Separated polypeptide and application thereof

Abstract

The invention relates to the technical field of peptide preparations, and provides a separated polypeptide and application thereof. The polypeptide has an amino acid sequence as shown in SEQ ID NO: 1. The polypeptide can effectively inhibit common pathogenic bacteria such as acinetobacter baumannii and multi-drug-resistant acinetobacter baumannii, is low in cytotoxicity and high in safety, and is suitable for preparing products with bacteriostatic and / or bactericidal performance, such as food or pharmaceutical preparations.

Description

Technical Field

[0001] The present invention relates to the technical field of peptide preparations, in particular to an isolated polypeptide and applications thereof. Background Art

[0002] Acinetobacter baumannii ( Acinetobacter baumannii , A. baumannii Acinetobacter baumannii is a Gram-negative bacterium and a common cause of hospital-acquired infections, particularly pneumonia and bloodstream infections in critically ill patients. It is naturally resistant to many antimicrobial agents. Research reports indicate that resistance to carbapenem antibiotics is increasing in Acinetobacter baumannii, making it a clinically important multidrug-resistant pathogen and a challenge to clinical treatment. The World Health Organization has designated it as a multidrug-resistant bacteria of priority concern.

[0003] Antimicrobial peptides are a class of small-molecule peptides composed of short chains of amino acids that exhibit antimicrobial activity against pathogens such as bacteria, fungi, viruses, and parasites. These peptides primarily destroy microbial cell membranes or cell walls, causing leakage of intracellular substances, thereby achieving bactericidal or antibacterial effects. Compared to traditional antibiotics, bacteria are less likely to resist antimicrobial peptides by mutating their membranes. Therefore, antimicrobial peptides have a lower risk of developing resistance and offer potential as an alternative to traditional antibiotics.

[0004] Archaea are prokaryotic, single-celled microorganisms that live in extreme environments. While they share many similarities with bacteria—namely, they lack a nucleus or other membrane-bound organelles—they possess certain eukaryotic features in terms of genome structure and cellular physiology, such as the presence of repetitive sequences and nucleosomes. Archaea are widely distributed in a variety of extreme natural environments, such as high-pressure thermal vents, hot springs, and saline-alkali lakes at the bottom of the ocean. Their unique survival mechanisms make them a potential resource for functional molecules.

[0005] Currently, most microbial antimicrobial peptides are discovered from bacteria, but archaeal antimicrobial peptide resources have not been fully developed. Therefore, it is urgent to strengthen the exploration and mining of archaeal antimicrobial peptides to expand the diversity and application potential of antimicrobial peptides. Summary of the Invention

[0006] The present invention is intended to solve one of the technical problems existing in the prior art at least to a certain extent, especially for the antibacterial demand of Acinetobacter baumannii and multidrug-resistant strains thereof.For this reason, an object of the present invention is to provide a kind of isolated polypeptide with significant antibacterial and bactericidal properties and its related application.Described polypeptide has antibacterial and bactericidal effect to various bacteria, for example Acinetobacter baumannii, multidrug-resistant Acinetobacter baumannii etc., this polypeptide is not easy to produce drug resistance, and has lower mammalian cell toxicity and hemolytic toxicity, possesses good application safety, can be used for preparing the antibacterial composition for the treatment of Acinetobacter baumannii, multidrug-resistant Acinetobacter baumannii, also can be used as peptide inhibitor and be applied to the antibacterial composition or the antibacterial product of food, pharmaceutical product or daily care field simultaneously.

[0007] Specifically, the technical solution of the present invention is as follows: In a first aspect of the present invention, the present invention provides an isolated polypeptide. According to an embodiment of the present invention, the isolated polypeptide has an amino acid sequence as shown in SEQ ID NO: 1.

[0008] According to an embodiment of the present invention, the isolated polypeptide is derived from PL-Br10-E2g29 Genus.

