A self-assembling antimicrobial peptide IL-9-Lau and its application

Abstract

The present invention belongs to the technical field of antimicrobial peptides, and specifically relates to a self-assembling antimicrobial peptide IL-9-Lau and its application. The self-assembling antimicrobial peptide IL-9-Lau of the present invention comprises a polypeptide backbone and lauric acid; the lauric acid is connected to the side-chain amino group of the lysine at the C-terminus of the amino acid sequence of the polypeptide backbone through an amide bond. By connecting the polypeptide backbone with lauric acid, the present invention 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-assembling antimicrobial peptide IL-9-Lau has good stability, no obvious cytotoxicity and hemolytic effect, has broad-spectrum antibacterial properties, and the minimum inhibitory concentrations against Acinetobacter baumannii, Escherichia coli, Pseudomonas aeruginosa and Staphylococcus aureus are 1.2-4.7 μM.

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, and viruses, etc. They are widely present in organisms and are an important part of the innate immune system. They are not only not easily induced to produce drug resistance in bacteria, but also exhibit advantages such as broad-spectrum antibacterial, micro-dose high-efficiency, and immunomodulation. However, not any small-molecule polypeptide has antibacterial activity. Even if it has antibacterial activity, there are many limitations in actual production and application. The essence of antimicrobial peptides is a polypeptide, which leads to 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, and there is instability in actual application, as well as unknown hemolytic activity and cytotoxicity, etc., which severely limit the development of antimicrobial peptides as antibacterial drugs. Therefore, it is particularly important to improve the stability and safety of antimicrobial peptides 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, which has 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;

[0006] The polypeptide backbone includes the amino acid sequence shown in SEQ ID NO:1;

[0007] 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.

[0008] 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;

[0009] The amino acid sequence of the linear polypeptide is shown in SEQ ID NO:2;

[0010] The amino acid sequence of the linker is GK.

[0011] 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.

[0012] Preferably, the antibacterial product includes antibacterial infection products.

[0013] Preferably, the bacteria include Gram-negative bacteria and / or Gram-positive bacteria.

[0014] Preferably, the Gram-negative bacteria include Acinetobacter baumannii ( Acinetobacter baumannii ), Pseudomonas aeruginosa ( Pseudomonas aeruginosa ), and Escherichia coli ( Escherichia coli ), one or more of them.

[0015] Preferably, the Gram-positive bacteria include Staphylococcus aureus ( Staphylococcus aureus ).

[0016] Preferably, the product includes reagents or drugs

[0017] 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.

[0018] Preferably, the antibacterial product includes antibacterial reagents or antibacterial drugs.

[0019] Advantageous effects:

[0020] 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 a 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. It presents 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

[0021] 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 in the embodiments.

[0022] Figure 1 It is the transmission electron microscopy observation result and particle size statistical result diagram of self-assembled antimicrobial peptide IL-9-Lau; wherein, A is the transmission electron microscopy diagram and B is the particle size statistical result diagram;

[0023] Figure 2 It is the critical micelle concentration determination result diagram of self-assembled antimicrobial peptide IL-9-Lau; wherein, A is the statistical result diagram of the fluorescence intensity of gradient concentration self-assembled antimicrobial peptide IL-9-Lau at different wavelengths, and B is the Nile red fluorescence curve diagram of gradient concentration self-assembled polypeptide IL-9-Lau;

[0024] Figure 3 It is the detection result diagram of the viability of human embryonic kidney cells HEK293T by different concentrations of self-assembled antimicrobial peptide IL-9-Lau;

[0025] Figure 4 It is the detection result diagram of the viability of human embryonic kidney cells HEK293T by different concentrations of linear polypeptide IL-9;

[0026] Figure 5 It is the evaluation result diagram of the hemolytic effect of different concentrations of self-assembled antimicrobial peptide IL-9-Lau;

[0027] Figure 6 It is the evaluation result diagram of the hemolytic effect of different concentrations of linear polypeptide IL-9. Detailed implementation manners

[0028] 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, which has an appropriate length, can not only increase the activity and promote self-assembly, but also will not significantly enhance the toxicity. Compared with other types of fatty acid chains with strong hydrophobicity, it is safer, and the toxicity of the antimicrobial peptide is smaller after self-assembly.

[0029] As an implementation manner, 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 ID NO: 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, which has a simple structure and no complex side chains, can isolate the main peptide and fatty acid, and will not affect the charge number, helicity, etc. of the linear polypeptide.

[0030] The self-assembling antibacterial peptide IL-9-Lau of 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 hemolysis 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 antibacterial activity. 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.

[0031] 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.

[0032] 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.

