A group of low-toxicity bioactive peptides derived from rhynchophorus phyllophagus, encoding genes and applications thereof

Abstract

The application belongs to but is not limited to the field of biological medicine, and discloses a group of low-toxicity bioactive peptides derived from Harbinia crocea, coding genes and applications of the bioactive peptides, including bioactive peptides Blap-3alpha, Blap-3beta, BCaCa2, BCeropin-B, BToxin1, BCCHa or BL(30-59). Amino acid sequences are SEQ ID No:1, SEQ ID No:2, SEQ ID No:3, SEQ ID No:4, SEQ ID No:5, SEQ ID No:6, and SEQ ID No:7 respectively. The sequences are obtained by a multi-strategy joint screening process on gene data measured from a transcriptome of Harbinia crocea. The active peptides have not only the safety advantage of low cytotoxicity, but also excellent antioxidant activity, and some polypeptides exhibit good in-vitro antibacterial effect.

Description

Technical Field

[0001] This invention belongs to, but is not limited to, the field of biomedical technology, and particularly relates to a group of low-toxicity bioactive peptides derived from the beak-tailed tussock, their encoding genes, and their applications. Background Technology

[0002] The overuse of antibiotics has made the prevention and control of drug-resistant bacterial infections a critical clinical issue, making the development of new anti-infection strategies imperative. Meanwhile, natural, safe, low-toxicity, and sustainable green functional ingredients are increasingly becoming a key focus for the pharmaceutical, food, and health industries. Bioactive peptides are polypeptide fragments derived from living organisms that can regulate and positively influence life activities, typically composed of 2-50 amino acids. Bioactive peptides often possess the characteristic of multiple effects per peptide, and are safer, have fewer side effects, are more effective, and are less likely to induce resistance compared to traditional chemical drugs. They show great application potential in the prevention and control of drug-resistant bacteria and the development of green functional ingredients.

[0003] Existing research indicates that insects are rich in a wide variety of bioactive peptides, which have been confirmed to possess multiple biological functions, including antibacterial, antioxidant, anti-inflammatory, blood pressure-lowering, blood sugar-lowering, lipase inhibition, and immunomodulatory effects. Among many insects used for both medicinal and edible purposes, antibacterial and antioxidant peptides are currently the most widely explored core active substances. The robinia pseudoacacia, a long-standing insect used for both medicinal and edible purposes, has been documented in both clinical and folk medicine for treating various malignant tumors. While preliminary studies have identified peptides with anti-Candida albicans activity, demonstrating some development potential, systematic exploration of the active peptides in the robinia pseudoacacia remains insufficient. Current research not only identifies a limited variety of peptides but also lacks in-depth exploration of multifunctional peptides that combine high bioactivity (such as antioxidant and broad-spectrum antibacterial activity) with low cytotoxicity.

[0004] Therefore, further exploration and identification of novel, biologically safe, and highly effective bioactive peptides from *Lithocarpus spicata* is of urgent need and great significance for the development of functional peptide products. Summary of the Invention

[0005] To address the problems existing in the prior art, this invention provides a group of low-toxicity bioactive peptides derived from the beak-tailed tussock, their encoding genes, and applications, which are suitable for the development of functional polypeptide products.

[0006] This invention is achieved by providing a group of bioactive peptides with low cytotoxicity derived from the beak-tailed rostellum methyl gene, wherein the bioactive peptides include Blap-3α, Blap-3β, BCaCa2, BCeropin-B, BToxin1, BCCha, and BL(30-59), which are selected from the amino acid sequences shown in SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, and SEQ ID NO: 7.

[0007] Furthermore, the cells are RAW.264.7.

[0008] Another object of the present invention is to provide a group of peptides or an antioxidant peptide derived from the beak-tailed lipomethyl gene that have multifunctional bioactivity, wherein the multifunctional bioactive peptides having antibacterial and antioxidant activities are Blap-3α, Blap-3β, BCaCa2, BCeropin-B, BToxin1, and BCHa, and wherein the bioactive peptide having only antioxidant activity is BL(30-59).