[0009] According to an embodiment of the present invention, the isolated polypeptide is derived from PL-Br10-E2g29 sp001563965 Archaeal strains.

[0010] In a second aspect, the present invention provides a nucleic acid molecule. According to an embodiment of the present invention, the nucleic acid encodes the isolated polypeptide described in the first aspect. The nucleic acid molecule according to the embodiment of the present invention can be expressed under appropriate conditions to obtain the isolated polypeptide.

[0011] It should be noted that the "suitable conditions" described in this specification refer to conditions suitable for the expression of the isolated polypeptide of the present invention. Those skilled in the art will readily appreciate that conditions suitable for the expression of the isolated polypeptide include, but are not limited to, a suitable transformation or transfection method, healthy host cells, a suitable host cell density, and an appropriate cell culture environment and time. "Suitable conditions" are not particularly limited, and those skilled in the art can optimize the optimal conditions for the expression of the isolated polypeptide as needed.

[0012] In a third aspect, the present invention provides a composition. According to an embodiment of the present invention, the composition comprises: the isolated polypeptide described in the first aspect.

[0013] According to an embodiment of the present invention, the composition is a drug, and the composition further includes a pharmaceutically acceptable carrier. "Pharmaceutically acceptable carrier" can include any and all solvents, dispersion media, coatings, antibacterial and antifungal agents, isotonic agents and absorption delay agents that are physiologically compatible. Specific examples can be one or more of water, saline, phosphate-buffered saline, glucose, glycerol, ethanol, and combinations thereof. In many cases, the composition includes an isotonic agent, such as a sugar, a polyol (such as mannitol, sorbitol), or sodium chloride. Of course, a pharmaceutically acceptable carrier may also include trace amounts of auxiliary substances, such as wetting agents or emulsifiers, preservatives, or buffers, to extend the shelf life or effectiveness of the antibody.

[0014] In a fourth aspect, the present invention provides use of the isolated polypeptide described in the first aspect, the nucleic acid molecule described in the second aspect, or the composition described in the third aspect in the preparation of a product and / or medicament. According to an embodiment of the present invention, the product and / or medicament is used to inhibit the growth of and / or kill pathogens.

[0015] According to an embodiment of the present invention, the pathogenic bacteria include Acinetobacter baumannii and / or multidrug-resistant Acinetobacter baumannii.

[0016] According to an embodiment of the present invention, the minimum inhibitory concentration of the polypeptide against Acinetobacter baumannii is 64 μM.

[0017] According to an embodiment of the present invention, the minimum inhibitory concentration of the polypeptide against multidrug-resistant Acinetobacter baumannii is 128 μM.

[0018] Those skilled in the art will understand that the minimum inhibitory concentration of the polypeptide against pathogens can be used to infer and calculate the dosage and frequency of use of the above-mentioned products and / or drugs, and guide the content of the polypeptide contained in the above-mentioned products and / or drugs.

[0019] In a fifth aspect, the present invention provides a method for inhibiting the growth of and / or killing pathogenic bacteria. According to an embodiment of the present invention, the method comprises contacting the isolated polypeptide described in the first aspect of the present invention or the composition described in the third aspect with a sample to be treated, wherein the sample to be treated contains the pathogenic bacteria.

[0020] According to an embodiment of the present invention, the pathogenic bacteria include Acinetobacter baumannii and / or multidrug-resistant Acinetobacter baumannii.

[0021] According to an embodiment of the present invention, the minimum inhibitory concentration of the polypeptide against Acinetobacter baumannii is 64 μM.

[0022] According to an embodiment of the present invention, the minimum inhibitory concentration of the polypeptide against multidrug-resistant Acinetobacter baumannii is 128 μM.

[0023] Those skilled in the art will appreciate that the dosage and frequency of use of the polypeptide or composition can be inferred and calculated based on the minimum inhibitory concentration of the polypeptide against pathogens.

