Self-assembled antibacterial peptide IL-9-Lau and application thereof

Abstract

The invention belongs to the technical field of antibacterial peptides, and particularly relates to a self-assembled antibacterial peptide IL-9-Lau and application thereof. The self-assembled antibacterial peptide IL-9-Lau disclosed by the invention comprises a polypeptide main chain and lauric acid, the lauric acid is connected with a side chain amino group of lysine at the tail end C of the polypeptide main chain amino acid sequence through an amido bond. A polypeptide main chain is connected with lauric acid, self-assembly driving force is provided for the polypeptide main chain by means of strong hydrophobicity of lauric acid, the polypeptide main chain is in a nano-particle state under an electron microscope, the average particle size is 11.81 nm, and the critical micelle concentration is 129.18 mu M; moreover, the self-assembled antibacterial peptide IL-9-Lau is good in stability, free of obvious cytotoxicity and hemolysis and broad-spectrum antibacterial property, and the minimum inhibitory concentration of the self-assembled antibacterial peptide IL-9-Lau to acinetobacter baumannii, escherichia coli, pseudomonas aeruginosa and staphylococcus aureus is 1.2-4.7 mu M.

Description

Technical Field

[0001] The present invention belongs to the technical field of antimicrobial peptides, and particularly relates to a self-assembled antimicrobial peptide IL-9-Lau and its application. Background Art

[0002] Microbial infections, including bacteria, fungi, viruses, etc., can cause many very serious human diseases, including hepatitis, pneumonia, AIDS, tuberculosis, etc. Infectious epidemics caused by pathogenic microorganisms have always been one of the important causes of human death. Since the invention of antibiotics, countless lives of patients with bacterial infections have been saved. However, the extensive use of antibiotics has given rise to a large number of antibiotic-resistant strains.

[0003] Antimicrobial peptides (AMPs) are a class of small molecule polypeptides that can inhibit the growth of bacteria, fungi, viruses, etc. They are widely present in organisms and are an important part of the innate immune system. They not only are not easily induced to produce drug resistance in bacteria, but also exhibit advantages such as broad-spectrum antibacterial activity, high efficiency at low concentrations, and immunomodulation. However, not any small molecule polypeptide has antibacterial activity. Even if it has antibacterial activity, there are many limitations in actual production applications. The essence of antimicrobial peptides is a polypeptide chain, which results in the sensitivity of antimicrobial peptides to the environment. The ionic concentration and the presence of enzymes will affect the structure and bactericidal effect of the polypeptide, resulting in instability in actual applications, as well as unknown hemolytic activity and cytotoxicity, etc., which severely limit the development of antimicrobial peptides as antibacterial drugs. Therefore, improving the stability and safety of antimicrobial peptides is particularly important in this field. Summary of the Invention

[0004] The purpose of the present invention is to provide a self-assembled antimicrobial peptide IL-9-Lau with good stability, no obvious cytotoxicity and hemolytic effect, having strong and broad-spectrum antibacterial activity and a low minimum inhibitory concentration.

[0005] The present invention provides a self-assembled antimicrobial peptide IL-9-Lau, and the self-assembled antimicrobial peptide IL-9-Lau includes a polypeptide backbone and lauric acid; The polypeptide backbone includes the amino acid sequence shown in SEQ ID NO:1; The lauric acid is connected to the side-chain amino group of the C-terminal lysine of the amino acid sequence shown in SEQ ID NO:1 through an amide bond.

[0006] Preferably, the polypeptide backbone is composed of a linear polypeptide and a linker; the linear polypeptide and the linker are connected through an amide bond; The amino acid sequence of the linear polypeptide is shown in SEQ ID NO:2; The amino acid sequence of the linker is GK.

[0007] The present invention also provides the application of the self-assembled antibacterial peptide IL-9-Lau described in the above technical solution in the preparation of antibacterial products.

[0008] Preferably, the antibacterial product includes antibacterial infection products.

[0009] Preferably, the bacteria include Gram-negative bacteria and / or Gram-positive bacteria.

[0010] Preferably, the Gram-negative bacteria include Acinetobacter baumannii ( Acinetobacter baumannii ), Pseudomonas aeruginosa ( Pseudomonas aeruginosa ), and Escherichia coli ( Escherichia coli ), or one or more of them.

[0011] Preferably, the Gram-positive bacteria include Staphylococcus aureus ( Staphylococcus aureus ).

