erythrocytes were washed 3 times (4 ℃, 3400rpm, 10min) with buffer (10mM Tris, 150mM NaCl, pH 7.4). 75 μ L of 0.25% (v/v) suspension of human erythrocytes was mixed with an equal volume of 2 × polypeptide solution diluted in a gradient in a 96-well plate, three duplicate wells per concentration. Blood cells without added polypeptide and blood cells with 1% Triton-X100 buffer were used as negative and positive controls, respectively. After incubation at 50rpm for 1 hour at 37 ℃, centrifugation was carried out at 4000rpm for 10 minutes at 4 ℃. 100 μ L of supernatant per well was added to a new 96 well plate. Detecting the light absorption value at 415nm by a microplate reader, and calculating the hemolysis of the polypeptide by the following formula: (OD 415) Polypeptide treatment of human erythrocytes –OD Blank control red blood cells )/(OD415 Triton-X100 treatment of human erythrocytes- OD Blank control red blood cells )×100。
FIG. 1 shows the hemolytic patterns of P to P18;
FIG. 2 shows the hemolytic pattern of P-P2-11.
As can be seen from FIG. 1 and FIG. 2, except for P2-7 and P2-11, the hemolysis of other antibacterial peptides is lower than 50%, and the biosafety is high.
Performance test 3: effect of polypeptide molecules on bacterial morphology
Bacteria in logarithmic growth phase (Escherichia coli, Staphylococcus aureus, Klebsiella pneumoniae, Pseudomonas aeruginosa and methicillin-resistant Staphylococcus aureus) and polypeptide molecules of P2 or P2-10(1 × MIC) are blended, incubated at 37 deg.C for 5 or 24 hr, centrifuged at 3000rpm for 10min, and the supernatant is removed. The bacteria were fixed with 2.5% glutaraldehyde (PBS buffer dilution) overnight at 4 ℃. The samples were washed 3 times with PBS buffer and dehydrated with a series of ethanol solutions of different concentrations (30, 50, 70, 90, and 100%). And transferring the sample onto a conductive adhesive tape, drying, spraying gold, and observing by using a scanning electron microscope.
Wherein, the control refers to bacteria without being added with antibacterial peptide.
We can see from fig. 3 that: the bacteria treated by the polypeptide have obvious damage to cell membranes, including shrinkage and fragmentation of the cell membranes.
Performance test 4: effect of polypeptide molecules on bacterial Membrane Permeability
Bacteria in logarithmic growth phase (Escherichia coli, Staphylococcus aureus, Klebsiella pneumoniae, Pseudomonas aeruginosa and methicillin-resistant Staphylococcus aureus) and polypeptide molecules of P2 or P2-10(1 × MIC) were mixed, incubated at 37 deg.C for 24 hours, centrifuged at 3000rpm for 10min, and the supernatant was removed. The bacteria were washed 3 times with PBS buffer, stained with 50ug/mL PI for 15min, and PI-excited red fluorescence was detected by flow cytometry. In addition, 50ug/mL of PI and10 ug/mL of Hoechst dye were added to the treated bacterial suspension of P2 or P2-10, and after 15min of treatment, the mixture was transferred onto a glass slide, and the degree of coincidence of PI and Hoechst was observed under a confocal microscope.
FIG. 4 is a confocal view of P2 and P-10 according to the present invention;
FIG. 5 is a flow chart of P2 and P-10 of the present invention.
We can see from fig. 4 and 5 that: the experimental results show that the polypeptide molecule can destroy the bacterial cell membrane.
And (5) performance test: drug resistance exploration of polypeptide molecules
The MIC values of polypeptides and the control antibiotic ciprofloxacin against staphylococcus aureus were tested according to the method of test 1. The bacteria in wells with maximal polypeptide concentration and visible bacteria survival were diluted 1/10000-fold with fresh medium, inoculated into new 96-well plates, and incubated for 24h with 2-fold dilution of the polypeptide or antibiotic. Subculture was continued for 21 days as described above.
FIG. 6 is a graph of the resistance of the P2, P5, P-10 and the control antibiotic ciprofloxacin of the present invention.
We can see by figure 6 that: the experimental results show that compared with ciprofloxacin antibiotic, the polypeptide molecule of the invention is not easy to generate drug resistance.