[0024] In a sixth aspect of the present invention, the present invention provides a daily necessity and / or a care product. According to an embodiment of the present invention, the daily necessity and / or fabric comprises the isolated polypeptide according to the first aspect of the present invention as an active ingredient.

[0025] According to an embodiment of the present invention, the daily necessities are selected from at least one of hand soap, shower gel, shampoo, mouthwash, toothpaste, soap, cosmetics, feminine care wash, laundry soap, laundry liquid, laundry powder, detergent, spray, ointment, gel base, disinfectant and toilet cleaning liquid; and / or the care products include at least one of sanitary napkins, diapers and urine pads.

[0026] As mentioned above, those skilled in the art will understand that the content of the polypeptide contained in the above-mentioned daily necessities and / or care products can be inferred and calculated based on the minimum inhibitory concentration of the polypeptide against pathogens.

[0027] In a seventh aspect, the present invention provides an antibacterial additive. According to an embodiment of the present invention, the antibacterial additive comprises the polypeptide described in the first aspect of the present invention.

[0028] The polypeptide of the present invention has the following beneficial technical effects: 1) The isolated polypeptide provided by the present invention is derived from deep-sea archaea and has antibacterial activity against Acinetobacter baumannii and multidrug-resistant Acinetobacter baumannii; 2) It has been verified that the polypeptide of the present invention is not prone to drug resistance, has low mammalian cytotoxicity and low hemolytic toxicity, and can be used to prepare antibacterial compositions for infections caused by Acinetobacter baumannii and multidrug-resistant Acinetobacter baumannii. In addition, the polypeptide can be used as a peptide inhibitor in daily necessities, food or medicine.

[0029] Additional aspects and advantages of the present invention will be set forth in part in the description which follows and, in part, will be obvious from the description which follows, or may be learned by practice of the present invention. BRIEF DESCRIPTION OF THE DRAWINGS

[0030] The above and / or additional aspects and advantages of the present invention will become apparent and readily understood from the following description of the embodiments with reference to the accompanying drawings, in which: Figure 1 Schematic diagram of HPLC detection results of the antimicrobial peptide cAMP102 in an embodiment of the present invention; Figure 2 Schematic diagram of LC-MS detection results of the antimicrobial peptide cAMP102 in an embodiment of the present invention; Figure 3 Schematic diagram of the minimum inhibitory concentration determination results of the antimicrobial peptide cAMP102 in the embodiment of the present invention; wherein, (a) Acinetobacter baumannii A. baumannii ATCC 19606; (b) Multi-drug resistant (MDR) Acinetobacter baumannii A. baumannii BAA-1605; Figure 4 Schematic diagram of the mammalian cell cytotoxicity assay results of the antimicrobial peptide cAMP102 in an embodiment of the present invention; Figure 5 Schematic diagram of the hemolytic toxicity assay results of the antimicrobial peptide cAMP102 in an example of the present invention. DETAILED DESCRIPTION

[0031] The following will clearly and completely describe the technical solutions in the embodiments of the present invention in conjunction with the accompanying drawings. Obviously, the described embodiments are only part of the embodiments of the present invention, not all of the embodiments. Based on the embodiments of the present invention, all other embodiments obtained by ordinary technicians in this field without making any creative efforts shall fall within the scope of protection of the present invention.

[0032] It should be noted that the terms "first", "second", etc. in the description and claims of the present invention and the above-mentioned drawings are used to distinguish similar objects and are not necessarily used to describe a specific order or sequence. It should be understood that the numbers used in this way are interchangeable where appropriate so that the embodiments of the present invention described herein can be implemented in an order other than those illustrated or described herein. In addition, the terms "including" and "having" and any variations thereof are intended to cover non-exclusive inclusions. For example, a process, method, system, product or server that includes a series of steps or units is not necessarily limited to those steps or units clearly listed, but may include other steps or units that are not clearly listed or inherent to these processes, methods, products or devices.

