Antibacterial peptide MZQ-28, coding gene and application thereof

Abstract

The present application relates to the technical field of biotechnology, in particular to an antibacterial peptide MZQ-28, a coding gene and application thereof.The present application provides a novel antibacterial peptide MZQ-28 which is screened and designed based on artificial intelligence, can maintain antibacterial activity in high-temperature and extreme pH environment, has significant inhibitory effect on gram-negative bacteria (Escherichia coli, Salmonella choleraesuis) and gram-positive bacteria (Staphylococcus aureus), enriches the types of antibacterial peptides, and is expected to be applied to prepare products with antibacterial activity and replace antibiotics for the treatment of fungal or bacterial infection in clinic, has potential application value in the fields of food preservation, cosmetics, biological pesticides and feed additives, and provides a new solution for solving the increasingly serious problem of antibiotic resistance.

Description

Technical Field

[0001] This invention relates to the field of biotechnology, specifically to the antimicrobial peptide MZQ-28, its encoding gene, and its applications. Background Technology

[0002] Pathogenic microorganisms can cause a variety of infectious diseases, such as influenza, tuberculosis, and pneumonia, seriously damaging human health. Infection with Streptococcus pneumoniae can produce clinical symptoms such as cough, high fever, purulent sputum, and chest pain, affecting the lungs' gas exchange function. Infection with Helicobacter pylori can cause chronic gastritis, peptic ulcers, and even increase the risk of stomach cancer. Infection with Staphylococcus aureus can cause purulent lesions on the skin and soft tissues, leading to folliculitis, boils, and cellulitis. Currently, the main treatment for pathogenic microorganism infections is antibiotic therapy; however, with the widespread use of antibiotics, drug-resistant bacteria have been identified and are proliferating.

[0003] Antimicrobial peptides (AMPs) possess unique mechanisms of action and biological characteristics, and are considered one of the alternatives to antibiotics. AMPs are a class of endogenous polypeptides produced by organisms, typically composed of 10-60 amino acids, and are widely distributed in bacteria, fungi, plants, invertebrates, and mammals. Traditional antibiotics often exert their effects by targeting specific metabolic pathways in bacteria, easily inducing drug-resistant mutations. In contrast, AMPs primarily rely on physical disruption of the cell membrane or synergistic effects across multiple targets to achieve bactericidal effects, making it difficult for bacteria to develop resistance through a single mutation. Furthermore, antimicrobial peptides offer advantages such as broad-spectrum antibacterial activity, immunomodulation, anti-inflammation, and rapid bactericidal action, while exhibiting low toxicity to normal human cells and good biocompatibility.

[0004] Traditional antimicrobial peptide design primarily relies on chemical modification and site-directed mutagenesis. These methods are not only cumbersome and time-consuming, but also inefficient and costly, and limited by known templates, hindering the development and application of antimicrobial peptides. However, by leveraging artificial intelligence to capture complex patterns in the relationship between antimicrobial peptide sequences and activity that are difficult for the human eye to discern, novel antimicrobial peptide sequences can be generated. This significantly improves the efficiency of initial antimicrobial peptide screening, reduces screening costs, shortens the screening cycle, and breaks through the template limitations of traditional antimicrobial peptide design. Summary of the Invention

[0005] To address the shortcomings of existing technologies, this invention provides the antimicrobial peptide MZQ-28, its encoding gene, and its applications. It has been demonstrated that MZQ-28 has significant inhibitory effects on common Gram-positive bacteria, such as Staphylococcus aureus and Streptococcus pneumoniae, as well as Gram-negative bacteria such as Escherichia coli and Salmonella choleraesuis. Furthermore, MZQ-28 exhibits multidimensional stability and maintains good antibacterial activity even under high temperature and extreme pH conditions.

[0006] To achieve the above objectives, the present invention provides an antimicrobial peptide MZQ-28, with an amino acid sequence of (a) or (b); (a) A protein composed of the amino acids shown in SEQ ID NO. 1; (b) A functionally equivalent derivative protein consisting of the amino acid sequence shown in SEQ ID NO. 1, with one or more amino acid residues substituted and / or deleted and / or added; The aforementioned antimicrobial peptide MZQ-28 can withstand pH values ​​of 3-11 and high-temperature environments of 90°C. It can specifically inhibit the growth of at least one of the following bacteria: Staphylococcus, Escherichia, Salmonella, Vibrio, Acinetobacter, and Propionibacterium. It can be applied in the fields of food, hygiene products, cosmetics, biopesticides, biofeed additives, or natural food preservatives.

