CN117886889A - Antibacterial peptide AI18 and application thereof - Google Patents
Antibacterial peptide AI18 and application thereof Download PDFInfo
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- CN117886889A CN117886889A CN202410047923.6A CN202410047923A CN117886889A CN 117886889 A CN117886889 A CN 117886889A CN 202410047923 A CN202410047923 A CN 202410047923A CN 117886889 A CN117886889 A CN 117886889A
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Classifications
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- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change
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- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
Abstract
The invention discloses an antibacterial peptide AI18 and application thereof, and belongs to the technical field of biology. The amino acid sequence of the antibacterial peptide AI18 is shown as SEQ ID NO.1, and the C terminal of the antibacterial peptide AI18 is amidated. The antibacterial peptide AI18 provided by the invention has broad-spectrum antibacterial activity, and has remarkable antibacterial effect on gram-negative bacteria resistant bacteria and non-resistant bacteria; animal model experiments show that the antibacterial peptide AI18 has good in-vivo antibacterial activity; the antibacterial peptide AI18 can exist in plasma more stably, has extremely low hemolytic activity and good biological safety, can be used for treating bacterial infection, and can also be applied to other scenes needing sterilization or inhibiting bacterial growth. The antibacterial peptide AI18 provided by the invention has the advantages of short sequence, small molecular weight, low chemical synthesis difficulty and capability of saving the large-scale production cost.
Description
Technical Field
The invention relates to the technical field of biology, in particular to an antibacterial peptide AI18 with high antibacterial activity and application thereof.
Background
In recent years, the abuse of antibiotics causes a series of problems of the generation of a large number of drug-resistant strains, the reduction of the curative effect of the antibiotics and the like, and seriously threatens the health of human beings and animals. As a possible substitute for antibiotics, the antibacterial peptide (antimicrobial peptides, AMPs) has broad-spectrum antibacterial activity, has inhibiting and killing effects on partial viruses, parasites, tumor cells and the like, is not easy to generate drug resistance, and has good application prospects in the research fields of medicine, veterinary medicine, life science and the like.
The antibacterial peptide is an alkaline polypeptide substance with antibacterial activity which is generated by in vivo induction, is an important component of the natural immune system of a biological organism, has the molecular weight of about 2000-7000 and consists of 20-60 amino acid residues. Most of the active polypeptides have the characteristics of strong alkalinity, thermal stability, broad-spectrum antibacterial property and the like. Since the 70 s of the 20 th century, related scholars have successively studied in organisms such as insects, crustaceans, molluscs, amphibians, mammals, humans, plants and the like for similar polypeptides having antibacterial activity. The data show up to 2000 AMPs reported in the literature up to the present time.
However, compared with antibiotics, the antibacterial peptide has the limitations of low antibacterial activity, uncertain toxicity characteristics, easy inactivation during production and transportation, and the like, thus preventing the wide application thereof. To address these challenges, current research is focused on developing antimicrobial peptides with enhanced activity, reduced toxicity, and enhanced hydrolysis resistance. In recent years, related scholars design and optimize an antibacterial protein coding sequence by means of related software auxiliary technologies such as computer biological information prediction and the like, and a series of improved recombinant antibacterial peptides/antibacterial proteins are obtained. In order to solve the problems of unstable spatial structure, hemolytic activity and the like of partial AMPs, researchers try to carry out related experimental researches by replacing partial amino acids in AMPs molecules, modifying the molecular structure and the like so as to enhance the antibacterial activity and reduce the immune response of the AMPs.
For example, patent document CN111925430a discloses that rational molecular design is performed for an antibacterial peptide Pexiganan derived from the epithelium of rana grahami, including increasing the number of electropositive amino acids, increasing the proportion of hydrophobic amino acids, increasing the proportion of α -helices, and properly introducing unnatural amino acids (such as ornithine) and D-type amino acids, so that the optimized antibacterial peptide improves the antibacterial effect to a certain extent, reduces the hemolysis rate, and reduces cytotoxicity.
Most studies of antibacterial peptides today are still in preclinical stages, and relatively few antibacterial peptides exist in patent medicine. Despite the great efforts, only about 80 peptide drugs were approved by regulatory authorities, indicating that the therapeutic-related antibacterial peptides are sparsely distributed in this vast sequence space. Therefore, development of an antibacterial peptide having high antibacterial activity and little side effect is urgent.