To summarize:
1. compared with the parent peptide, the polypeptide of the invention has the advantages that the concentration of the polypeptide can be as low as 2-15% of the concentration of the parent peptide under the condition of the same antibacterial effect, and is 2-8% in most cases, and compared with the improvement of the antibacterial performance of 25-50% after the traditional cell-penetrating peptide is modified, the antibacterial effect can be remarkably improved. The antibacterial effect of some antibacterial peptides (such as P2-9) and a glycopeptide named as vancomycin with the last line of defense of human is in the same order of magnitude, and compared with the vancomycin which can only treat gram-positive bacterial infection, the antibacterial peptide has the advantage of broad-spectrum antibacterial property.
It should be noted that, for those skilled in the art, for modifying polypeptides with the same chain length to achieve an improvement in antibacterial effect, the MIC may be generally 25% to 50% of the original parent peptide; in the SEQ ID No. 1-SEQ ID No.20, the MIC of at least one of the polypeptides in the antibacterial property of a certain bacterium can be reduced to about 6% of the parent peptide, and most of the polypeptides can reach 1-3%.
Specifically, it is to be noted that: the polypeptides P2, P3-P5, P9, P14, P15, P2-2 to P2-11 all achieve very excellent effects in 5 antibacterial tests.
Among them, P2, P4, P5, P14, P15, P2-2, P2-6, P2-9 and P2-10 are particularly the same.
2. From the existing experimental results, the screening of the polypeptide has randomness. Changes in amino acids at other positions may result in changes in antimicrobial properties, except for the amino acids at positions 4-8 of the parent peptide.
In particular, the polypeptides shown in SEQ ID No. 21-SEQ ID No.29 of the present invention do not show antibacterial activity obviously superior to that of the parent peptide, and the selection of the polypeptides in the present invention is random, so that extensive experiments are required to determine the selection of several amino acid changes, the selection of amino acid changes at which positions, and the selection of which amino acid replaces the original amino acid.
3. The polypeptide has very high safety and wide application prospect.
4. The chain length of the polypeptide is consistent with that of the parent peptide, and the polypeptide has a spiral structure similar to that of the parent peptide, so that the cell destruction performance is reserved.
In summary, the outstanding contribution of the scheme is as follows: the antibacterial property is greatly improved while the cell membrane penetrating property of the parent peptide is kept, and the aims of broad-spectrum antibacterial property and difficult generation of drug resistance are achieved.
It will be evident to those skilled in the art that the invention is not limited to the details of the foregoing illustrative embodiments, and that the present invention may be embodied in other specific forms without departing from the spirit or essential attributes thereof. The present embodiments are therefore to be considered in all respects as illustrative and not restrictive, the scope of the invention being indicated by the appended claims rather than by the foregoing description, and all changes which come within the meaning and range of equivalency of the claims are therefore intended to be embraced therein. Any reference sign in a claim should not be construed as limiting the claim concerned.
Sequence listing
<110> university of Hunan
<120> an antibacterial peptide
<160> 30
<170> SIPOSequenceListing 1.0
<210> 1
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
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Arg Trp Ile Lys Ile Trp Phe Gln Ile Arg Arg Trp Lys Trp Lys Lys
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<210> 2
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 2
Arg Gln Ile Lys Ile Trp Phe Gln Ile Arg Arg Trp Lys Trp Lys Lys
1 5 10 15
<210> 3
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 3
Arg Trp Ile Lys Ile Trp Phe Gln Ile Arg Arg Trp Lys Asn Lys Lys
1 5 10 15
<210> 4
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 4
Arg Gln Ile Lys Ile Trp Phe Gln Trp Arg Arg Trp Lys Trp Lys Lys
1 5 10 15
<210> 5
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 5
Arg Gln Ile Lys Ile Trp Leu Gln Ile Arg Arg Trp Lys Asn Lys Lys
1 5 10 15
<210> 6
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 6
Arg Trp Ile Lys Ile Gln Leu Gln Ile Arg Arg Trp Lys Asn Lys Lys
1 5 10 15
<210> 7