[0007] In some specific embodiments, the present invention provides an antimicrobial protein having an amino acid sequence that has 80% identity with the sequence shown in SEQ ID NO. 1; preferably, it has 85% identity, more preferably... The first type has 90% similarity, the second type has 95% similarity, and the third type has 99% similarity.

[0008] In some specific embodiments, the antimicrobial peptide MZQ-28 was prepared using the following method, with the specific steps as follows: 1) Collect antimicrobial peptide and non-antimicrobial peptide sequences, calculate their physicochemical properties, and predict the three-dimensional structure of the sequences; 2) After the antimicrobial peptide data is preprocessed, it is input into a pre-trained masked language model to extract multimodal representations of the sequence with fused structural features. Novel candidate sequences are generated based on the feature representations using a conditional diffusion model. After initial screening for authenticity by a pre-trained GAN discriminator, the structural stability of the sequence under physiological conditions is verified by molecular dynamics simulation to obtain the amino acid sequence of antimicrobial peptide MZQ-28 (as shown in SEQ ID NO. 1). 3) Construct an expression vector using the coding gene of the designed antimicrobial peptide MZQ-28, introduce the recombinant expression vector into host cells, and obtain the recombinant antimicrobial peptide MZQ-28 through heterologous expression.

[0009] In a second aspect, the present invention also provides a gene encoding the antimicrobial peptide MZQ-28, wherein the nucleotide sequence of the gene encoding the peptide is as shown in (a), (b), or (c). (a) A nucleotide sequence as shown in SEQ ID NO. 2; (b) The nucleotide sequence encoded by hybridization to the nucleotide sequence shown in SEQ ID NO. 2 under stringent conditions; (c) A nucleotide sequence that has more than 80% homology with the nucleotide sequence shown in SEQ ID NO. 2 and encodes a nucleotide sequence.

[0010] Those skilled in the art will fully understand that, since the same amino acid may be determined by multiple different codons, the nucleotide sequence encoding the above-mentioned protein is not limited to one type. It can be obtained by mutating one or more nucleotides of the mutant nucleotide sequence shown in SEQ ID NO. 2 to form a synonymous mutation, resulting in a nucleotide sequence that can also encode the mutant amino acid sequence of the present invention. Alternatively, a nucleotide sequence that can encode the mutant amino acid sequence of the present invention can be designed based on codon optimization.

[0011] In this invention, the nucleic acid may be optimized or unoptimized, and this invention does not limit the specific type of nucleic acid.

[0012] In this invention, the stringent conditions refer to conditions where the probe hybridizes with its target sequence to a level of detectability exceeding that with other sequences. These stringent conditions are sequence-dependent and can vary depending on the environment. By strictly controlling hybridization or washing conditions, target sequences that are 100% complementary to the probe can be identified. The stringent conditions can be selectively adjusted to allow for some sequence mismatches, thereby enabling the detection of lower levels of similarity.

[0013] In some specific embodiments, the present invention provides a protein gene nucleotide sequence that has 80% identity with the sequence shown in SEQ ID NO. 2; preferably 85% identity, more preferably 90% identity, even more preferably 95% identity, and most preferably 99% identity.

[0014] Thirdly, biological materials containing the aforementioned genes also fall within the scope of protection of this invention, specifically any one of (a) to (c) below: (a) an expression cassette containing the gene shown in SEQ ID NO. 2; (b) a recombinant vector containing the gene shown in SEQ ID NO. 2, or a recombinant vector containing the expression cassette of (a); (c) a recombinant bacterium containing the gene shown in SEQ ID NO. 2, or a recombinant expression cassette containing the expression cassette of (a), or a recombinant vector containing the recombinant vector of (b).