[0033] As used herein, the term "composition" generally refers to a unit dosage form and can be prepared by any of the methods well known in the pharmaceutical art. All methods include the step of bringing the active ingredient into association with a carrier which constitutes one or more accessory ingredients. Generally, the composition is prepared by uniformly and thoroughly combining the active antibody or antigen-binding fragment with a liquid carrier, a finely divided solid carrier, or both.

[0034] This study used the Extreme Environment Microbiome Catalogue (EEMC) database, a global database developed by the Sanya BGI Life Sciences Institute, to identify novel antimicrobial peptides. They first used antiSMASH (v7.0) (Kai Blin, Simon Shaw, Hannah E Augustijn, et al., antiSMASH 7.0: new and improved predictions for detection, regulation, chemical structures and visualization, Nucleic Acids Research, Volume 51, Issue W1, 5 July 2023, Pages W46–W50) software with a --minlength 5000 parameter to identify biosynthesis gene clusters (BGCs) in extreme environment archaeal genomes. Deep learning models (RNN, LSTM) were then used to predict the core peptide sequences within these RiPP-like BGCs. Furthermore, the obtained core peptide sequences were used to predict low-toxicity antimicrobial peptides using three pre-trained protein language models (ESM2-3B, ESM3, and PTRANS), and the peptide sequences ranked in the top 50% by each model prediction score were screened as candidate low-toxicity antimicrobial peptides. The candidate antimicrobial peptides were compared with the known antimicrobial peptide database, and the peptide sequences consistent with the known database were removed to obtain new candidate low-toxicity antimicrobial peptide sequences, and the next step of experimental verification was carried out. The species annotation of extreme environment archaea was obtained using GTDB-Tk (The GenomeTaxanomy Database Toolkit) and the R220 database annotation that comes with the tool. Finally, the present invention obtained an archaea from extreme environments such as the deep sea through the above steps. PL-Br10-E2g29 sp001563965 The following is the experimental verification process of the antimicrobial peptide's antibacterial function and toxicity.

[0035] The A. baumannii in the present invention is Acinetobacter baumannii (ATCC 19606), and MDR A. baumannii is multidrug-resistant Acinetobacter baumannii (BAA-1605, Shanghai Beinuo Biotechnology Co., Ltd.).

[0036] The sequences involved in the present invention are shown in Table 1.

[0037] Table 1

[0038] The technology of the present invention is described below through specific examples. If specific techniques or conditions are not specified in the examples, the techniques or conditions described in the literature in the field or the product instructions are used. If the manufacturer of the reagents or instruments is not specified, they are all conventional products that can be obtained commercially.

[0039] Example 1: Synthesis and purification of antimicrobial peptide cAMP102 The antimicrobial peptide cAMP102 in Table 1 was chemically synthesized by Shanghai Sangon Biotechnology Co., Ltd. using solid-phase peptide synthesis based on its amino acid sequence (SEQ ID NO: 1). The purity of the antimicrobial peptide obtained by solid-phase synthesis was then determined by high-performance liquid chromatography (HPLC), and the exact molecular weight of the antimicrobial peptide cAMP102 was determined by liquid chromatography-mass spectrometry (LC-MS). The specific experimental procedures are as follows: 1.1 Purity determination of antimicrobial peptide cAMP102 by high-performance liquid chromatography (HPLC) HPLC analytical column model: SHIMADZU shim-pack GIST (4.6*250mm*5UM); Mobile phase A: deionized water containing 0.1% trifluoroacetic acid (TFA); Mobile phase B: acetonitrile containing 0.1% trifluoroacetic acid (TFA); Sample: Dissolve 0.5 mg of the antimicrobial peptide cAMP102 in 0.5 mL using 10% acetonitrile and 90% water.