Disclosure of Invention
The invention aims to provide a novel antibacterial peptide with strong antibacterial activity, simple structure and good biological safety.
In order to achieve the above purpose, the invention adopts the following technical scheme:
the invention designs and obtains the antibacterial peptide AI18 by artificial intelligence technology, the amino acid sequence of which is shown as SEQ ID NO.1, and the C terminal of which is amidated.
Specifically, the sequence of the antibacterial peptide AI18 is as follows: ala-Ile-Pro-Lys-Arg-Leu-Arg-Arg-Phe-Tyr-Leu-Arg-Ala-Leu-Ala-Arg-Arg-Leu-NH 2 。
In the present invention, the antibacterial peptide AI18 can be prepared by chemical synthesis or genetic engineering.
The invention provides application of the antibacterial peptide AI18 in preparation of antibacterial drugs.
Further, the antibacterial agent is an agent for inhibiting escherichia coli, pseudomonas aeruginosa, acinetobacter baumannii, klebsiella pneumoniae, staphylococcus aureus, propionibacterium acnes or enterococcus faecalis.
Further, the minimum antibacterial concentration of the antibacterial peptide AI18 on the escherichia coli is 8 mug/mL; the minimum antibacterial concentration for pseudomonas aeruginosa is 8 mug/mL; the minimum antibacterial concentration of Acinetobacter baumannii is 8 mug/mL; the minimum antibacterial concentration for klebsiella pneumoniae is 16 mug/mL; the minimum inhibitory concentration for staphylococcus aureus is 32 mug/mL; the minimum antibacterial concentration of propionibacterium acnes is 16 mug/mL; the minimum inhibitory concentration for enterococcus faecalis was 32. Mu.g/mL.
The cells inhibited by the antibacterial agent include drug-resistant bacteria and non-drug-resistant bacteria. The research of the invention shows that the antibacterial peptide AI18 has better antibacterial activity on drug-resistant bacteria and non-drug-resistant bacteria of escherichia coli, pseudomonas aeruginosa, acinetobacter baumannii and klebsiella pneumoniae.
Compared with polymyxin E, the antibacterial peptide AI18 provided by the invention has longer duration of bactericidal action on escherichia coli, and can effectively prevent bacterial drug resistance. The research of the invention shows that the antibacterial peptide AI18 has good in-vivo antibacterial activity and plays a synergistic antibacterial role with components in blood plasma. And has low hemolytic activity and biological safety.
The antibacterial peptide AI18 provided by the invention can be applied to various scenes needing to kill or inhibit bacteria, and particularly, the invention also provides application of the antibacterial peptide AI18 in preparation of preservatives, daily chemical washing products and medical instruments with antibacterial effect.
The invention provides a biological antibacterial agent, and the antibacterial component of the biological antibacterial agent comprises the antibacterial peptide AI18. The antibacterial peptide AI18 and pharmaceutically or edible auxiliary materials are combined to prepare the corresponding biological antibacterial agent.
The invention provides a preservative, which comprises the antibacterial peptide AI18.
Further, the preservative is a preservative for foods or a preservative for cosmetics.
The invention provides a daily chemical washing article composition which comprises the antibacterial peptide AI18.
Further, the composition may be, but is not limited to, a hand wash, soap, body wash, shampoo, toothpaste, liquid laundry, powder laundry, and the like.
The invention provides a medical dressing, which comprises the antibacterial peptide AI18 and a matrix.
The invention has the beneficial effects that:
(1) The antibacterial peptide AI18 provided by the invention has broad-spectrum antibacterial activity, and has remarkable antibacterial effect on gram-negative bacteria resistant bacteria and non-resistant bacteria; animal model experiments show that the antibacterial peptide AI18 has good in-vivo antibacterial activity; the antibacterial peptide AI18 can exist in plasma more stably, has extremely low hemolytic activity and good biological safety, can be used for treating bacterial infection, and can also be applied to other scenes needing sterilization or inhibiting bacterial growth.
(2) The antibacterial peptide AI18 provided by the invention has the advantages of short sequence, small molecular weight, low chemical synthesis difficulty and capability of saving the large-scale production cost.
Drawings
FIG. 1 is a time sterilization curve of the antimicrobial peptide AI18 against E.coli ATCC 25922.
FIG. 2 shows the haemolysis of the antimicrobial peptide AI18 at various concentrations.