[0015] Furthermore, the recombinant vector is selected from Escherichia coli expression vectors, yeast expression vectors, Bacillus subtilis expression vectors, lactic acid bacteria expression vectors, Streptomyces expression vectors, bacteriophage vectors, filamentous fungal expression vectors, or plant expression vectors. Furthermore, the recombinant bacteria used for recombinant expression of the antimicrobial peptide MZQ-28 are selected from one of Escherichia coli, Agrobacterium, yeast, Bacillus subtilis, lactic acid bacteria, actinomycetes, and filamentous fungi.

[0016] Fourthly, the present invention also provides the application of antimicrobial peptide MZQ-28 in the preparation of antimicrobial products.

[0017] Further, the application is any one of (a) to (c) below: (a) preparing antibacterial agents; (b) preparing pharmaceuticals; (c) preparing additives.

[0018] Furthermore, the antimicrobial peptide MZQ-28 is used to inhibit the growth of at least one of the following bacteria: Staphylococcus spp., Escherichia spp., Salmonella spp., Vibrio spp., Acinetobacter spp., and Propionibacterium spp.

[0019] Fifthly, an antibacterial drug comprising the antimicrobial peptide MZQ-28 also falls within the scope of protection of this invention.

[0020] Furthermore, the antimicrobial agent also comprises one or more pharmaceutically acceptable carriers; Optionally, the pharmaceutically acceptable carrier includes one or more of the following: solvent, solubilizer, cosolvent, emulsifier, flavoring agent, odorant, colorant, binder, disintegrant, filler, lubricant, wetting agent, osmotic pressure regulator, pH regulator, stabilizer, surfactant, and preservative.

[0021] In a sixth aspect, the present invention provides a method for inhibiting or killing bacteria, wherein the method comprises contacting bacteria with the antimicrobial peptide MZQ-28 shown in SEQ ID NO. 1 or a pharmaceutically acceptable salt, ester or solvate thereof, or contacting bacteria with an antimicrobial drug containing the antimicrobial peptide MZQ-28; Optionally, the bacterial infection is selected from Staphylococcus, Escherichia, Salmonella, Vibrio, Acinetobacter, and Propionibacterium.

[0022] Beneficial Effects: This invention, based on artificial intelligence-based screening and design, yields the novel antimicrobial peptide MZQ-28, which maintains its antibacterial activity under high temperature and extreme pH conditions. It exhibits significant inhibitory effects against both Gram-negative bacteria (Escherichia coli, Salmonella choleraesuis) and Gram-positive bacteria (Staphylococcus aureus), enriching the variety and antibacterial spectrum of antimicrobial peptides. With its high stability and broad-spectrum antimicrobial properties, antimicrobial peptide MZQ-28 has potential applications in food preservation, cosmetics, biopesticides, and feed additives, providing a new solution to the increasingly serious problem of antibiotic resistance. Attached Figure Description

[0023] Figure 1 This is a 3D model diagram of the antimicrobial peptide MZQ-28 in this invention; Figure 2 This is a protein purification diagram of the antimicrobial peptide MZQ-28 in this invention; Figure 3 This is a diagram showing the antibacterial activity of the antimicrobial peptide MZQ-28 in this invention; Figure 4 This is a thermal stability diagram of the antimicrobial peptide MZQ-28 in this invention; Figure 5 This is a pH stability diagram of the antimicrobial peptide MZQ-28 in this invention. Detailed Implementation

[0024] To enable those skilled in the art to better understand the technical solutions of the present invention, the present invention will be described in detail below with reference to specific embodiments. Experimental methods in the following embodiments that do not specify specific conditions are generally performed under conventional conditions or as recommended by the manufacturer. Unless otherwise specified, the test materials used in the following embodiments were purchased from conventional biochemical reagent stores. Unless otherwise stated, percentages and parts are by weight. Unless otherwise defined, all technical and scientific terms used herein have the same meaning as those familiar with the art. Furthermore, any methods and materials similar to or equivalent to those described herein can be applied to the present invention. The preferred embodiments and materials described herein are for illustrative purposes only.

[0025] Some of the experimental materials and reagents used in this invention: Strains: Escherichia coli BL21(DE3) was purchased from Kunming Qingke Biotechnology Co., Ltd.; Staphylococcus aureus, Escherichia coli K88, Escherichia coli K99, Streptococcus pneumoniae, and Salmonella choleraesuis were previously preserved in our laboratory.