[0012] Preferably, the product includes a reagent or a drug. The present invention provides an antibacterial product, and the antibacterial product includes the self-assembled antibacterial peptide IL-9-Lau described in the above technical solution.

[0013] Preferably, the antibacterial product includes an antibacterial reagent or an antibacterial drug.

[0014] Beneficial effects: The present invention provides a self-assembled antibacterial peptide IL-9-Lau, which includes a polypeptide backbone and lauric acid; the polypeptide backbone includes the amino acid sequence shown in SEQ ID NO: 1; the lauric acid is connected to the side-chain amino group of the C-terminal lysine of the amino acid sequence shown in SEQ ID NO: 1 through an amide bond. The self-assembled antibacterial peptide IL-9-Lau of the present invention is connected by the polypeptide backbone and lauric acid, and relies on the strong hydrophobicity of lauric acid to provide a self-assembly driving force for the polypeptide backbone, presenting a nanoparticle state under an electron microscope, with an average particle size of 11.81 nm and a critical micelle concentration of 129.18 μM; moreover, the self-assembled antibacterial peptide IL-9-Lau obtained in the present invention has good stability, no obvious cytotoxicity and hemolytic effect, has broad-spectrum antibacterial properties, has strong antibacterial activity against both Gram-negative bacteria and Gram-positive bacteria, and the minimum inhibitory concentration against Acinetobacter baumannii, Escherichia coli, Pseudomonas aeruginosa and Staphylococcus aureus is 1.2-4.7 μM. Description of the drawings

[0015] In order to more clearly illustrate the technical solutions in the embodiments of the present invention or the prior art, the following will briefly introduce the drawings required for use in the embodiments.

[0016] Figure 1Transmission electron microscopy observation results and particle size statistics results of self-assembled antimicrobial peptide IL-9-Lau; among them, A is the transmission electron microscopy image, and B is the particle size statistics result graph; Figure 2 Critical micelle concentration determination results of self-assembled antimicrobial peptide IL-9-Lau; among them, A is the fluorescence intensity statistics result graph of gradient concentration self-assembled antimicrobial peptide IL-9-Lau at different wavelengths, and B is the Nile red fluorescence curve graph of gradient concentration self-assembled polypeptide IL-9-Lau; Figure 3 Cell viability detection results of self-assembled antimicrobial peptide IL-9-Lau at different concentrations on human embryonic kidney cells HEK293T; Figure 4 Cell viability detection results of linear polypeptide IL-9 at different concentrations on human embryonic kidney cells HEK293T; Figure 5 Hemolysis evaluation results of self-assembled antimicrobial peptide IL-9-Lau at different concentrations; Figure 6 Hemolysis evaluation results of linear polypeptide IL-9 at different concentrations. Detailed implementation mode

[0017] The present invention provides a self-assembled antimicrobial peptide IL-9-Lau, and the self-assembled antimicrobial peptide IL-9-Lau includes a polypeptide backbone and lauric acid; the polypeptide backbone includes the amino acid sequence shown in SEQ ID NO:1; the lauric acid is connected to the side chain amino group of the C-terminal lysine of the amino acid sequence shown in SEQ ID NO:1 through an amide bond. The present invention utilizes lauric acid, and the length of lauric acid is appropriate, which can not only increase the activity and promote self-assembly, but also will not significantly increase the toxicity. It is safer than other types of fatty acid chains with strong hydrophobicity, and the toxicity of the antimicrobial peptide is smaller after self-assembly.

[0018] As an implementation mode, the polypeptide backbone of the self-assembled antimicrobial peptide IL-9-Lau of the present invention is composed of a linear polypeptide and a linker; the linear polypeptide and the linker are connected through an amide bond; the amino acid sequence of the linear polypeptide is shown in SEQ IDNO:2; the amino acid sequence of the linker is GK. The present invention uses GK as the linker between the linear polypeptide and lauric acid, with a simple structure and no complex side chains, which can isolate the main peptide and fatty acid and will not affect the charge number, helicity, etc. of the linear polypeptide.

