CN107312080B

CN107312080B - Antibacterial peptide derived from GSDMD protein and application thereof

Info

Publication number: CN107312080B
Application number: CN201710603544.0A
Authority: CN
Inventors: 李继喜; 匡思运; 郑军
Original assignee: Fudan University
Current assignee: Fudan University
Priority date: 2017-07-23
Filing date: 2017-07-23
Publication date: 2021-02-26
Anticipated expiration: 2037-07-23
Also published as: CN107312080A

Abstract

The invention belongs to the technical field of biology, and particularly relates to an antibacterial peptide derived from GSDMD protein and application thereof. The antibacterial peptide provided by the invention is a polypeptide of M-N position of a human GSDMD protein sequence, or a derivative polypeptide which has at least more than 90% of homology after various substitutions, additions and/or deletions of amino acids of other amino acids except FHFYDAMDGQI in the polypeptide sequence; wherein M is an integer between 60 and 80, and N is an integer between 90 and 110. The antibacterial peptide disclosed by the invention has a high-efficiency antibacterial effect, has strong antibacterial activity on various bacteria including but not limited to gram-negative bacteria (escherichia coli and mycobacterium smegmatis) and gram-positive bacteria (staphylococcus aureus), and has the advantages of small molecular weight, simplicity in synthesis and better application value.

Description

Antibacterial peptide derived from GSDMD protein and application thereof

Technical Field

The invention belongs to the technical field of biology, and particularly relates to an antibacterial peptide derived from GSDMD protein and application thereof.

Background

Although traditional antibiotics have achieved some success in the treatment of bacterial infectious diseases, in recent years, due to abuse of antibiotics, more and more microorganisms have developed resistance to traditional antibiotics, which poses a great threat to human health. Therefore, it is necessary to develop a novel antibacterial agent.

Antimicrobial peptides (AMPs) originally refer to polypeptide substances with antimicrobial activity generated in the body of insects by induction, have extremely strong killing capability on bacteria, fungi and viruses, and are important components in a biological immune defense system. Compared with the traditional antibiotics, the antibacterial peptide has the advantages of small molecular weight, good thermal stability, good water solubility, wide antibacterial spectrum and difficult induction of drug resistance of bacteria.

The current research suggests that the antibacterial peptide may be mainly used to kill tumor cells and microorganisms through the mechanism of cell membrane attack: the most basic action mechanism of most antibacterial peptides is to destroy the structure of the plasma membrane of tumor cells or bacteria, cause massive exudation of intracellular water-soluble substances, and finally cause the death of the tumor cells and bacteria, and the structural characteristics of the antibacterial peptide molecules are important bases for ensuring the action of the mechanisms.

The inflammatory necrosis or scorching of cells is an immune defense reaction initiated by the body after sensing the infection of pathogenic microorganisms, and plays an important role in antagonizing and eliminating pathogenic infection and endogenous danger signals. Cell apoptosis is essentially a programmed cell necrosis: the cell membrane forms a hole, and the cell gradually swells until the cell membrane is broken, finally, a large amount of cell contents are released, and a strong inflammatory reaction is activated. Excessive cell scorch can induce a variety of auto-inflammatory and autoimmune diseases. Recent studies have shown that the occurrence of AIDS is also associated with cellular apoptosis. Cell apoptosis is thought to be mediated by two cysteine-containing aspartate proteolytic enzymes (caspases), including caspase-1 and caspase-4/5/11. Caspase-1 is activated by a complex called Inflammasome (inflamasome) upon sensing pathogenic signals, and is one of the most important pathways for cytoplasmic innate immunity. In the latest studies, gasdermin D (GSDMD) protein is a consensus substrate for the inflammatory protease Caspase.

GSDMD belongs to the gasdermin protein family, which also includes GSDMA, GSDMB, GSDMC, GSDME (DFNA 5), DFNB59, and the like. The N-terminal of the GSDMDM protein can mostly trigger cell apoptosis, and in the absence of infection, the protein is also kept in an inactive state through the self-inhibition of the N-terminal and the C-terminal. The N-terminal domain released by GSDMDM after being cut by inflammatory caspase is enough to trigger cell apoptosis; in general, the N-terminal and C-terminal domains interact strongly, leaving GSDMD in an inactive, self-inhibitory state. The expression of the genetically engineered GSDMD in the cell (insertion of other protease sites between the two domains) can lead the cell to generate the apoptosis under the stimulation of other proteases, and even can convert the apoptosis into the apoptosis. These results all demonstrate that the N-terminal domain of GSDMD has activity to induce apoptosis in cells.