[0026] Biochemical reagents: Ni-NTA was purchased from Bogelon (Zhejiang) Biotechnology Co., Ltd., IPTG was purchased from Beijing Solarbio Technology Co., Ltd., and kanamycin was purchased from Shanghai Maclean Biotechnology Co., Ltd.

[0027] Culture media: LB liquid medium: 1% peptone (w / v), 0.5% yeast extract (w / v), 1% NaCl (w / v), add distilled water to make up to volume and adjust pH to 7.0; LB solid medium is based on this and 2.0% (w / v) agar is added.

[0028] Example 1: Obtaining the protein sequence of the antimicrobial peptide MZQ-28 1.1 First-order sequences of antimicrobial and non-antimicrobial peptides were obtained from antimicrobial peptide databases such as APD3. Then, their corresponding three-dimensional structures (PDB format) were obtained through batch prediction using AlphaFold2. After preprocessing the sequences and structures, they were input into a feature encoding module. The feature encoding module was constructed based on a pre-trained masked language model (MLM). MLM extracts the sequence-space association features of antimicrobial peptides by fusing and embedding preprocessed three-dimensional structural features into a Transformer backbone network, outputting an antimicrobial peptide vector representation that integrates multimodal information. The sequence generation module is a conditionally controlled diffusion model. The diffusion model, through inputting the feature vectors output by MLM, performs denoising sampling to generate vectors corresponding to novel candidate antimicrobial peptides. These vectors are then reverse-quantized by MLM, transforming the numerical matrix into an amino acid sequence, thus establishing a library of candidate antimicrobial peptides. To ensure a high probability of antimicrobial activity, the designed peptides all meet the following conditions: a. The peptide is a positively charged cation; b. Isoelectric point greater than 8.0; c. It has a double α-helix structure; d. The number of cysteine ​​residues in the sequence is less than 5; e. The sequence length does not exceed 30 amino acids; the adversarial screening module uses a generative adversarial network (GAN) discriminator. After the GAN is pre-trained with positive and negative samples (antimicrobial peptides / non-antimicrobial peptides), it scores the authenticity of candidate sequences generated by the diffusion model and selects candidate sequences with scores higher than a preset threshold; finally, molecular dynamics simulation (MD) is used to evaluate the changes in the root mean square deviation (RMSD) and radius of gyration (Rg) of the target candidate sequence under physiological temperature and pH conditions to verify the structural stability of the target sequence. Then, the sequences with better stability are incorporated into the Martini coarse-grained force field for membrane activity simulation, and finally a novel antimicrobial peptide MZQ-28 with stable structure and membrane activity is obtained (as shown in SEQ ID NO. 1).

[0029] 1.2 The physicochemical properties of the antimicrobial peptide MZQ-28 were predicted using the ProtParam tool, including molecular weight, isoelectric point, net charge, and average hydrophilicity, as shown in Table 1 below: Table 1

[0030] 1.3 The three-dimensional structure of MZQ-28 was constructed using PEP-FOLD3, a software suitable for constructing three-dimensional structures of short peptides, as shown below. Figure 1 As shown.

[0031] Example 2 Preparation of antimicrobial peptide MZQ-28 The antimicrobial peptide MZQ-28 was prepared by heterologous expression, specifically including the construction and transformation of the recombinant vector of the antimicrobial peptide MZQ-28 and the preparation of the target protein.

[0032] Construction of the recombinant vector for the antimicrobial peptide MZQ-28: The expression host was determined according to this embodiment. E. coli Codon usage preference of BL21(DE3) was investigated, and codon optimization was performed on the amino acid sequence of the antimicrobial peptide MZQ-28 to obtain the optimized MZQ-28 encoding nucleotide sequence (as shown in SEQ ID NO. 2). The full-length sequence is 57 bp with a GC content of 45.61%, and a stop codon TAA is introduced at the 3' end of the sequence. The sequence was downloaded from the NCBI database (https: / / www.ncbi.nlm.nih.gov / ) using *Saccharomyces cerevisiae*. Saccharomyces cerevisiae The SUMO tag sequence of the SMT3 protein (amino acid sequence as shown in SEQ ID NO. 3) was codon-optimized to obtain its encoding nucleotide sequence (as shown in SEQ ID NO. 4); the recombinant plasmid SUMO-MZQ-28-pET-28a(+) was synthesized by Kunming Qingke Biotechnology Co., Ltd., and its nucleotide sequence is shown in SEQ ID NO. 5.