[0019] The self-assembling antibacterial peptide IL-9-Lau described in the present invention has a molecular weight of 1407.91 daltons, and all amino acids are of the L type. The self-assembling antibacterial peptide IL-9-Lau presents a nanoparticle state under an electron microscope, with an average particle size of 11.81 nm, a critical micelle concentration reaching 129.18 μM, good stability, no obvious cytotoxicity and hemolytic effect, and strong antibacterial activity against both Gram-negative bacteria and Gram-positive bacteria. The minimum inhibitory concentration against Acinetobacter baumannii, Escherichia coli, Pseudomonas aeruginosa and Staphylococcus aureus is 1.2 - 4.7 μM, showing strong broad-spectrum property. The present invention has no strict requirements for the preparation method of the antibacterial peptide, and conventional methods in the art can be used, such as solid-phase peptide synthesis. The present invention has no special requirements for the solid-phase peptide synthesis method, and methods well-known to those skilled in the art can be used.

[0020] The present invention also provides the application of the self-assembling antibacterial peptide IL-9-Lau described in the above technical solution in the preparation of antibacterial products.

[0021] As an embodiment, the antibacterial product is an antibacterial infection product. As an embodiment, the bacteria include Gram-negative bacteria and / or Gram-positive bacteria. As an embodiment, the Gram-negative bacteria include one or more of Acinetobacter baumannii, Pseudomonas aeruginosa and Escherichia coli; as another embodiment, the Gram-positive bacteria include Staphylococcus aureus.

[0022] As an embodiment, the Acinetobacter baumannii described in the present invention includes one or more of Acinetobacter baumannii ATCC 19606, 10769 and 0357; as another embodiment, the Acinetobacter baumannii described in the present invention is Acinetobacter baumannii ATCC 19606. In the examples of the present invention, Acinetobacter baumannii ATCC 19606, 10769 and 0357 are taken as examples for illustration, but it should not be understood as the entire protection scope of the present invention only.

[0023] As an embodiment, the Escherichia coli described in the present invention includes one or more of Escherichia coli ATCC 8739, 0894 and 5017; as another embodiment, the Escherichia coli described in the present invention is Escherichia coli ATCC 8739. In the examples of the present invention, Escherichia coli ATCC 8739, 0894 and 5017 are taken as examples for illustration, but it should not be understood as the entire protection scope of the present invention only.

[0024] As an implementation manner, the Pseudomonas aeruginosa described in the present invention includes one or more of Pseudomonas aeruginosa ATCC 27853, 90068, and 17068; as another implementation manner, the Pseudomonas aeruginosa described in the present invention is Pseudomonas aeruginosa ATCC27853. In the embodiments of the present invention, Pseudomonas aeruginosa ATCC 27853, 90068, and 17068 are taken as examples for illustration, but it should not be understood that this is the entire protection scope of the present invention.

[0025] As an implementation manner, the Staphylococcus aureus described in the present invention includes one or more of Staphylococcus aureus ATCC 6538, 220823, and 15775; as another implementation manner, the Staphylococcus aureus described in the present invention is Staphylococcus aureus ATCC 6538. In the embodiments of the present invention, Staphylococcus aureus ATCC 6538, 220823, and 15775 are taken as examples for illustration, but it should not be understood that this is the entire protection scope of the present invention.

[0026] In the present invention, the strains corresponding to the numbers 10769, 0357, 0894, 5017, 90068, 170682, 20823, and 15775 are known strains in the art, which are preserved in the Institute of Medical Biology, Chinese Academy of Medical Sciences and are disclosed in the prior art Development of α-Helical Antimicrobial Peptides with Imperfect Amphipathicity for Superior Activity and Selectivity. J Med Chem. 2024 Nov 14;67(21):19561-19572.

[0027] As an implementation manner, the product includes a reagent or a drug.

[0028] The present invention provides an antibacterial product, and the antibacterial product includes the self-assembled antibacterial peptide IL-9-Lau described in the above technical solution; the antibacterial product includes an antibacterial reagent or an antibacterial drug. As an implementation manner, the minimum inhibitory concentration of the antibacterial peptide in the antibacterial product is ≥1.2 μM; as another implementation manner, the minimum inhibitory concentration of the antibacterial peptide in the antibacterial product is 1.2 - 4.7 μM; as another implementation manner, the minimum inhibitory concentration of the antibacterial peptide in the antibacterial product is 1.2 - 2.3 μM; as another implementation manner, the minimum inhibitory concentration of the antibacterial peptide in the antibacterial product is 1.2 μM.