[0040] Determination method: Set the total flow rate of the mobile phase to 1 mL / min, the detection wavelength to 214 nm, and linearly increase the gradient of mobile phase B from 0 to 20 minutes (20% to 80%), and linearly decrease the gradient of mobile phase A (80% to 20%). Inject 30 μL of the sample to be tested and record the detection signal. The results are as follows Figure 1 shown.

[0041] from Figure 1 The results show that the purity of the synthesized antimicrobial peptide cAMP102 is greater than 95%.

[0042] 1.2 Liquid chromatography-mass spectrometry (LC-MS) determination of the molecular weight of the antimicrobial peptide cAMP102 Mass spectrometer: Shimadzu LC-MS-2020; Mobile phase: 50% water / 50% methanol; Sample: Dissolve 0.1 mg of the antimicrobial peptide cAMP102 in 50% acetonitrile and 50% water to 0.5 mL.

[0043] Detection method: Set the atomizing gas flow rate to 1.50 L / min, CDL temperature to 250℃, CDL voltage to 0 V, module temperature to 200℃, rod front deviation to +4.5 kV, detector to -0.2 kV, T.Flow to 0.2 mL / min, inject 1 μL of the sample to be tested, and record the detection signal. The results are as follows Figure 2 shown.

[0044] The amino acid sequence of the antimicrobial peptide cAMP102 is STATICIGRVSRSSTSERSARLRTVS (SEQ ID No. 1). Its theoretical molecular weight is 2782.123. Figure 2 The mass spectrometry results shown indicate that the molecular weight of the antimicrobial peptide cAMP102 synthesized in this example is consistent with the theoretical molecular weight.

[0045] Example 2: Activity analysis of antimicrobial peptides 2.1 Minimum inhibitory concentration (MIC) determination Acinetobacter baumannii A. baumannii and multidrug-resistant Acinetobacter baumannii MDR A. baumannii Both bacterial strains were streaked onto Luriae–Bertani (LB) agar medium and incubated overnight at 37°C.

[0046] Single colonies of the two bacterial strains were inoculated into Mueller-Hinton Broth (MHB) liquid medium (Thermo Fisher Scientific Inc.) and cultured overnight at 37°C and 120 rpm. The next day, the overnight culture was diluted 1:100 with fresh MHB and cultured until the exponential growth phase (OD 600 The bacterial solution was then diluted to a final concentration of 1×10 6 cfu / mL for future use.

[0047] In the antimicrobial activity assay, the antimicrobial peptide cAMP102 was first diluted in a two-fold gradient using MHB medium to prepare working solutions with concentrations ranging from 0.5, 1, 2, 4, 8, 16, 32, 64, 128, and 256 μM. The dilution steps were as follows: first prepare the highest concentration working solution (128 μM), then dilute it 1:1 with an equal volume of MHB to form a continuous two-fold concentration series. Each concentration gradient of cAMP102 solution (100 μL) was mixed with an equal volume of the diluted bacterial solution (100 μL) and added to a 96-well microplate to ensure that the antimicrobial peptide concentration in the final reaction system covered a series of gradients from 0.5–256 μM. The experimental group settings included: Negative control group: 100 μL MHB and 100 μL bacterial solution were added without adding antimicrobial peptides; Blank control group: 200 μL MHB was added without bacterial solution and antimicrobial peptide; Antimicrobial peptide group: The diluted antimicrobial peptide solution and bacterial solution were mixed, and the final antimicrobial peptide concentration range was 0.5, 1, 2, 4, 8, 16, 32, 64, 128, and 256 μM.

[0048] After incubation at 37°C for 16-18 hours, the MIC value was determined. The MIC value was the lowest concentration of the antimicrobial peptide at which no bacterial growth was observed visually. All experiments were repeated three times. This method is a routine method in the art and will not be described in detail here.

[0049] Figure 3 The experimental results showed that the antimicrobial peptide cAMP102 A. baumannii The MIC of (a) is 64 μM, and the MDR A. baumannii The MIC of (b) is 128 μM.