In addition, early termination mutations (translation into fragments that induce apoptosis) in human GSDME (DFNA 5) and mouse Gsdma3 in the gasdermin family lead to diseases such as non-syndromic deafness (Nonsyndromic hearing impairment) in humans and mice, and skin inflammation, respectively, suggesting that these diseases are caused by abnormal cell apoptosis induced by gasdermin protein. Therefore, a brand-new drug target is provided for various autoinflammatory diseases and endotoxin induced septicemia, and a novel antibacterial mechanism is provided for resisting the drug resistance of bacteria.

Disclosure of Invention

The invention aims to overcome the defects of the traditional antibiotics, provides an antibacterial peptide from human GSDMD protein, and also provides an amino acid sequence of the antibacterial peptide, an antibacterial activity detection method and application thereof.

The antibacterial peptide is polypeptide of M-N position of a human GSDMDM protein (shown in Seq ID No.1) sequence, or derivative polypeptide with homology of at least 90% after various amino acid substitutions, additions and/or deletions are carried out on other amino acids except FHFYDAMDGQI in the polypeptide sequence of M-N position; wherein M is an integer between 60 and 80, and N is an integer between 90 and 110.

Preferably, the antibacterial peptide is a polypeptide of M-N position of a human GSDMD protein (Seq ID No.1) sequence or a derivative polypeptide of the M-N position polypeptide sequence with at least 95% homology after various amino acid substitutions, additions and/or deletions are carried out on other amino acids except FHFYDAMDGQI sequence; wherein M is selected from integers between 70 and 80, and N is selected from integers between 90 and 100.

Preferably, the antibacterial peptide is a polypeptide of M-N position of the human GSDMD protein sequence or a derivative polypeptide of the polypeptide sequence with at least 99% homology after various substitutions, additions and/or deletions of amino acids of other amino acids except FHFYDAMDGQI; wherein M is selected from integers between 70 and 80, and N is selected from integers between 90 and 100.

The invention relates to a derivative polypeptide which has at least more than 90% of homology after various substitutions, additions and/or deletions of amino acids of other amino acids except FHFYDAMDGQI in the polypeptide at M-N position of a human GSDMDM protein (Seq ID No.1) sequence, preferably comprises artificial variants with no more than 3 amino acids substituted, deleted and/or inserted, more preferably mutants with no more than 2 amino acids, and most preferably mutation of only 1 amino acid. Examples of conservative substitutions are within the following groups: the basic amino acid group (arginine, lysine and histidine), the acidic amino acid group (glutamic acid and aspartic acid), the polar amino acid group (glutamine and asparagine), the hydrophobic amino acid group (leucine, isoleucine and valine), the aromatic amino acid group (phenylalanine, tryptophan and tyrosine) and the small amino acid group (glycine, alanine, serine, threonine and methionine). Amino acid substitutions that do not generally alter specific activity are known in The art and are described, for example, by H.Neurath and R.L. Hill, 1979, in The Proteins, Academic Press, New York. The most commonly occurring exchanges are Ala/Ser, Val/Ile, Asp/Glu, Thr/Ser, Ala/Gly, Ala/Thr, Ser/Asn, Ala/Val, Ser/Gly, Tyr/Phe, Ala/Pro, Lys/Arg, Asp/Asn, Leu/Ile, Leu/Val, Ala/Glu, Asp/Gly, and the like.

More preferably, the antibacterial peptide is a polypeptide of human GSDMDM protein (Seq ID No.1) sequence M-N position, wherein M is 80, and N is selected from an integer between 90-100.

More preferably, the antibacterial peptide is a polypeptide of human GSDMDM protein (Seq ID No.1) sequence M-N position, wherein M is an integer between 70 and 80, and N is 90.

More preferably, the antibacterial peptide of the present invention is a polypeptide of human GSDMDM protein (Seq ID No.1) sequence 80-90, and the sequence of the antibacterial peptide is FHFYDAMDGQI.

More preferably, the antibacterial peptide of the present invention is a polypeptide of 70-90 th position of the sequence of human GSDMDM protein (Seq ID No.1), and the sequence of the antibacterial peptide is AEPDVQRGRSFHFYDAMDGQI.