[0033] As an embodiment, the Acinetobacter baumannii of the present invention includes one or more of Acinetobacter baumannii ATCC 19606, 10769 and 0357; as another embodiment, the Acinetobacter baumannii of the present invention is Acinetobacter baumannii ATCC 19606. The present invention takes Acinetobacter baumannii ATCC 19606, 10769 and 0357 as examples in the examples, but it should not be understood as the entire protection scope of the present invention only.

[0034] As an embodiment, the Escherichia coli of the present invention includes one or more of Escherichia coli ATCC 8739, 0894 and 5017; as another embodiment, the Escherichia coli of the present invention is Escherichia coli ATCC 8739. The present invention takes Escherichia coli ATCC 8739, 0894 and 5017 as examples in the examples, but it should not be understood as the entire protection scope of the present invention only.

[0035] As an embodiment, the Pseudomonas aeruginosa in the present invention includes one or more of Pseudomonas aeruginosa ATCC 27853, 90068, and 17068; as another embodiment, the Pseudomonas aeruginosa in the present invention is Pseudomonas aeruginosa ATCC 27853. In the examples 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.

[0036] As an embodiment, the Staphylococcus aureus in the present invention includes one or more of Staphylococcus aureus ATCC 6538, 220823, and 15775; as another embodiment, the Staphylococcus aureus in the present invention is Staphylococcus aureus ATCC 6538. In the examples 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.

[0037] 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.

[0038] As an embodiment, the product includes a reagent or a drug.

[0039] The present invention provides an antibacterial product, which 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 embodiment, the minimum inhibitory concentration of the antibacterial peptide in the antibacterial product is ≥1.2 μM; as another embodiment, the minimum inhibitory concentration of the antibacterial peptide in the antibacterial product is 1.2 - 4.7 μM; as another embodiment, the minimum inhibitory concentration of the antibacterial peptide in the antibacterial product is 1.2 - 2.3 μM; as another embodiment, the minimum inhibitory concentration of the antibacterial peptide in the antibacterial product is 1.2 μM.

[0040] To further illustrate the present invention, a self-assembling 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.

[0041] Example 1

[0042] Entrust GIL Biochemicals (Shanghai) Co., Ltd. to synthesize a linear polypeptide IL-9 consisting of only 9 amino acids through solid-phase peptide synthesis. Its amino acid sequence is IKKGIKKLL (SEQ ID NO:2), all of which are L-amino acids. To form nanoparticles by self-assembly of IL-9, a glycine-lysine (GK) is 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 carboxyl group of a lauric acid is connected to the side-chain amino group of lysine in the linker by forming a peptide bond to obtain the self-assembling antimicrobial peptide IL-9-Lau; finally, desalting and purification are carried out by HPLC reversed-phase column chromatography to obtain the self-assembling antimicrobial peptide IL-9-Lau. The molecular weight of the IL-9-Lau is 1407.91 Daltons, and all amino acids are L-type.

[0043] Comparative Example 1

[0044] Entrust GIL Biochemicals (Shanghai) Co., Ltd. to synthesize a linear polypeptide IL-9 consisting of only 9 amino acids through solid-phase peptide synthesis. Its amino acid sequence is IKKGIKKLL (SEQ ID NO:2), all of which are L-amino acids.

[0045] Test Example 1

[0046] Observation by transmission electron microscope

[0047] (1) Drop the solution containing the self-assembling antimicrobial peptide IL-9-Lau obtained in Example 1 on 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 uranyl 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-assembling 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).

[0048] (2) Data processing: Use Image J software to count the nanoparticle particle size, and GraphPad Prism to make a particle size distribution map. The results show that the average particle size of the self-assembling antimicrobial peptide IL-9-Lau is 14.81 nm (Figure 1 in B).

[0049] Test Example 2

[0050] Determination of Critical Micelle Concentration (CMC)

[0051] (1) Add 100 μL of the self-assembled antibacterial peptide IL-9-Lau solution with gradient concentrations from 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 multifunctional microplate reader ( Figure 2 in A).

[0052] 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.

[0053] (2) Data processing: Use 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 starts to form micelles in aqueous solution, that is, the CMC value ( Figure 2 in B).

[0054] 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.

[0055] Test Example 3

[0056] Antibacterial Activity Analysis

[0057] 1. Test Strains

[0058] (1) Acinetobacter baumannii: ATCC 19606, 10769, and 0357;

[0059] (2) Escherichia coli: ATCC 8739, 0894, and 5017;

[0060] (3)Pseudomonas aeruginosa: ATCC 27853, 90068, and 17068;

[0061] (4)Staphylococcus aureus: ATCC 6538, 220823, and 15775.