[0029] To further illustrate the present invention, a self-assembled antimicrobial peptide IL-9-Lau and its applications provided by the present invention will be described in detail below in conjunction with the accompanying drawings and embodiments, but they should not be construed as limiting the scope of protection of the present invention.

[0030] Example 1 Entrusted GIL Biochemicals (Shanghai) Co., Ltd. to synthesize a linear polypeptide IL-9 consisting of only 9 amino acids by solid-phase peptide synthesis method. Its amino acid sequence is IKKGIKKLL (SEQ ID NO:2), all of which are L-amino acids. In order to form nanoparticles by self-assembly of IL-9, a glycine-lysine (CK) was added to the C-terminus of the linear polypeptide as a linker to form a polypeptide backbone, and its amino acid sequence is IKKGIKKLLGK (SEQ ID NO:1); then the side-chain amino group of lysine in the linker and the carboxyl group of a lauric acid were connected by forming a peptide bond to obtain the self-assembled antimicrobial peptide IL-9-Lau; finally, it was desalted and purified by HPLC reverse-phase column chromatography to obtain the self-assembled antimicrobial peptide IL-9-Lau. The molecular weight of the IL-9-Lau is 1407.91 Daltons, and all amino acids are L-type.

[0031] Comparative Example 1 Entrusted GIL Biochemicals (Shanghai) Co., Ltd. to synthesize a linear polypeptide IL-9 consisting of only 9 amino acids by solid-phase peptide synthesis method. Its amino acid sequence is IKKGIKKLL (SEQ ID NO:2), all of which are L-amino acids.

[0032] Test Example 1 Transmission electron microscopy observation (1) Drop the solution containing the self-assembled antimicrobial peptide IL-9-Lau obtained in Example 1 on the smooth paper, clamp a 300-mesh copper grid with the carbon film side facing down, cover and adsorb for 5 minutes, and blot dry the excess liquid; after uranium staining (2%wt uranyl acetate) for 2 minutes, blot dry the excess staining solution, air dry, and observe and take pictures using a transmission electron microscope (model JEM-1400 Plus, JEOL Ltd., Japan). The results show that under the transmission electron microscope, the self-assembled antimicrobial peptide IL-9-Lau all presents a nanoparticle state, and the antimicrobial peptide IL-9-Lau can form nanoparticles by self-assembly ( Figure 1 in A).

[0033] (2) Data processing: Use Image J software to count the particle size of the nanoparticles, and use GraphPad Prism to make a particle size distribution map. The results show that the average particle size of the self-assembled antimicrobial peptide IL-9-Lau is 14.81 nm ( Figure 1 in B).

[0034] Test Example 2 Determination of Critical Micelle Concentration (CMC) (1) Add 100 μL of the self-assembled antibacterial peptide IL-9-Lau solution with gradient concentrations in Example 1 to a black-bottomed and clear-bottomed 96-well fluorescence microplate. Then add 100 μL of 25 μM nile red solution to each well. After mixing, let it stand at room temperature for 30 min, and scan the emission spectrum of the solution with a multi-functional microplate reader ( Figure 2 as shown in A).

[0035] Among them, the buffer solution used for preparing the nile red solution and the self-assembled antibacterial peptide IL-9-Lau solution with gradient concentrations is 10 mM phosphate buffer solution (pH value is 7.4); Fluorescence spectrum scanning conditions: excitation wavelength is 550 nm, emission wavelength is 600 - 700 nm, and bandwidth is 1 nm.

[0036] (2) Data processing: Take the logarithm of the concentration of the self-assembled antibacterial peptide IL-9-Lau as the abscissa, and the maximum fluorescence intensity of nile red at each concentration as the ordinate to plot the nile red fluorescence curve in the presence of the self-assembled antibacterial peptide IL-9-Lau with gradient concentrations (excitation wavelength is 550 nm, emission wavelength is 630 nm). The polypeptide concentration corresponding to the inflection point of the fluorescence curve is the minimum concentration at which the self-assembled antibacterial peptide IL-9-Lau begins to form micelles in aqueous solution, that is, the CMC value ( Figure 2 as shown in B).