Preferred antimicrobial peptides of the invention also include the following polypeptides:

SFHFYDAMDGQI（Seq ID No.2）；

RSFHFYDAMDGQI（Seq ID No.3）；

GRSFHFYDAMDGQI（Seq ID No.4）；

RGRSFHFYDAMDGQI（Seq ID No.5）；

QRGRSFHFYDAMDGQI（Seq ID No.6）；

VQRGRSFHFYDAMDGQI（Seq ID No.7）；

DVQRGRSFHFYDAMDGQI（Seq ID No.8）；

PDVQRGRSFHFYDAMDGQI（Seq ID No.9）；

EPDVQRGRSFHFYDAMDGQI（Seq ID No.10）。

according to the literature, the N-terminal domain of GSDMD has bacteriostatic activity but no toxicity to the cells of human body. From the results of the present study, it is not known which region of the N-terminus of GSDMD is capable of inhibiting bacteria. To find out the bacteriostatic region, we constructed truncations of different lengths by using GSDMDM sequence as a template, respectively linked to pSMT3 vector with His-sumo tag, and transformed it into E.coli (Escherichia coli) The cells were plated on LB medium solid plates supplemented with 37. mu.g/ml of resistant chloramphenicol and 50. mu.g/ml of kanamycin and IPTG at a final concentration of 0.5mM, and cultured in a 37 ℃ incubator for 20 hours, and the range of the inhibitory region was finally determined based on the growth state of colonies on the plates.

The results in FIG. 1 show that the full-length GSDMD protein has no bacteriostatic effect, and the GSDMD protein sequences 90-185, 185-275 and 1-64+94-295 also have no bacteriostatic effect.

In contrast, the GSDMDM protein sequences 1-90, 70-205, 70-90, 70-85, 70-80 and 80-90 show bacteriostatic effects.

Therefore, through continuous search, the inventor unexpectedly finds that the amino acid sequence 80-90 (antimicrobial peptide 1, FHFYDAMDGQI) of the human GSDMD protein is the core bacteriostatic region of the GSDMD end domain. The artificially synthesized antibacterial peptide 1 consists of 11 amino acids, has an amino acid sequence of FHFYDAMDGQI (Seq ID No. 11), a molecular weight of 1343.48Da and an isoelectric point of 4.20. In vitro experiments prove that the antibacterial peptide 1 (FHFYDAMDGQI) has strong antibacterial activity on bacteria, including but not limited to escherichia coli, mycobacterium smegmatis, staphylococcus aureus and the like.

It was further verified that other short peptides comprising antimicrobial peptide 1 (FHFYDAMDGQI) also have antimicrobial activity, for example, the GSDMDM protein sequence 70-90 shown in FIG. 1 has antimicrobial activity. The inventor artificially synthesizes antibacterial peptide 2 containing an antibacterial peptide 1 (FHFYDAMDGQI) sequence, the amino acid sequence of the antibacterial peptide is AEPDVQRGRSFHFYDAMDGQI (Seq ID No. 12), the antibacterial peptide consists of 21 amino acids, the molecular weight of the antibacterial peptide is 2439.64Da, and the isoelectric point of the antibacterial peptide is 4.66. In vitro experiments prove that the antibacterial peptide 2 has strong antibacterial activity on bacteria, including but not limited to escherichia coli, mycobacterium smegmatis, staphylococcus aureus and the like.

To further verify that the polypeptide comprising the core sequence of the GSDMD protein 70-80 also has antibacterial activity, the inventors further artificially synthesized antibacterial peptide 3 (AEPDVQRGRSF) having an amino acid sequence of AEPDVQRGRSF (Seq ID No. 13), consisting of 11 amino acids, and having a molecular weight of 1398.51 Da. In vitro experiments prove that the antibacterial peptide 3 has strong antibacterial activity on bacteria, including but not limited to escherichia coli, mycobacterium smegmatis, staphylococcus aureus and the like.

To further verify that the polypeptide comprising the core sequence of GSDMD protein 70-85 also had antibacterial activity, the inventors further artificially synthesized antibacterial peptide 4 (AEPDVQRGRSFHFYDA) having an amino acid sequence of AEPDVQRGRSFHFYDA (Seq ID No. 14), consisting of 16 amino acids, and having a molecular weight of 1895.03 Da. In vitro experiments prove that the antibacterial peptide 4 has strong antibacterial activity on bacteria, including but not limited to escherichia coli, mycobacterium smegmatis, staphylococcus aureus and the like.