[0033] Transformation of the recombinant vector for the antimicrobial peptide MZQ-28: An appropriate amount of recombinant plasmid SUMO-MZQ-28-pET-28a(+) was added to competent E. coli BL21(DE3) cells in a semi-ice, semi-water environment and incubated on ice for 30 min. The cells were then heat-shocked in a 42℃ water bath for 60-90 s and immediately placed on ice for 3-5 min. An appropriate amount of antibiotic-free LB liquid medium was added to a clean bench and incubated at 37℃ and 200 rpm for 1 h in a shaker. An appropriate amount of the incubated bacterial solution was evenly spread onto an LB kanamycin-resistant plate. After 16 h, single colonies were picked for positive clone recombinant screening to obtain the recombinant strain BL21(DE3) / SUMO-MZQ-28.

[0034] Preparation of the target protein: Single colonies of recombinant strain BL21(DE3) / SUMO-MZQ-28 were picked and placed in LB medium with 1‰ (50 mg / ml) kanamycin added. The culture was incubated overnight at 37°C and 200 rpm / min. The overnight culture was then inoculated into fresh LB medium at a 1% inoculum size, with 1‰ (50 mg / ml) kanamycin added. The culture was incubated at 37°C and 200 rpm / min for approximately 4 hours until OD (Organic Demand) was reached. 600mmWhen the concentration was 0.6, IPTG was added for induction at 16℃ and 150 rpm / min for 20 h. The induced bacterial cells were collected by centrifugation at 4℃ and 6500 rpm / min for 10 min using a refrigerated centrifuge. The cells were then resuspended in pH 7.0 citrate-phosphate buffer and sonicated in an ice-water bath. The sonicated bacterial solution was centrifuged at 4℃ and 12000 rpm / min for 10 min using a refrigerated centrifuge. The supernatant was the crude enzyme solution. The target protein was purified by elution using a Ni-NTA affinity chromatography column with a 0-500 mM imidazole gradient. The purified protein was analyzed by SDS-PAGE and showed a single band with a molecular weight consistent with the target protein. Figure 2 As shown, the recombinant antimicrobial peptide MZQ-28 was successfully prepared. The purified recombinant antimicrobial peptide MZQ-28 was placed in a dialysis bag and dialyzed in PBS buffer (pH 7.0) for 12 h. Then, Ulp1 protease was added, and the mixture was digested at 30°C for 3 h to obtain the antimicrobial peptide MZQ-28.

[0035] Example 3: Analysis of the antibacterial activity of the antimicrobial peptide MZQ-28 The antibacterial activity of the antimicrobial peptide MZQ-28 was investigated using the Oxford cup method, which included the following steps: Preparation of indicator bacterial suspension: Indicator bacteria (Staphylococcus aureus, Salmonella choleraesuis, and Escherichia coli K88) frozen at -80℃ were inoculated into 5 ml of LB liquid medium at a 1% inoculation rate and cultured overnight at 37℃ and 200 rpm / min for 12-16 h. 50 μl of the overnight culture was then inoculated into 5 ml of LB liquid medium and cultured at 37℃ and 200 rpm / min. Samples were taken every 10 minutes after 30 min of culture to measure the OD600nm value until it reached 0.1. At this point, the concentration of the indicator bacteria was approximately 10⁻⁶. 8 CFU / ml.

[0036] Spreading: Use a sterile cotton swab to apply an appropriate amount of indicator bacteria suspension evenly to LB solid medium three times. After each spread, rotate the sterile cotton swab and the plate by 60 degrees. Finally, use a sterile cotton swab to spread around the edge of the plate.