[0037] According to Figure 2 It can be seen that the CMC value of the self-assembled antibacterial peptide IL-9-Lau is 129.18 μM. Nile red is a lipophilic fluorescent dye, and it can produce strong fluorescence after inserting into the hydrophobic pocket of the micelle. When the concentration of the self-assembled antibacterial peptide IL-9-Lau is higher than the CMC, it can induce a significant increase in the fluorescence of nile red in the solution, indicating that the self-assembled antibacterial peptide IL-9-Lau undergoes self-assembly in aqueous solution to form amphiphilic micelles with hydrophilic periphery and hydrophobic interior.

[0038] Test Example 3 Antibacterial Activity Analysis 1. Test Strains (1) Acinetobacter baumannii: ATCC 19606, 10769, and 0357; (2) Escherichia coli: ATCC 8739, 0894, and 5017; (3) Pseudomonas aeruginosa: ATCC 27853, 90068, and 17068; (4) Staphylococcus aureus: ATCC 6538, 220823, and 15775.

[0039] 2. Minimum Inhibitory Concentration (MIC) Detection First, inoculate the test strain onto an LB solid plate. After colonies grow, pick a single colony and transfer it to an LB liquid medium. Incubate it under the conditions of 37°C and 180 rpm for 5 h, and measure the OD of the bacterial solution with an ultraviolet spectrophotometer. 600 , and according to the ratio of 1 OD 600 = 1×10 9 CFU / mL, dilute the bacterial solution to a concentration of 2×10 5 CFU / mL with LB liquid medium; add 100 μL of the diluted bacterial solution to each well of a sterile 96-well plate. Subsequently, add 100 μL of the test sample diluted in gradient with normal saline to each well, mix well with a pipette, and then place it in a 37°C constant temperature incubator and incubate with slow shaking overnight; the test sample is the self-assembled antimicrobial peptide IL-9-Lau obtained in Example 1 and the linear polypeptide IL-9 obtained in Comparative Example 1; the concentration of the diluted test sample is 0 - 200 μg / mL; after incubation, measure the absorbance value of the bacterial solution at OD 600 nm with an enzyme-labeled instrument. Take the average value of the sample concentrations of the wells where bacteria growth cannot be detected and the adjacent wells as the MIC value. The results are shown in Table 1.

[0040] Table 1 Minimum inhibitory concentration values of the test samples against the test strain

[0041] It can be seen from Table 1 that the self-assembled antimicrobial peptide IL-9-Lau obtained in Example 1 showed significant antibacterial effects against all the tested strains, with MIC values of 1.2 - 4.7 μM. Compared with the linear polypeptide IL-9 in Comparative Example 1, the antibacterial activity changed from none (MIC > 50 μM) to some.

[0042] Test Example 4 Cytotoxicity analysis Routinely culture human embryonic kidney cells (HEK293T) with DMEM medium (containing 10% fetal bovine serum and 1% double antibody). When the cells grow to 80% of the culture flask, wash them 3 times with phosphate buffer first, then digest the cells with 0.25% trypsin, and prepare a cell suspension with a concentration of 5×10 5 cells / mL with DMEM culture solution. Add 200 μL of the cell suspension to each well of a sterile 96-well plate and continue to culture overnight; the next day, add test samples with different concentration gradients (final concentration of 0 - 100 μM) or the same volume of DMEM medium respectively. Set 3 replicates for each sample concentration, and continue to culture for 24 h. Then add 15 μL of MTT solution with a concentration of 5 mg / mL to each well, continue to culture in the dark for 4 h. Subsequently, aspirate the culture solution in the plate wells, add 200 μL of DMSO to each well, place the culture plate on a shaker and gently shake for 10 min to dissolve the crystals. Then measure the absorbance value of each well at 450 nm with an enzyme-labeled instrument. The results are asFigure 3 and Figure 4 As shown; wherein, the samples to be tested are the self-assembled antimicrobial peptide IL-9-Lau obtained in Example 1 and the linear polypeptide IL-9 obtained in Comparative Example 1.

[0043] according to Figure 3 and Figure 4 It can be seen that the linear polypeptide IL-9 obtained in Comparative Example 1 has no toxicity to human keratinocytes HaCaT within the tested concentration range; the self-assembled antimicrobial peptide IL-9-Lau obtained in Example 1 has no toxicity to human keratinocytes HaCaT within the concentration range of 50 μM, and only exhibits weak cytotoxicity at a concentration of 100 μM ( P <0.05). The present invention realizes the antibacterial activity of the linear polypeptide IL-9 from no (MIC>50μM) to yes through self-assembly, while having no cytotoxicity and good safety.