The invention further verifies the application of the antibacterial peptide in inhibiting the bacterial reproduction. The antibacterial peptide has good growth inhibition activity on bacteria through detection, and the antibacterial peptide comprises but is not limited to gram-negative bacteria (escherichia coli, mycobacterium smegmatis and the like) and gram-positive bacteria (staphylococcus aureus and the like). The absorbance at 600nm was measured by adding appropriate amounts of bacteria in the logarithmic growth phase to sterile 96-well plates, adding varying concentrations of antimicrobial peptide, and shaking-culturing at 37 ℃ and 220rpm at 150-. Has good bacteriostatic activity against different bacteria, such as Escherichia coli, Mycobacterium smegmatis, Staphylococcus aureus, etc., and has a minimum inhibitory concentration of 0.5 nM-31.25. mu.M.

In a preferred embodiment of the present invention, the present invention provides assays for the inhibition of growth activity of antimicrobial peptide 1 (FHFYDAMDGQI), antimicrobial peptide 2 (AEPDVQRGRSFHFYDAMDGQI), antimicrobial peptide 3 (AEPDVQRGRSF), and antimicrobial peptide 4 (AEPDVQRGRSFHFYDA) against bacteria, including but not limited to, e.

The invention has the advantage of providing the antibacterial peptide from human and the function of the antibacterial peptide in the aspect of bacteriostasis. The antibacterial peptide has high-efficiency antibacterial action, strong antibacterial activity on bacteria, small molecular weight, simple synthesis and good application value, and can be used for preparing medicines for inhibiting bacterial reproduction.

Drawings

FIG. 1 shows the results of the analysis of the GSDMD bacteriostatic area. The analysis result of the GSDMD bacteriostatic area shows that the amino acid sequences 70-80, 70-85, 80-90 and 70-90 can inhibit the growth of bacteria.

FIG. 2 shows the results of the assay of antibacterial peptide 1 (FHFYDAMDGQI) for inhibiting E.coli activity, indicating that the minimum inhibitory concentration is 0.5 nM.

FIG. 3 shows the result of the analysis of the inhibitory activity of antibacterial peptide 1 (FHFYDAMDGQI) against Mycobacterium smegmatis, which shows that the minimum inhibitory concentration is 0.5 nM.

FIG. 4 shows the activity of antibacterial peptide 1 (FHFYDAMDGQI) in inhibiting Staphylococcus aureus. The results showed a minimum inhibitory concentration of 8 nM.

FIG. 5 shows the results of the assay of antibacterial peptide 2 (AEPDVQRGRSFHFYDAMDGQI) for inhibiting E.coli activity, which showed a minimum inhibitory concentration of 31.25. mu.M.

FIG. 6 shows the result of the analysis of the inhibitory activity of antibacterial peptide 2 (AEPDVQRGRSFHFYDAMDGQI) against Mycobacterium smegmatis, which shows that the minimum inhibitory concentration is 0.5 nM.

FIG. 7 shows the activity of antimicrobial peptide 2 (AEPDVQRGRSFHFYDAMDGQI) in inhibiting Staphylococcus aureus. The results showed a minimum inhibitory concentration of 0.5 nM.

FIG. 8 shows the experiment of antibacterial peptide 3 (AEPDVQRGRSF) inhibiting the activity of Escherichia coli. The results showed a minimum inhibitory concentration of 0.5 nM.

FIG. 9 shows the activity of antibacterial peptide 3 (AEPDVQRGRSF) in inhibiting Staphylococcus aureus. The results showed a minimum inhibitory concentration of 0.5 nM.

FIG. 10 shows the experiment of antibacterial peptide 4 (AEPDVQRGRSFHFYDA) inhibiting the activity of E.coli. The results showed a minimum inhibitory concentration of 0.5 nM.

FIG. 11 shows the activity of antimicrobial peptide 4 (AEPDVQRGRSFHFYDA) in inhibiting Staphylococcus aureus. The results showed a minimum inhibitory concentration of 0.5 nM.

Detailed Description

Example 1: discovery of humanized antibacterial peptide

From the results of fig. 1, it can be analyzed that the four regions of amino acid sequences 80 to 90 (antimicrobial peptide 1, FHFYDAMDGQI), 70 to 90 (antimicrobial peptide 2, AEPDVQRGRSFHFYDAMDGQI), 70 to 80 (antimicrobial peptide 3, AEPDVQRGRSF) and 70 to 85 (antimicrobial peptide 4, AEPDVQRGRSFHFYDA) are the inhibitory regions of the GSDMD end domain.