[0050] 2.2 Mammalian cell cytotoxicity assay To evaluate the potential toxicity of the candidate antimicrobial peptide cAMP102 to mammalian cells, four experimental treatment groups were set up: a blank control group (Blank), a negative control group (PBS group), a positive control group (cisplatin-treated group), and an experimental group (cAMP102-treated group). The antimicrobial peptide solution was prepared in sterile PBS buffer at a concentration of 60 μM.

[0051] The cells used in the experiment included L-02 normal human hepatocytes (Beina Biotech) and HEK-293T human embryonic kidney cells (Pnosai Biotech). After trypsinization, the cells were resuspended in DMEM (Gibco, USA) supplemented with 10% fetal bovine serum (FBS, Cat. No. 04-001-1ACS, Biological Industries, Israel) to prepare a single-cell suspension. The cell density was adjusted to 5 × 10 4 Cells from each treatment group were seeded into a 96-well culture plate, with 90 μL of cell suspension added to each well. A blank control group was left untreated, with only 100 μL of FBS-DMEM culture medium added. After seeding, cells were incubated in a 5% CO2, 37°C incubator for 24 hours to promote adherence. After 24 hours, each group was treated as follows: Negative control group (Control): 10 μL PBS was added to each well; Positive control group (cisplatin): 10 μL of pre-prepared cisplatin solution (Cat. No. D8810, Solarbio) was added to each well to a final concentration of 60 μM; Experimental group (cAMP102): 10 μL of antimicrobial peptide cAMP102 solution was added to each well to a final concentration of 60 μM; The blank group (Blank) maintained its original state without adding any treatment solution.

[0052] After the treatment is completed, continue incubation for 48 hours. Then discard the culture medium and treatment solution in the wells, add 100 μL of CCK-8 detection reagent diluted 10 times with DMEM to each well (final concentration is 10% (v / v), product number BS350A, White Shark Bio), and continue incubation for 1 hour in a dark environment with 5% CO2 and 37°C. After the incubation is completed, use a microplate reader to measure the absorbance (OD value) at a wavelength of 450nm and record the raw data results. The formula for calculating the inhibition rate of mammalian cells is (OD Control -OD cAMP102 / 顺铂 ) / (OD Control -OD Blank ) × 100%, and all experiments were repeated 3 times.

[0053] Figure 4 The results show that compared with the positive control group (cisplatin group), the antimicrobial peptide cAMP102 group has a lower inhibition rate and significantly lower mammalian cell toxicity. The inhibition rate of the antimicrobial peptide cAMP102 on L-02 human hepatocytes was 0%, and the inhibition rate on 293T human embryonic kidney cells was 7.38%.

[0054] 2.3 Hemolytic toxicity assay To evaluate the hemolytic activity of the candidate antimicrobial peptide cAMP102, three treatment groups were set up in this experiment: a blank group, a positive control group (Triton X-100 group), and an experimental group (cAMP102 group). The red blood cells used in the experiment were obtained from fresh defibrinated sheep blood (Beekman Biotechnology, China). Plasma and red blood cells were separated by centrifugation at 1500 rpm for 10 minutes, and the plasma fraction was discarded. The obtained red blood cells were repeatedly washed 3-4 times with sterile PBS buffer until the supernatant was clear and transparent to remove residual plasma and other components. The washed red blood cells were resuspended in PBS to prepare a 4% (v / v) red blood cell suspension. 100 μL of the red blood cell suspension was added to each well of a 96-well plate, and then the following treatments were performed: Blank group: 100 μL PBS buffer without any hemolytic agent was added to each well; Positive control group (Triton X-100, Control): Triton X-100 (final concentration 1%) was added to each well to induce complete hemolysis; Experimental group (cAMP102): The candidate antimicrobial peptide cAMP102 solution was added to each well to a final concentration of 60 μM.