[0044] Test Example 6 Hemolysis assay 1. Mix fresh human whole blood and Aldrich solution in a volume ratio of 1:1, centrifuge at 1000rpm for 5min, discard the supernatant, wash the obtained red blood cells with physiological saline, repeat 3 times until the supernatant no longer appears red, and obtain the washed red blood cells.

[0045] 2. Dilute the washed red blood cells to 1×10 7 The red blood cell suspension was incubated with different concentrations (0-100 μM) of the test sample dissolved in physiological saline at 37°C for 30 min, and then centrifuged at 1000 rpm for 5 min. The absorbance of the supernatant was detected at 540 nm. The positive control used the same volume of Triton X-100 solution (PC), and the volume concentration of the Triton X-100 solution was 10%; the negative control used physiological saline; wherein the test sample was the self-assembled antimicrobial peptide IL-9-Lau obtained in Example 1 and the linear polypeptide IL-9 obtained in Comparative Example 1.

[0046] 3. Data processing: Detect the absorbance at 540nm, define the hemolysis rate of the positive control (PC group) as 100%, and calculate the hemolysis rate of the sample group to be tested relative to the PC group according to the following formula. The results are as follows: Figure 5 and Figure 6 shown.

[0047] Hemolysis rate (%) = (positive control OD 540 Value - negative control OD 540 value) / (OD of the sample group to be tested 540 Value - negative control OD 540 value) × 100%.

[0048] According to Figure 5 and Figure 6 It can be seen that the linear polypeptide IL-9 obtained in Comparative Example 1 and the self-assembled antimicrobial peptide IL-9-Lau obtained in Example 1 both show high safety to human red blood cells and have no significant hemolytic effect within the concentration range of 100 μM. By means of self-assembly, the present invention enables the antibacterial activity of the linear polypeptide IL-9 to change from non-existent (MIC > 50 μM) to existent, while having no significant hemolytic effect and good safety.

[0049] It can be seen from the above that the self-assembled antimicrobial peptide IL-9-Lau provided by the present invention has strong antibacterial activity against both Gram-negative bacteria and Gram-positive bacteria, good stability, strong broad-spectrum property, and extremely high safety, without either cytotoxicity or hemolytic effect.

[0050] Although the above embodiments have made a detailed description of the present invention, they are only a part of the embodiments of the present invention, rather than all embodiments. People can also obtain other embodiments based on these embodiments without creative efforts, and these embodiments all fall within the protection scope of the present invention.

Claims

1. A self-assembling antimicrobial peptide IL-9-Lau, characterized in that: The self-assembling antimicrobial peptide IL-9-Lau comprises a polypeptide main chain and lauric acid; The polypeptide backbone comprises the amino acid sequence shown in SEQ ID NO: 1; The lauric acid is connected to the side chain amino group of the C-terminal lysine in the amino acid sequence shown in SEQ ID NO: 1 through an amide bond.

2. The self-assembling antimicrobial peptide IL-9-Lau according to claim 1, characterized in that: The polypeptide main chain consists of a straight-chain polypeptide and a linker; the straight-chain polypeptide and the linker are connected by an amide bond; The amino acid sequence of the linear polypeptide is shown in SEQ ID NO: 2; The amino acid sequence of the linker is GK.

3. Use of the self-assembling antimicrobial peptide IL-9-Lau according to claim 1 or 2 in the preparation of antibacterial products.

4. The use according to claim 3, characterized in that: The anti-bacterial products include anti-bacterial infection products.

5. The use according to claim 3, characterized in that: The bacteria include Gram-negative bacteria and / or Gram-positive bacteria.

6. The use according to claim 5, characterized in that: The Gram-negative bacteria include Acinetobacter baumannii ( Acinetobacter baumannii )、Pseudomonas aeruginosa( Pseudomonas aeruginosa ) and Escherichia coli ( Escherichia coli ) 7. The use according to claim 5, characterized in that: The Gram-positive bacteria include Staphylococcus aureus ( Staphylococcus aureus ).

8. The use according to any one of claims 3 to 7, characterized in that: The product includes a reagent or a drug.

9. An antibacterial product, characterized in that: The antibacterial product comprises the self-assembling antimicrobial peptide IL-9-Lau according to claim 1 or 2.

10. The product according to claim 9, characterized in that The antibacterial product includes an antibacterial agent or an antibacterial drug.

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