FIG. 3 shows the induced resistance of the antibacterial peptide AI18 to E.coli ATCC 25922, wherein NOR is norfloxacin; COL is polymyxin E.
FIG. 4 shows the results of plasma stability test of the antibacterial peptide AI18.
FIG. 5 shows the in vivo antibacterial activity of the antibacterial peptide AI18.
Fig. 6 is a histological image of a section of lung tissue. First row: overview of lung tissue after H & E staining (scale bar, 500 μm). Second row: detailed histological images of black box subregions (scale bar, 100 μm). Experiments were repeated with similar results showing a representative graph. The first column is the mouse lung tissue image of the PBS-treated group, the second column is the mouse lung tissue image of the AI 18-treated group, the third column is the mouse lung tissue image of the Indolicidin-treated group, and the fourth column is the normal healthy mouse lung tissue image.
Detailed Description
The invention will be further illustrated with reference to specific examples. The following examples are only for illustrating the present invention and are not intended to limit the scope of the present invention. Modifications and substitutions to methods, procedures, or conditions of the present invention without departing from the spirit and nature of the invention are intended to be within the scope of the present invention.
The test methods used in the following examples are conventional methods unless otherwise specified; the materials, reagents and the like used, unless otherwise specified, are those commercially available.
Experimental materials used in the following examples:
1. strain
The standard strains used in this experiment were: enterococcus faecalis ATCC 29212, staphylococcus aureus ATCC 29213, klebsiella pneumoniae ATCC 700603, acinetobacter baumannii ATCC 19606, pseudomonas aeruginosa ATCC 27853, escherichia coli ATCC 25922, propionibacterium acnes ATCC 6919 and ATCC 11827.
The clinical drug resistant strains include: the drug sensitivity results of full-drug resistance (PDR) klebsiella pneumoniae 418015, drug-resistant (XDR) klebsiella pneumoniae 325016, multi-drug resistance (MDR) klebsiella pneumoniae 327004, MDR escherichia coli 103231, MDR pseudomonas aeruginosa 304238, and MDR acinetobacter baumannii 316039 are shown in table 1.
TABLE 1 clinical strain drug sensitivity results
Note that: r: drug resistance; s: sensitivity; i: and (5) intermediating.
2. Medicament
Polymyxin E: CAS number 1066-17-7, purchased from Shanghai Bi, inc. of medical technology Co., ltd; norfloxacin: CAS number 70458-96-7, purchased from Shanghai Michelin Biochemical technologies Co., ltd; antibacterial peptide Indolicidin: CAS number 140896-21-5, available from Nanjing peptide Valley Biotech Co.
Example 1
1. Preparation of antibacterial peptide AI18
The antibacterial peptide AI18 provided in this example is designed by artificial intelligence technology, and has the amino acid sequence: AIPKRLRRFYLRALARRL (SEQ ID NO. 1) the C-terminus is amidated, in particular, the structure of which is Ala-Ile-Pro-Lys-Arg-Leu-Arg-Arg-Phe-Tyr-Leu-Arg-Ala-Leu-Ala-Arg-Arg-Leu-NH 2 . The biological company was entrusted with the solid phase synthesis of the antimicrobial peptide AI18.
2. MIC determination of antimicrobial peptides
(1) MIC determination method for enterococcus faecalis, staphylococcus aureus, klebsiella pneumoniae, acinetobacter baumannii, pseudomonas aeruginosa and escherichia coli
The determination was performed by a micro broth dilution method according to the MIC determination procedure guidelines of the american society for Clinical and Laboratory Standards (CLSI). The antimicrobial peptide was first dissolved in sterile distilled water at an initial concentration of 5120 μg/mL and stored at 4 ℃. In use, the antimicrobial peptides were diluted to 512 μg/mL with cation-adjusted Mueller-Hinton broth (CAMHB) and then serially diluted 2-fold in 96-well plates. Adjusting the bacterial culture solution to 0.5 McO concentration, diluting with fresh CAMHB 100 times, adding 100 μl into 96-well plate containing antibacterial peptide to give final bacterial concentration of 5×10 5 CFU/mL. After incubation at 37 ℃ for 18 hours, the MIC value is the minimum concentration of antimicrobial peptide at which no apparent bacterial growth is observed visually.