[0009] The amino acid sequence of the active peptide Blap-3α is shown in SEQ ID NO: 1; the amino acid sequence of the active peptide Blap-3β is shown in SEQ ID NO: 2; the amino acid sequence of the active peptide BCaCa2 is shown in SEQ ID NO: 3; the amino acid sequence of the active peptide BCeropin-B is shown in SEQ ID NO: 4; the amino acid sequence of the active peptide BToxin1 is shown in SEQ ID NO: 5; the amino acid sequence of the active peptide BCHa is shown in SEQ ID NO: 6; and the amino acid sequence of the active peptide BL(30-59) is shown in SEQ ID NO: 7.

[0010] Furthermore, the pathogenic bacteria are bacteria; wherein the bacteria are Gram-negative or Gram-positive bacteria.

[0011] Furthermore, the Gram-negative bacteria are Escherichia coli, Klebsiella pneumoniae, Salmonella, Pseudomonas aeruginosa, Acinetobacter baumannii, or Morganella morganii; the Gram-positive bacteria are methicillin-resistant Staphylococcus aureus or Staphylococcus aureus.

[0012] Furthermore, the peptide exhibits in vitro antioxidant activity.

[0013] Another object of the present invention is to provide the use of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, and SEQ ID NO: 6 in the preparation of medicaments for treating bacterial infectious diseases.

[0014] Another object of the present invention is to provide the application of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, and SEQ ID NO: 7 in the preparation of antioxidant products; among the said polypeptides, the polypeptide with the amino acid sequence SEQ ID No. 7 has the best antioxidant activity and development potential.

[0015] Based on the above technical solutions and the technical problems solved, the advantages and positive effects of the technical solution to be protected by this invention are as follows:

[0016] This invention, using the methyl rostellum of the beak-tailed insect as a source, limits the acquisition of seven bioactive peptides with clearly defined amino acid sequences: Blap-3α, Blap-3β, BCaCa2, BCeropin-B, BToxin1, BCHa, and BL(30-59). This allows the active ingredients to move beyond crude extracts or uncertain peptide fragments, forming a defined peptide sequence combination bounded by SEQ ID NO:1 to SEQ ID NO:7, facilitating subsequent synthesis, quality control, and activity replication verification. All of the aforementioned peptides originate from the same insect genetic resource, but were obtained through a multi-strategy combined screening process; sequence homology is not a defining characteristic among the candidate peptides. Compared to traditional methods that focus on screening and evaluating only a single peptide fragment, this invention can obtain multiple comparable candidate bioactive peptides from the same species, thus facilitating subsequent parallel evaluation and functional screening. Further research shows that the histidine as a whole has low cytotoxicity, and some candidate peptides exhibit good biological activity. Therefore, the active peptides provided by this invention enrich the research content of insect-derived active molecules and provide a candidate molecular basis for subsequent functional research and application development. Furthermore, due to their unique low cytotoxicity, they have a good foundation for industrial transformation.

[0017] This invention addresses the challenge of simultaneously achieving both bioactivity and safety in the application of existing bioactive peptides by providing a novel group of bioactive peptides derived from the beak-tailed scalyx. Activity evaluation of the obtained peptides revealed that this group exhibits extremely low cytotoxicity, good biocompatibility, and safety. Furthermore, several peptides also demonstrated significant in vitro antibacterial and antioxidant activities. This indicates that the bioactive peptides provided by this invention not only maintain good safety but also achieve a unified set of multiple biological functions, overcoming the problem that some bioactive peptides in the prior art often exhibit high activity accompanied by high toxicity, or good safety but limited functionality. Based on the above technical solution and experimental results, this invention has obtained a group of bioactive peptide molecules that combine low cytotoxicity, good biocompatibility, and antibacterial and antioxidant activities, achieving an effective balance between activity and safety.

[0018] (1) The expected benefits and commercial value of the technical solution of this invention after transformation are as follows:

[0019] This invention provides a group of novel bioactive peptides derived from the beak-tailed lutea, exhibiting low cytotoxicity, good biocompatibility, and multiple activities including antibacterial and antioxidant effects, thus possessing significant development and utilization value. These peptides can serve as candidate molecules for naturally derived functional peptides, enabling further research and development in antibacterial agents, antioxidant agents, and multifunctional peptide products. Furthermore, based on their good safety and comprehensive bioactivity, they also hold promise for applications in pharmaceuticals, functional biological products, cosmetics, and related biomaterials. In addition, the bioactive peptide resources provided by this invention can provide a molecular basis for subsequent structural optimization, functional mechanism research, and the development of a series of products, demonstrating promising transformational prospects and application value.