Example 2: synthesis and identification of antibacterial peptide

Antimicrobial peptide 1 (FHFYDAMDGQI), antimicrobial peptide 2 (AEPDVQRGRSFHFYDAMDGQI), antimicrobial peptide 3 (AEPDVQRGRSF) and antimicrobial peptide 4 (AEPDVQRGRSFHFYDA) were provided by shanghai hao qiao corporation, with a purity of greater than 90%.

Example 3: detection of antibacterial peptide activity against Escherichia coli

An appropriate amount of E.coli in logarithmic growth phase was added to a sterile 96-well plate to make the total volume reach 200. mu.l, and the final concentration of the antimicrobial peptide reached 500. mu.M, 125. mu.M, 31.25. mu.M, 8. mu.M, 2. mu.M, 488nM, 122nM, 30nM, 8nM, 2nM, 0.5nM, 0nM, and the absorbance at 600nM was measured by shaking culture at 150-220rpm at 37 ℃.

As shown in FIG. 2, the result of the antibacterial peptide 1 (FHFYDAMDGQI) inhibiting the activity of Escherichia coli shows that the minimum inhibitory concentration is 0.5 nM.

As shown in FIG. 5, the inhibitory concentration of antimicrobial peptide 2 (AEPDVQRGRSFHFYDAMDGQI) was 31.25. mu.M, as a result of inhibiting E.coli activity.

The results of the antibacterial peptide 3 (AEPDVQRGRSF) inhibiting the activity of Escherichia coli in FIG. 8 show that the minimum inhibitory concentration is 0.5 nM.

FIG. 10 shows the inhibition of Escherichia coli activity by antibacterial peptide 4 (AEPDVQRGRSFHFYDA). The results showed a minimum inhibitory concentration of 0.5 nM.

Example 4: detection of activity of antibacterial peptide against mycobacterium smegmatis

An appropriate amount of Mycobacterium smegmatis in the logarithmic growth phase is added into a sterile 96-well plate, so that the total volume reaches 200 mu l, the final concentration of the antibacterial peptide reaches 500 mu M, 125 mu M, 31.25 mu M, 8 mu M, 2 mu M, 488nM, 122nM, 30nM, 8nM, 2nM, 0.5nM and 0nM, and the light absorption value at 600nM is detected by shaking culture at 150-220rpm under the condition of 37 ℃.

As shown in FIG. 3, the minimum inhibitory concentration of antibacterial peptide 1 (FHFYDAMDGQI) was 0.5nM as a result of its inhibitory activity against M.smegmatis.

As shown in FIG. 6, the minimum inhibitory concentration of antibacterial peptide 2 (AEPDVQRGRSFHFYDAMDGQI) was 0.5nM as a result of its inhibition of M.smegmatis activity.

Example 5: detection of activity of antibacterial peptide against staphylococcus aureus

Adding a proper amount of staphylococcus aureus in the logarithmic growth phase into a sterile 96-well plate to ensure that the total volume reaches 200 mu l, the final concentration of the antibacterial peptide reaches 500 mu M, 125 mu M, 31.25 mu M, 8 mu M, 2 mu M, 488nM, 122nM, 30nM, 8nM, 2nM, 0.5nM and 0nM, carrying out shaking culture at 150-220rpm under the condition of 37 ℃, and detecting the light absorption value at 600 nM.

FIG. 4 antimicrobial peptide 1 (FHFYDAMDGQI) inhibits Staphylococcus aureus activity assay. The results showed a minimum inhibitory concentration of 8 nM.

FIG. 7 antimicrobial peptide 2 (AEPDVQRGRSFHFYDAMDGQI) was tested for its ability to inhibit Staphylococcus aureus activity. The results showed a minimum inhibitory concentration of 0.5 nM.

FIG. 9 shows that antibacterial peptide 3 (AEPDVQRGRSF) inhibits Staphylococcus aureus activity. The results showed a minimum inhibitory concentration of 0.5 nM.

FIG. 11 antimicrobial peptide 4 (AEPDVQRGRSFHFYDA) inhibits Staphylococcus aureus activity assay. The results showed a minimum inhibitory concentration of 0.5 nM.