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 7
Arg Trp Ile Lys Ile Trp Phe Gln Asn Arg Arg Trp Lys Trp Lys Lys
1 5 10 15
<210> 8
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 8
Arg Trp Ile Lys Ile Trp Phe Gln Trp Arg Arg Trp Lys Trp Lys Lys
1 5 10 15
<210> 9
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 9
Arg Gln Ile Lys Ile Trp Phe Gln Ile Arg Arg Trp Lys Asn Lys Lys
1 5 10 15
<210> 10
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 10
Arg Trp Ile Lys Ile Gln Phe Gln Ile Arg Arg Trp Lys Asn Lys Lys
1 5 10 15
<210> 11
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 11
Arg Gln Ile Lys Ile Trp Phe Ile Trp Arg Lys Trp Arg Trp Lys Lys
1 5 10 15
<210> 12
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 12
Arg Trp Ile Lys Ile Trp Phe Gln Ile Arg Arg Trp Lys Trp Arg Lys
1 5 10 15
<210> 13
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 13
Arg Trp Ile Lys Ile Trp Phe Gln Ile Arg Arg Trp Arg Trp Lys Lys
1 5 10 15
<210> 14
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 14
Lys Trp Ile Lys Ile Trp Phe Gln Trp Arg Arg Trp Arg Trp Lys Lys
1 5 10 15
<210> 15
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 15
Lys Trp Ile Lys Ile Trp Phe Gln Trp Arg Arg Trp Lys Trp Lys Arg
1 5 10 15
<210> 16
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 16
Lys Trp Ile Lys Ile Trp Phe Ile Trp Arg Arg Ile Lys Trp Arg Lys
1 5 10 15
<210> 17
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 17
Lys Gln Ile Lys Ile Trp Phe Ile Trp Arg Arg Ile Lys Ile Lys Lys
1 5 10 15
<210> 18
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 18
Arg Gln Ile Lys Ile Trp Phe Gln Trp Lys Arg Ile Lys Trp Arg Arg
1 5 10 15
<210> 19
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 19
Arg Gln Ile Arg Ile Trp Phe Gln Trp Lys Arg Trp Lys Trp Lys Arg
1 5 10 15
<210> 20
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 20
Arg Trp Ile Lys Ile Trp Phe Ile Trp Arg Arg Trp Arg Trp Arg Lys
1 5 10 15
<210> 21
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 21
Arg Gln Ile Lys Ile Trp Phe Gln Asn Lys Lys Trp Lys Trp Lys Lys
1 5 10 15
<210> 22
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 22
Arg Gln Ile Lys Ile Trp Phe Gln Asn Arg Lys Trp Lys Trp Lys Lys
1 5 10 15
<210> 23
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 23
Arg Gln Ile Lys Ile Trp Phe Gln Asn Lys Arg Trp Lys Trp Lys Lys
1 5 10 15
<210> 24
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 24
Arg Gln Ile Lys Ile Trp Phe Gln Asn Arg Arg Trp Lys Trp Lys Lys
1 5 10 15
<210> 25
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 25
Arg Trp Ile Lys Ile Trp Phe Gln Asn Arg Arg Trp Lys Asn Lys Lys
1 5 10 15
<210> 26
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 26
Arg Gln Ile Lys Ile Trp Phe Gln Asn Arg Arg Trp Arg Trp Lys Lys
1 5 10 15
<210> 27
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 27
Arg Trp Ile Lys Ile Gln Leu Gln Asn Arg Arg Trp Lys Asn Lys Lys
1 5 10 15
<210> 28
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 28
Arg Trp Ile Lys Ile Gln Phe Gln Asn Arg Arg Trp Lys Asn Lys Lys
1 5 10 15
<210> 29
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 29
Arg Trp Ile Lys Ile Trp Phe Gln Trp Arg Lys Ile Arg Trp Lys Lys
1 5 10 15
<210> 30
<211> 16
<212> PRT
<213> Artificial sequence (Artificial sequence)
<400> 30
Arg Gln Ile Lys Ile Trp Phe Gln Asn Arg Arg Met Lys Trp Lys Lys
1 5 10 15
Claims (1)
1. An antimicrobial peptide, comprising:
(I) and an amino acid sequence as shown in any one of SEQ ID No. 1-SEQ ID No. 20;
or
(II) an amino acid sequence obtained by substituting, deleting and adding one or more amino acids in the amino acid sequence described in (I) or an amino acid sequence obtained by converting one or more amino acids in the amino acid sequence described in (I) into D-type amino acids, and the amino acid sequence has the same function with the amino acid sequence described in (I).
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202210171227.7A CN114907447B (en) | 2022-02-23 | 2022-02-23 | Antibacterial peptide |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202210171227.7A CN114907447B (en) | 2022-02-23 | 2022-02-23 | Antibacterial peptide |
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| Publication Number | Publication Date |
|---|---|
| CN114907447A true CN114907447A (en) | 2022-08-16 |
| CN114907447B CN114907447B (en) | 2023-07-25 |
Family
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|---|---|---|---|
| CN202210171227.7A Active CN114907447B (en) | 2022-02-23 | 2022-02-23 | Antibacterial peptide |
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| CN (1) | CN114907447B (en) |
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