[0020] (2) The technical solution of this invention fills a technical gap in the industry both domestically and internationally:

[0021] A review and analysis of existing technologies reveals that while there are some reports on research on *Euphorbia pulcherrima*, the main focus is on organic extracts and their active ingredients. A few studies also address the direct isolation of antimicrobial peptides from hemolymph. Beyond this, systematic exploration of bioactive peptides derived from *Euphorbia pulcherrima*, the discovery of specific novel peptide structures, and research on their comprehensive biological activities are relatively rare. In particular, no bioactive peptide structures or technical solutions identical or substantially the same as those described in this invention have been disclosed. This invention has extracted and obtained a new group of bioactive peptides from *Euphorbia pulcherrima*, and verified their cytotoxicity, biocompatibility, antibacterial, and antioxidant activities. The resulting technical solution differs from existing technologies that primarily focus on organic extracts or are limited to the direct isolation and identification of known antimicrobial peptides from hemolymph. This invention further expands the research scope of bioactive substances derived from *Euphorbia pulcherrima* and supplements the technical content regarding the structure and functional evaluation of novel bioactive peptides from this source. Attached Figure Description

[0022] Figure 1 This is a report on high-performance liquid chromatography and mass spectrometry analysis of candidate active peptides after chemical synthesis, provided in embodiments of the present invention (SEQ ID No: 1 to SEQ ID NO: 2).

[0023] Figure 2 This is a report on high-performance liquid chromatography and mass spectrometry analysis of candidate active peptides after chemical synthesis, as provided in embodiments of the present invention (SEQ ID No: 3 to SEQ ID NO: 4).

[0024] Figure 3 This is a report on high-performance liquid chromatography and mass spectrometry analysis of candidate active peptides after chemical synthesis, provided in embodiments of the present invention (SEQ ID No: 5 to SEQ ID NO: 7).

[0025] Figure 4 The cytotoxicity of the candidate active peptides SEQ ID NO: 1 to SEQ ID NO: 7 to RAW264.7 cells provided in the embodiments of the present invention is shown.

[0026] Figure 5 These are the results of the inhibition zone experiment of the candidate active peptides SEQ ID NO: 1 to SEQ ID NO: 7 provided in the embodiments of the present invention;

[0027] Figure 6 These are the in vitro antioxidant experiment results of the candidate active peptides SEQ ID NO: 1 to SEQ ID NO: 7 provided in the embodiments of the present invention;

[0028] Figure 7This is a flowchart illustrating the preparation and detection process of the bioactive peptides SEQ ID NO: 1 to SEQ ID NO: 7 provided in the embodiments of the present invention. Detailed Implementation

[0029] To make the objectives, technical solutions, and advantages of this invention clearer, the invention will be further described in detail below with reference to embodiments. It should be understood that the specific embodiments described herein are merely illustrative and not intended to limit the invention.

[0030] This invention provides a group of bioactive peptides with low cytotoxicity derived from the beak-tailed rostellum methyl gene. The bioactive peptides include Blap-3α, Blap-3β, BCaCa2, BCeropin-B, BToxin1, BCCHa, and BL(30-59), which are selected from the amino acid sequences shown in SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, and SEQ ID NO: 7.

[0031] The cells in question were RAW.264.7.

[0032] This invention provides a group of peptides or an antioxidant peptide derived from the beak-tailed rostellum methyl gene that have multifunctional biological activity. The multifunctional active peptides with antibacterial and antioxidant activities include Blap-3α, Blap-3β, BCaCa2, BCeropin-B, BToxin1, and BCHa. The active peptides with antioxidant activity only include BL(30-59).