[0037] Sample addition: Using sterile tweezers, pick up the sterilized Oxford cup and place it vertically on the plate with the indicator bacteria. Press it gently to ensure close contact between the Oxford cup and the surface of the culture medium. Then add 80 μL of antimicrobial peptide MZQ-28 sample to the Oxford cup. After adding the sample, place it in a 37°C constant temperature incubator and incubate for 12-16 hours.

[0038] Observation and measurement: After removing the Oxford cup with tweezers, observe whether an inhibition zone has formed. Use vernier calipers and the cross-section method to measure the diameter of the inhibition zone. When measuring, use the outer edge of the inhibition zone that completely inhibits bacterial growth as the boundary.

[0039] like Figure 3 As shown, distinct inhibition zones were observed on plates containing Staphylococcus aureus (Gram-positive), Salmonella cholerae, and Escherichia coli K88 (Gram-negative). The measured sizes of the inhibition zones were 18.00 mm, 14.00 mm, and 12.50 mm, respectively. This indicates that the antimicrobial peptide MZQ-28 has a good inhibitory effect on Staphylococcus aureus, Salmonella cholerae, and Escherichia coli K88.

[0040] Example 4: Determination of the MIC value of antimicrobial peptide MZQ-28 The minimum inhibitory concentration (MIC), which is the lowest drug concentration capable of inhibiting bacterial growth and reproduction, was determined using a two-fold serial dilution method. The specific steps included: First, the test strain was inoculated onto LB agar plates and incubated at 37°C for 18-24 hours. Then, a single colony was picked and transferred to LB liquid medium and cultured at 37°C with shaking at 200 rpm / min until the logarithmic growth phase (approximately 5 hours). At this point, the OD600nm value measured using a UV spectrophotometer was 0.1, indicating a bacterial concentration of approximately 1 × 10⁻⁶. 8 CFU / mL; further dilute the bacterial culture with LB liquid medium to the working concentration (2×10⁻⁶). 5 (CFU / mL) for later use.

[0041] In a sterile 96-well plate, add 100 μL of the above bacterial suspension to each well; perform serial two-fold dilutions of the antimicrobial peptide MZQ-28 sample, with an initial concentration of 254.8192 μg / mL; add 100 μL of each concentration gradient sample to the corresponding well, making the final volume of each well 200 μL, shake to mix, and incubate at 37℃ for 16 h.

[0042] The results were analyzed by a combination of visual observation and enzyme-linked immunosorbent assay (ELISA) detection. The lowest concentration at which the antimicrobial peptide MZQ-28 completely inhibited bacterial growth was taken as the MIC value for each bacterium. The results are shown in Table 2.

[0043] Table 2. MICs of antimicrobial peptide MZQ-28 against different bacteria.

[0044] Example 5: Determination of pH stability of antimicrobial peptide MZQ-28: Antimicrobial peptide MZQ-28 samples were thoroughly mixed with equal volumes of buffer solutions with pH values ​​of 3, 4, 6, 7, 11, and 12, respectively, and incubated at 37°C for 1 hour. Subsequently, following the method described in Example 3, Staphylococcus aureus was used as an indicator bacterium to determine its antimicrobial activity under different pH conditions. The antimicrobial activity of the antimicrobial peptide treated with buffer solution at pH 7 was used as a control (relative antimicrobial efficiency was 100%), and the relative antimicrobial efficiency of antimicrobial peptide MZQ-28 after treatment with buffer solutions at different pH values ​​was calculated.

[0045] like Figure 4 As shown, the antimicrobial peptide MZQ-28 can still maintain high antibacterial activity after being treated with buffer solutions in the pH range of 3 to 11 for 1 hour. Even after treatment with buffer solution at pH 3 for 1 hour, it still has a relative antibacterial efficiency of 89.01% against Staphylococcus aureus, indicating that the antimicrobial peptide MZQ-28 has good acid and base stability and a wide pH range.

[0046] Example 6: Determination of the thermal stability of antimicrobial peptide MZQ-28: The antimicrobial peptide MZQ-28 sample was incubated at constant temperatures of 4℃, 25℃, 37℃, 50℃, 70℃, and 90℃ for 1 hour, respectively. Then, following the method described in Example 3, its antimicrobial activity after incubation at different temperatures was determined using Staphylococcus aureus as an indicator bacterium. The antimicrobial activity of the antimicrobial peptide after incubation at 25℃ was used as a control (relative antimicrobial efficiency was 100%).