(2) MIC determination method of propionibacterium acnes
Activated propionibacterium acnes standard strains (including ATCC 6919 and ATCC 11827) were inoculated into BHI solid medium and incubated in anaerobic bags at 37 ℃ for 48h, after which the bacterial concentration was determined by microscopic examination every 1h to determine the logarithmic growth phase. When the growth reached the logarithmic phase, 7000rpm was set offThe pellet was resuspended 3 times in fresh sterile BHI medium for 10min and its OD was measured 600 Is about 0.3 for standby. Stock solutions were prepared at a concentration of 128 μg/mL by dissolving the polypeptides in sterile distilled water, with 3 rows of duplicate wells per polypeptide/control. 200 mu L of liquid medicine is added in the 1 st row, 100 mu L of corresponding culture medium is added in the 2-12 th row, 100 mu L is sucked from the 1 st row to the next row, the liquid is repeatedly blown, the dilution is sequentially performed by multiple ratio, and the 100 mu L of the last row is discarded, so that the polypeptide concentration is 128, 64, 32, 16, 8, 4, 2, 1, 0.5, 0.25 and 0.125 mu g/mL. The concentration of clindamycin as a control drug was set to the same polypeptide. And then adjusting the concentration of the bacterial liquid to 0.5 McO concentration, diluting the bacterial liquid by 100 times, sucking 100 mu L of bacterial liquid, adding the bacterial liquid into corresponding holes, placing a 96-well plate into an anaerobic bag for culturing for 48 hours, and visually observing the concentration of a clarification hole to obtain the lowest antibacterial concentration.
The results are shown in tables 2 and 3.
TABLE 2 antibacterial Activity of AI18 against 8 Standard strains
| MIC of antibacterial peptide AI18 a (μg/mL) | |
| ATCC 29212 b | 32 |
| ATCC 29213 c | 32 |
| ATCC 700603 d | 16 |
| ATCC 19606 e | 8 |
| ATCC 27853 f | 8 |
| ATCC 25922 g | 8 |
| ATCC6919 h | 16 |
| ATCC11827 h | 16 |
Note that: a: minimum inhibitory concentration; b: enterococcus faecalis; c: staphylococcus aureus; d: klebsiella pneumoniae; e: acinetobacter baumannii; f: pseudomonas aeruginosa; g: coli; h: propionibacterium acnes; all quality controls were within the allowed range, all growth control wells were cloudy, and blank control wells were clear.
TABLE 3 antibacterial Activity of AI18 against drug-resistant bacteria
| MIC of antibacterial peptide AI18 (μg/mL) | |
| 418015 | 32 |
| 325016 | 8 |
| 327004 | 16 |
| 103231 | 4 |
| 304238 | 16 |
| 316039 | 8 |
As can be seen from Table 2, the MIC of AI18 for Standard Klebsiella pneumoniae (ATCC 700603), acinetobacter baumannii (ATCC 19606), pseudomonas aeruginosa (ATCC 27853), escherichia coli (ATCC 25922), propionibacterium acnes (ATCC 6919 and ATCC 11827) were all between 8-16 μg/mL.
As shown in Table 3, AI18 also shows better antibacterial activity against clinically resistant bacteria, with MIC ranging from 4-32 μg/mL.
3. Time sterilization experiment
The bactericidal kinetics of AI18 against standard e.coli ATCC 25922 were studied. The E.coli broth was adjusted to a concentration of 0.5 M.RTM, diluted 100-fold with fresh CAMHB medium and incubated at 37℃and 150rpm for 3-4 hours to bring the bacteria to the logarithmic growth phase. 3 shaking tubes were taken and 10mL of 4 XMIC polymyxin E, AI at 2. Mu.g/mL and 32. Mu.g/mL, respectively, were dissolved in the CAMHB medium, and 1 shaking tube was taken and 10mL of the CAMHB medium was added. Regulating the coliform bacteria liquid in logarithmic growth phase to 1MCF, diluting 100 times, adding into 4 shaking tubes to obtain bacteria liquid with final concentration of 3×10 6 CFU/mL and incubated at 37℃and 150 rpm. Serial dilutions 10-fold were made in fresh CAMHB medium at 0, 2, 4, 6, 18 and 24 hours, and the results were read by dropping on Mueller-Hinton agar (MHA) plates and incubating at 37 ℃ for 18-24 hours at 150 rpm. The blank control was not added with the antimicrobial peptide and the positive control was polymyxin E.