[0033] The amino acid sequence of the active peptide Blap-3α is shown in SEQ ID NO: 1; the amino acid sequence of the active peptide Blap-3β is shown in SEQ ID NO: 2; the amino acid sequence of the active peptide BCaCa2 is shown in SEQ ID NO: 3; the amino acid sequence of the active peptide BCeropin-B is shown in SEQ ID NO: 4; the amino acid sequence of the active peptide BToxin1 is shown in SEQ ID NO: 5; the amino acid sequence of the active peptide BCHa is shown in SEQ ID NO: 6; and the amino acid sequence of the active peptide BL(30-59) is shown in SEQ ID NO: 7.

[0034] The pathogenic bacteria are bacteria; wherein the bacteria are Gram-negative or Gram-positive bacteria. The Gram-negative bacteria are Escherichia coli, Klebsiella pneumoniae, Salmonella, Pseudomonas aeruginosa, Acinetobacter baumannii, or Morganella morganii; the Gram-positive bacteria are methicillin-resistant Staphylococcus aureus or Staphylococcus aureus.

[0035] The present invention provides the application of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, and SEQ ID NO: 6 in the preparation of medicaments for treating bacterial infectious diseases.

[0036] This invention provides the application of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, and SEQ ID NO: 7 in the preparation of antioxidant products; among the peptides, the peptide with the amino acid sequence SEQ ID No. 7 has the best antioxidant activity and development potential.

[0037] Example 1: Discovery of bioactive peptides SEQ ID NO: 1 to SEQ ID NO: 7

[0038] The bioactive peptide involved in this invention is a new bioactive peptide of *Rhizoctonia solani*, obtained through the following method: Analysis of *Rhizoctonia solani* transcriptome data was used to systematically screen for potential bioactive peptides. Based on conventional screening pathways such as sequence homology alignment and precursor signal peptide prediction, a supplementary bioinformatics strategy based on sequence characteristics was introduced. This strategy, combined with potential restriction enzyme site analysis and physicochemical parameter evaluation, delineated short peptide boundaries and prioritized candidate precursor regions. Thus, in addition to obtaining antimicrobial peptide-related genes, antioxidant-related genes and neural regulatory genes involved in immune process regulation were also obtained. The peptide gene sequences are as follows:

[0039] Bioactive peptide (Blap-3α): YWRGSKGPNGRVLYNIFHIRLRKVIK (SEQ ID NO: 1)

[0040] Bioactive peptide (Blap-3β): HWRGSKYLNGCVLYNIFHILLRKV (SEQ ID NO: 2)

[0041] Bioactive peptide (BCaCa2): RLLKTQLLKHMTVGARVVRGIDWKWR (SEQ ID NO: 3)

[0042] Bioactive peptide (BCeropin-B): WKGWKKIEKAGRRVFKY (SEQ ID NO: 4)

[0043] Bioactive peptide (BToxin1): RKLMCVPFIYGGCRGNRNNFL (SEQ ID NO: 5)

[0044] Bioactive peptide (BCCHa): SCLSYGHACWGAHGKR-NH2 (SEQ ID NO: 6).

[0045] Bioactive peptide (BL(30-59)): QQCLSCIEATSSCNTSTCDGGLCGPFG (I SEQ ID NO: 7).

[0046] Example 2: Preparation of bioactive peptides SEQ ID NO: 1 to SEQ ID NO: 7

[0047] The obtained candidate active peptide sequences were sent to Wuhan Dangang Biotechnology Co., Ltd. for chemical synthesis. High-performance liquid chromatography and mass spectrometry analysis confirmed that the synthesis was effective, achieving a purity of 98%. Results are shown below. Figures 1-3 .

[0048] Example 3: Cytotoxicity assay of bioactive peptides SEQ ID NO: 1 to SEQ ID NO: 7