Therefore, the antibacterial peptide 1 has better inhibitory effect on escherichia coli, mycobacterium smegmatis and staphylococcus aureus, and the minimum inhibitory concentration is 0.5 nM. The antibacterial peptide 2 has better inhibitory effect on mycobacterium smegmatis and staphylococcus aureus, and the minimum inhibitory concentration is 0.5 nM. The antibacterial peptides 3 and 4 have good inhibition effect on escherichia coli and staphylococcus aureus, and the minimum inhibition concentration is 0.5 nM. Therefore, the antibacterial peptide 1 (FHFYDAMDGQI), the antibacterial peptide 2 (AEPDVQRGRSFHFYDAMDGQI), the antibacterial peptide 3 (AEPDVQRGRSF) and the antibacterial peptide 4 (AEPDVQRGRSFHFYDA) are expected to have good application prospects in the aspect of medicines for treating bacterial diseases.

In conclusion, the invention provides a natural antibacterial peptide from human and the function of the natural antibacterial peptide in bacteriostasis. The antibacterial peptide has high-efficiency antibacterial action, has strong antibacterial activity on bacteria, and has good prospect in the aspect of replacing antibiotics to treat bacterial diseases.

Sequence listing

<110> university of Compound Dan

<120> antibacterial peptide derived from GSDMD protein and application thereof

<160> 1

<170> PatentIn version 3.3

<210> 1

<211> 484

<212> PRT

<213> Homo sapiens (Human)

<400> 1

MGSAFERVVR RVVQELDHGG EFIPVTSLQS STGFQPYCLV VRKPSSSWFW 50

KPRYKCVNLS IKDILEPDAA EPDVQRGRSF HFYDAMDGQI QGSVELAAPG 100

QAKIAGGAAV SDSSSTSMNV YSLSVDPNTW QTLLHERHLR QPEHKVLQQL 150

RSRGDNVYVV TEVLQTQKEV EVTRTHKREG SGRFSLPGAT CLQGEGQGHL 200

SQKKTVTIPS GSTLAFRVAQ LVIDSDLDVL LFPDKKQRTF QPPATGHKRS 250

TSEGAWPQLP SGLSMMRCLH NFLTDGVPAE GAFTEDFQGL RAEVETISKE 300

LELLDRELCQ LLLEGLEGVL RDQLALRALE EALEQGQSLG PVEPLDGPAG 350

AVLECLVLSS GMLVPELAIP VVYLLGALTM LSETQHKLLA EALESQTLLG 400

PLELVGSLLE QSAPWQERST MSLPPGLLGN SWGEGAPAWV LLDECGLELG 450

EDTPHVCWEP QAQGRMCALY ASLALLSGLS QEPH 484

<210> 2

<211> 12

<212> PRT

<213> Artificial

<400> 2

SFHFYDAMDG QI 12

<210> 3

<211> 13

<212> PRT

<213> Artificial

<400> 3

RSFHFYDAMD GQI 13

<210> 4

<211> 14

<212> PRT

<213> Artificial

<400> 4

GRSFHFYDAM DGQI 14

<210> 5

<211> 15

<212> PRT

<213> Artificial

<400> 5

RGRSFHFYDA MDGQI 15

<210> 6

<211> 16

<212> PRT

<213> Artificial

<400> 6

QRGRSFHFYD AMDGQI 16

<210> 7

<211> 17

<212> PRT

<213> Artificial

<400> 7

VQRGRSFHFY DAMDGQI 17

<210> 8

<211> 18

<212> PRT

<213> Artificial

<400> 8

DVQRGRSFHF YDAMDGQI 18

<210> 9

<211> 19

<212> PRT

<213> Artificial

<400> 9

PDVQRGRSFH FYDAMDGQI 19

<210> 10

<211> 20

<212> PRT

<213> Artificial

<400> 10

EPDVQRGRSF HFYDAMDGQI 20

<210> 11

<211> 11

<212> PRT

<213> Artificial

<400> 11

FHFYDAMDGQ I 11

<210> 12

<211> 21

<212> PRT

<213> Artificial

<400> 12

AEPDVQRGRS FHFYDAMDGQ I 21

<210> 13

<211> 11

<212> PRT

<213> Artificial

<400> 13

AEPDVQRGRS F 11

<210> 14

<211> 16

<212> PRT

<213> Artificial

<400> 14

AEPDVQRGRS FHFYDA 16

Claims

1. An antibacterial peptide, which is a polypeptide at M-N position of a human GSDMDM protein sequence, wherein M is an integer between 60 and 80, and N is an integer between 90 and 110; the amino acid sequence of the polypeptide is shown as any one of Seq ID No.2-Seq ID No. 14.

2. Use of the antimicrobial peptide of claim 1 for the preparation of a medicament for inhibiting bacterial reproduction; the bacteria is Escherichia coli, Mycobacterium smegmatis or Staphylococcus aureus.