[0055] After the treatment is completed, the 96-well plate is placed in a 37°C constant temperature incubator and incubated for 1 hour. After the incubation is completed, centrifuge at 4°C and 1500 rpm for 10 minutes, collect the supernatant from each well and transfer it to a new 96-well plate. Then, use a microplate reader to measure the absorbance value (OD) at a wavelength of 570 nm and record the raw data. The formula for calculating the hemolysis rate is (OD cAMP102 -OD Blank ) / (OD Control -OD Blank ) × 100%, and all experiments were repeated 4 times.

[0056] Figure 5 The results show that compared with the positive control group, the antimicrobial peptide cAMP102 group has a lower OD value and significantly lower hemolytic toxicity. The hemolytic rate of the antimicrobial peptide cAMP102 was calculated to be 2.32%.

[0057] In the description of this specification, the reference terms "one embodiment," "some embodiments," "example," "specific example," or "some examples" mean that the specific features, structures, materials, or characteristics described in conjunction with the embodiment or example are included in at least one embodiment or example of the present invention. In this specification, the schematic representations of the above terms do not necessarily refer to the same embodiment or example. Moreover, the specific features, structures, materials, or characteristics described can be combined in any one or more embodiments or examples in a suitable manner. In addition, those skilled in the art can combine and combine different embodiments or examples described in this specification and features of different embodiments or examples without contradiction.

[0058] Although the embodiments of the present invention have been shown and described above, it will be understood that the above embodiments are illustrative and are not to be construed as limitations on the present invention. A person skilled in the art may change, modify, replace and modify the above embodiments within the scope of the present invention.

Claims

1. An isolated polypeptide, characterized in that It has the amino acid sequence shown in SEQ ID NO:

1.

2. The isolated polypeptide according to claim 1, characterized in that The isolated polypeptide is derived from PL-Br10- E2g29 sp001563965 Archaeal strains.

3. A nucleic acid molecule, characterized in that The nucleic acid molecule encodes the isolated polypeptide according to any one of claims 1 to 2, and the nucleic acid molecule has a nucleotide sequence as shown in SEQ ID NO:

2.

4. A composition, characterized in that The composition comprises the isolated polypeptide according to any one of claims 1 to 2.

5. Use of the isolated polypeptide according to any one of claims 1 to 2, the nucleic acid molecule according to claim 3, or the composition according to claim 4 in the preparation of a product and / or a medicine, characterized in that: The product and / or medicine is used to inhibit the growth of pathogens and / or kill pathogens, and the pathogens include Acinetobacter baumannii and / or multidrug-resistant Acinetobacter baumannii.

6. A method for inhibiting the growth of pathogens and / or killing pathogens in vitro, characterized in that: include: The isolated polypeptide according to any one of claims 1 to 2 or the composition according to claim 4 is contacted with a sample to be treated, wherein the sample to be treated contains the pathogenic bacteria, and the pathogenic bacteria include Acinetobacter baumannii and / or multidrug-resistant Acinetobacter baumannii.

7. The method according to claim 6, wherein The minimum inhibitory concentration of the polypeptide against Acinetobacter baumannii is 64 μM, and / or The minimum inhibitory concentration of the polypeptide against multidrug-resistant Acinetobacter baumannii is 128 μM.

8. A daily necessity and / or care product, characterized in that: The daily necessities and / or care products comprise the isolated polypeptide according to any one of claims 1 to 2 as an active ingredient.

9. The daily necessities and / or care products according to claim 8, characterized in that: The daily necessities include at least one selected from hand soap, shower gel, shampoo, mouthwash, toothpaste, soap, cosmetics, feminine care wash, laundry soap, laundry liquid, laundry powder, detergent, spray, ointment, gel matrix, disinfectant and toilet cleaning liquid; and / or the care products include at least one selected from sanitary napkins, diapers and urine pads.

10. An antibacterial additive, characterized in that The antibacterial additive comprises the isolated polypeptide according to any one of claims 1 to 2.

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