[0047] like Figure 5 As shown, after treatment at the five temperature conditions in the examples for 1 hour, the relative antibacterial efficiency of antimicrobial peptide MZQ-28 remained above 90%. Even at a treatment temperature of 90°C, the relative antibacterial efficiency against Staphylococcus aureus still reached 91.59%, indicating that antimicrobial peptide MZQ-28 has good temperature stability.

[0048] Finally, it should be noted that the above description is only a preferred embodiment of the present invention. Those skilled in the art, under the guidance of the present invention, can make various similar representations without departing from the spirit and claims of the present invention, and such modifications all fall within the protection scope of the present invention.

Claims

1. An antimicrobial peptide MZQ-28, characterized in that, The amino acid sequence is (a) or (b); (a) A protein composed of the amino acids shown in SEQ ID NO. 1; (b) A functionally equivalent derivative protein consisting of the amino acid sequence shown in SEQ ID NO. 1, with substitution and / or deletion and / or addition of one or more amino acid residues.

2. The encoding gene of the antimicrobial peptide MZQ-28 according to claim 1, characterized in that, The nucleotide sequence of the encoding gene is as shown in (a), (b), or (c); (a) A nucleotide sequence as shown in SEQ ID NO. 2; (b) The nucleotide sequence encoded by hybridization to the nucleotide sequence shown in SEQ ID NO. 2 under stringent conditions; (c) A nucleotide sequence that has more than 80% homology with the nucleotide sequence shown in SEQ ID NO. 2 and encodes a nucleotide sequence.

3. A biomaterial containing the gene of claim 2, characterized in that... It is any one of (a) to (c) below: (a) an expression cassette containing the gene shown in SEQ ID NO. 2; (b) a recombinant vector containing the gene shown in SEQ ID NO. 2, or a recombinant vector containing the expression cassette of (a); (c) a recombinant bacterium containing the gene shown in SEQ ID NO. 2, or a recombinant expression cassette containing the expression cassette of (a), or a recombinant vector containing the recombinant vector of (b).

4. The biomaterial according to claim 3, characterized in that: The recombinant vector is selected from Escherichia coli expression vectors, yeast expression vectors, Bacillus subtilis expression vectors, lactic acid bacteria expression vectors, Streptomyces expression vectors, bacteriophage vectors, filamentous fungal expression vectors, or plant expression vectors; and / or, The recombinant bacteria strain is selected from one of the following: Escherichia coli, Agrobacterium, yeast, Bacillus subtilis, lactic acid bacteria, actinomycetes, and filamentous fungi.

5. The use of the antimicrobial peptide MZQ-28 as described in claim 1 in the preparation of antimicrobial products.

6. The application according to claim 5, characterized in that, The application is any one of the following (a) to (c): (a) preparing antibacterial agents; (b) preparing pharmaceuticals; (c) preparing additives.

7. The application according to claim 5 or 6, characterized in that, It is used to inhibit the growth of at least one of the following bacteria: Staphylococcus, Escherichia, Salmonella, Vibrio, Acinetobacter, and Propionibacterium.

8. An antibacterial drug, characterized in that, Includes the antimicrobial peptide MZQ-28 as described in claim 1.

9. The antibacterial drug according to claim 8, wherein, The antimicrobial agent further comprises one or more pharmaceutically acceptable carriers; and / or, The pharmaceutically acceptable carriers include one or more of the following: solvents, solubilizers, cosolvents, emulsifiers, flavoring agents, odorants, colorants, binders, disintegrants, fillers, lubricants, wetting agents, osmotic pressure regulators, pH regulators, stabilizers, surfactants, and preservatives.

10. A method for inhibiting or killing bacteria, wherein, The method comprises contacting bacteria with the antimicrobial peptide of claim 1 or a pharmaceutically acceptable salt, ester, or solvate thereof, or contacting bacteria with the antimicrobial agent of claim 8 or 9; and / or, The bacterial infections are selected from Staphylococcus, Escherichia, Salmonella, Vibrio, Acinetobacter, and Propionibacterium.

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