[0049] Cytotoxicity assays were performed using the CCK-8 assay. The mouse macrophage cell line RAW264.7 was used. 90 μl of cell suspension (5.5 × 10⁻⁶) was added to each well of a 96-well plate. 4 The samples were cultured at 37°C in a 5% CO2 incubator (number of samples per mL). After 24 h, 10 μl of peptide solution (final concentrations of 100, 50, 25, 12.5, and 6.25 μg / mL) was added, ensuring three replicates. The samples were cultured again for 24 h. The drug and culture medium were removed, the plates were washed with PBS, and fresh culture medium containing CCK-8 was added (final CCK-8 concentration in the wells was 10%). The plates were then incubated in the dark for 1.5 h, and the absorbance was measured at 450 nm. Results are as follows: Figure 4As shown, the cell viability of the candidate peptides remained at a high level overall within a concentration range of 100 μg / mL to 6.25 μg / mL. The cell viability of all bioactive peptide groups was above 80%, indicating that these peptides did not exhibit significant cytotoxicity under the experimental conditions. During the experiment, it was observed that all candidate peptides maintained good dispersion after being added to the cell culture medium, with no visible precipitation, indicating good solubility and processing stability in the experimental system. This helps ensure the consistency of cell exposure conditions, thereby improving the reliability of the detection results.

[0050] Implementation Case 4: Detection of inhibition zones of bioactive peptides SEQ ID NO: 1 to SEQ ID NO: 7

[0051] Escherichia coli, Klebsiella pneumoniae, Salmonella, Pseudomonas aeruginosa, Acinetobacter baumannii, Morganella morganii, methicillin-resistant Staphylococcus aureus, and Staphylococcus aureus were cultured separately in LB medium to the logarithmic growth phase. The bacterial concentration was adjusted to 1×10⁻⁶. 6 CFU / mL was evenly spread onto MHⅡ solid culture plates and allowed to stand. Sterilized filter paper discs, carrying the peptide at a concentration of 80 μg / disc, were then attached to agar and incubated at 4℃. The culture dishes were then inverted and placed in a 37℃ incubator for 18-20 h. The plates were then removed and the presence of inhibition zones was observed. Inhibition zones would be visible if antibacterial activity was present; otherwise, no inhibition zone would be observed.

[0052] The results are as follows Figure 5 As shown, SEQ ID NO: 1 shows activity against Acinetobacter baumannii, methicillin-resistant Staphylococcus aureus, or Staphylococcus aureus; SEQ ID NO: 2 shows activity against Escherichia coli, Klebsiella pneumoniae, Pseudomonas aeruginosa, Acinetobacter baumannii, methicillin-resistant Staphylococcus aureus, or Staphylococcus aureus; SEQ ID NO: 3 shows activity against Escherichia coli, Klebsiella pneumoniae, Salmonella, Pseudomonas aeruginosa, Acinetobacter baumannii, or Staphylococcus aureus; SEQ ID NO: 4 shows activity against Escherichia coli, Klebsiella pneumoniae, Salmonella, Pseudomonas aeruginosa, Acinetobacter baumannii, methicillin-resistant Staphylococcus aureus, or Staphylococcus aureus; SEQ ID NO: 5 shows activity against Pseudomonas aeruginosa, Acinetobacter baumannii, or Staphylococcus aureus; SEQ ID NO: 6 shows activity against Staphylococcus aureus, exhibiting slight activity.

[0053] Example 5: Determination of the minimum inhibitory concentration (MIC) of bioactive peptides SEQ ID NO: 1 to SEQ ID NO: 4

[0054] To further evaluate the antibacterial activity of candidate active peptides, the minimum inhibitory concentration (MIC) was determined for candidate peptides that performed well in the inhibition zone experiment. After culturing the bacterial culture to the logarithmic growth phase, the medium was adjusted to 2 × 10⁻⁶ m² / L using MHB medium. 5 CFU / mL. Prepare 256 μg / mL of the test peptide using sterile aqueous solution (0.2% BSA + 0.01% acetic acid). Dilute to 50 µL per well in a 96-well plate using a two-fold dilution method. Add bacterial culture and mix well. Include a negative control, peptide solvent control, and growth control. After incubation at 37℃ for 16 h, measure the absorbance at 600 nm. The lowest final concentration corresponding to the well with no bacterial growth is defined as the MIC.

[0055] Table 1: Minimum inhibitory concentrations (MICs) of the four novel bioactive peptides exhibiting the best antibacterial activity against Escherichia coli and Staphylococcus aureus.