[0062] 2. Minimum Inhibitory Concentration (MIC) Detection

[0063] First, inoculate the test strains onto LB solid plates. After colonies grow, pick single colonies and transfer them to LB liquid medium. Incubate with shaking at 37 °C and 180 rpm for 5 h. Measure the OD of the bacterial solution using an ultraviolet spectrophotometer. 600 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; in a sterile 96-well plate, add 100 μL of the diluted bacterial solution to each well. Then, add 100 μL of the test samples diluted in physiological saline in gradients to each well. Use a pipette to blow and mix evenly. After mixing, place it in a 37 °C constant temperature incubator and incubate with slow shaking overnight; the test samples are 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 samples is 0 - 200 μg / mL; after incubation, use a microplate reader to measure the absorbance of the bacterial solution at OD 600 nm. Take the average value of the sample concentrations in the wells where no bacterial growth is detected and the adjacent wells as the MIC value. The results are shown in Table 1.

[0064] Table 1 Minimum Inhibitory Concentration Values of Test Samples Against Test Strains

[0065]

[0066] As can be seen from Table 1, 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 having antibacterial activity.

[0067] Test Example 4

[0068] Cytotoxicity Analysis

[0069] Cultivate human embryonic kidney cells (HEK293T) routinely 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 them into a cell suspension of 5×10 5Cell suspension at a concentration of cells / mL, add 200 μL of cell suspension to each well in a sterile 96-well plate, and continue to culture overnight; the next day, add the test samples at different concentration gradients (final concentration 0 - 100 μM) or the same volume of DMEM medium respectively. Set 3 replicates for each sample concentration, continue to culture for 24 h, then add 15 μL of MTT solution at a concentration of 5 mg / mL to each well, and continue to culture for 4 h in the dark. Subsequently, aspirate the culture medium 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, and then measure the absorbance value of each well at 450 nm with an enzyme-linked immunosorbent assay (ELISA) reader. The results are as Figure 3 and Figure 4 shown; among them, 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.

[0070] 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 keratinocyte HaCaT within the test concentration range; the self-assembled antimicrobial peptide IL-9-Lau obtained in Example 1 has no toxicity to human keratinocyte HaCaT within a concentration range of 50 μM, and only shows weak cytotoxicity at a concentration of 100 μM ( P < 0.05). By means of self-assembly, the present invention enables the antibacterial activity of the linear polypeptide IL-9 to change from none (MIC > 50 μM) to having, while not having cytotoxicity and having good safety.

[0071] Test Example 6

[0072] Hemolysis analysis

[0073] 1. Mix fresh human whole blood and Alsever's solution according to a volume ratio of 1:1, centrifuge at 1000 rpm for 5 min, discard the supernatant, wash the obtained red blood cells with physiological saline, and repeat 3 times until the supernatant no longer shows red, to obtain well-washed red blood cells.

[0074] 2. Dilute the well-washed red blood cells with physiological saline to a density of 1×10 7 cells / mL. Incubate the red blood cell suspension with the test samples at different concentrations (0 - 100 μM) dissolved in physiological saline at 37 °C for 30 min, then centrifuge at 1000 rpm for 5 min, and detect the absorbance value of the supernatant at 540 nm. The positive control uses the same volume of Triton X-100 solution (PC), and the volume concentration of the Triton X-100 solution is 10%; the negative control uses physiological saline; among them, 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.

[0075] 3. Data processing: Detect the absorbance value at 540 nm, 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 Figure 5 and Figure 6 shown.

[0076] Hemolysis rate (%) = (OD value of positive control - OD value of negative control) / (OD value of sample group to be tested - OD value of negative control) × 100%. 540 value - OD value of negative control 540 value) / (OD value of sample group to be tested 540 value - OD value of negative control 540 value) × 100%.

[0077] It can be seen from Figure 5 and Figure 6 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.

[0078] It can be seen from the above content 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 any cytotoxicity or hemolytic effect.

[0079] Although the above embodiments have described the present invention in detail, they are only a part of the embodiments of the present invention, not all of them. 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 consists of a polypeptide main chain and lauric acid; The amino acid sequence of the polypeptide backbone is 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. Use of the self-assembling antimicrobial peptide IL-9-Lau according to claim 1 in the preparation of antibacterial products; The bacteria are Gram-negative bacteria and / or Gram-positive bacteria; The Gram-negative bacteria are Acinetobacter baumannii ( Acinetobacter baumannii )、Pseudomonas aeruginosa( Pseudomonas aeruginosa ) and Escherichia coli ( Escherichia coli ) one or more; The Gram-positive bacteria is Staphylococcus aureus ( Staphylococcus aureus ).

3. The use according to claim 2, characterized in that: The anti-bacterial products include anti-bacterial infection products.

4. The use according to claim 2 or 3, characterized in that: The product includes reagents.

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

6. The product according to claim 5, characterized in that The antibacterial product includes an antibacterial agent.

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