[0056] Example 6: ABTS of bioactive peptides SEQ ID NO: 1 to SEQ ID NO: 7 + Free radical scavenging experiment

[0057] A 7.4 mM ABTS stock solution was prepared, with 2.45 mM potassium persulfate as the stock solution concentration. These were mixed in a 1:1 ratio to obtain ABTS. + Keep away from light overnight and prepare fresh before use. During the experiment, use ABTS... + Mix with sample reagents, incubate at 30℃ for 6 min in the dark, and then detect the absorbance at 734 nm. A background group, experimental group, blank control group, and positive control group need to be established. Results are verified by ABTS. + Scavenging rate (%) = [1 - (OD)] 实验组 –OD 背景组 ) / (OD 空白对照组 –OD 背景组 )]×100%.

[0058] The results are as follows Figure 6 As shown, the analysis of ABTS + Free radical scavenging experiment results and bar chart. IC50 values ​​for different peptides. 50 The results are as follows: IC of SEQ ID NO: 1 50 The IC is 36.73 μM; SEQ ID NO: 2 50 22.72 μM; IC of SEQ ID NO:3 50 The concentration was 237.58 μM; IC of SEQ ID NO: 4 50 The IC is 75.67 μM; SEQ ID NO: 5 50The IC is 18.34 μM; SEQ ID NO: 6 50 The value is 23 μM. IC of SEQ ID NO: 7 50 It is 17.33 μM.

[0059] This invention identified and obtained seven bioactive peptides, which were then chemically synthesized. The peptides all exhibited low cytotoxicity and demonstrated in vitro biological activity. Except for SEQ ID NO: 7, which only showed antioxidant activity, SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, and SEQ ID NO: 6 all showed some degree of antibacterial and antioxidant activity.

[0060] The above description is merely a specific embodiment of the present invention, but the scope of protection of the present invention is not limited thereto. Any modifications, equivalent substitutions, and improvements made by those skilled in the art within the scope of the technology disclosed in the present invention, and within the spirit and principles of the present invention, should be covered within the scope of protection of the present invention.

Claims

1. A group of bioactive peptides with low cytotoxicity derived from the beak-tailed rostellum methyl gene, characterized in that, The active peptides include Blap-3α, Blap-3β, BCaCa2, BCeropin-B, BToxin1, BCHa, and BL(30-59), which are selected from the amino acid sequences shown in SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, and SEQ ID NO:

7.

2. The active peptide as described in claim 1, characterized in that, The cells in question were RAW.264.

7.

3. A group of peptides or an antioxidant peptide derived from the beak-tailed rostellum methyl gene that have multifunctional bioactivity, wherein the multifunctional bioactive peptides having antibacterial and antioxidant activities include Blap-3α, Blap-3β, BCaCa2, BCeropin-B, BToxin1, and BCHa, wherein the bioactive peptide has only antioxidant activity of BL(30-59). The amino acid sequence of the active peptide Blap-3α is shown in SEQ ID NO: 1; the amino acid sequence of the active peptide Blap-3β is shown in SEQ ID NO: 2; the amino acid sequence of the active peptide BCaCa2 is shown in SEQ ID NO: 3; the amino acid sequence of the active peptide BCeropin-B is shown in SEQ ID NO: 4; the amino acid sequence of the active peptide BToxin1 is shown in SEQ ID NO: 5; the amino acid sequence of the active peptide BCHa is shown in SEQ ID NO: 6; and the amino acid sequence of the active peptide BL(30-59) is shown in SEQ ID NO:

7.

4. The active peptide as described in claim 3, characterized in that, The pathogenic bacteria are bacteria; wherein the bacteria are Gram-negative or Gram-positive bacteria.

5. The active peptide as described in claim 3, characterized in that, The Gram-negative bacteria are Escherichia coli, Klebsiella pneumoniae, Salmonella, Pseudomonas aeruginosa, Acinetobacter baumannii, or Morganella morganii; the Gram-positive bacteria are methicillin-resistant Staphylococcus aureus or Staphylococcus aureus.

6. The active peptide as described in claim 3, characterized in that, The peptide has in vitro antioxidant activity.

7. The application of a group of active peptides as described in claims 1-6, characterized in that, The use of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, and SEQ ID NO: 6 in the preparation of medicaments for treating bacterial infectious diseases.

8. The application of a group of active peptides as described in claims 1-6, characterized in that, The application of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, and SEQ ID NO: 7 in the preparation of antioxidant products.

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