As a result, as shown in FIG. 1, AI18 of 4×MIC killed all E.coli at 2h, and no E.coli could resume growth until 24 h. While 4×mic polymyxin E showed rapid bactericidal effect at 2h, bacteria gradually recovered to grow after 6h of co-incubation, and the bacterial concentration at 18h was comparable to that of the blank. The AI18 has shown to sterilize standard e.coli at a rate comparable to polymyxin E but for a longer duration of action.
4. Antibacterial peptide hemolysis experiment
Fresh human Red Blood Cells (RBCs) were washed three times with sterile PBS and then added to 96-well U-shaped bottom plates containing different concentrations of antimicrobial peptide to give a RBCs concentration of 2% and an antimicrobial peptide concentration of 1000-7.8 μg/mL with a final volume of 200 μl per well. RBCs treated with PBS alone served as negative control and RBCs treated with 0.5% Triton X-100 served as positive control. After incubation at 37℃for 1 hour, centrifugation at 1200g for 15 minutes at 4 ℃. Supernatants were collected in a new flat bottom 96-well plate and OD was measured 570 . The haemolysis rate was calculated according to the following formula:
as a result, as shown in FIG. 2, the median hemolysis value HC of AI18 50 Greater than 1000. Mu.g/mL indicates very low hemolytic activity.
5. Antibacterial peptide induced drug resistance
The antibacterial peptide plays an antibacterial role mainly by influencing the permeability of cell membranes, and the action mechanism is not limited to a specific target point, so that bacteria are not easy to generate drug resistance to the antibacterial peptide. The experiment is used for researching the induced drug resistance condition of the antibacterial peptide AI18 on escherichia coli ATCC 25922.
Coli ATCC 25922 in logarithmic growth phase was adjusted to 0.5 M.meyeri with CAPHB medium, diluted 100-fold with fresh CAPMB medium, added to 96-well plates containing gradient concentration of antimicrobial peptide, and incubated at 37℃for 18h to read MIC. After 24h of cultivation, the bacterial liquid which can grow under the maximum drug concentration hole is used as a new CAMHB culture medium 1:10000 diluted and added into 96-well plate containing antibiotic peptide with gradient concentration, cultured for 18h and then read the second generation MIC. The 24 th hour is transmitted to the next generation in the same way, and 30 generations are transmitted in total.
Meanwhile, the induction drug resistance of norfloxacin and polymyxin E to escherichia coli ATCC 25922 is compared.
As a result, as shown in FIG. 3, after 30 consecutive generations of induction with 1/2 XMIC of the antimicrobial peptide AI18, neither E.coli developed resistance. The MIC value of the control antibiotic norfloxacin is increased by 16 times after 17 times of continuous passages, and the MIC value is increased to 128 times of the original MIC value after 30 times of continuous passages, and the escherichia coli shows obvious drug resistance to the norfloxacin. From this, it can be seen that the antibacterial peptide AI18 is effective in preventing the generation of bacterial drug resistance.
6. Plasma stability test
Sterile human blood was centrifuged at 3500rpm for 10 minutes to give supernatant, i.e., fresh plasma. AI18 was dissolved in water and fresh plasma at a volume ratio of 1:1 to prepare 2500 μg/mL stock.
200. Mu.L of each sample was collected at 0, 60, 120 and 240 minutes by gently shaking the tube at 100rpm in a shaker at 37℃and 800. Mu.L of 10% methanol containing 1% acetic acid was added: 10% water: in a mixed solvent of 80% acetonitrile to prevent further degradation of AI18. After centrifugation of the suspension, the supernatant was collected and subjected to High Performance Liquid Chromatography (HPLC) using an Agilent ZORBAX C18 reverse phase analytical column (5 μm, 4.6X1250 mm). The mobile phase is phase A: acetonitrile (containing 0.1% trifluoroacetic acid); and B phase: deionized water (containing 0.1% trifluoroacetic acid), gradient elution was 10% to 99% phase a, elution time was 33 minutes, flow rate was 1mL/min, and absorbance was measured at 214nm wavelength. Experiments were repeated 3 times.
The plasma stability test result of the antibacterial peptide AI18 is shown in FIG. 4, and the AI18 is degraded by less than 40% in human plasma for 4h, which shows that the AI18 can exist in human blood more stably.
7. Model of mouse pneumonia infection
To further evaluate the in vivo activity of the antibacterial peptide AI18, they were used to treat XDR klebsiella pneumoniae (325016) -infected neutropenic pneumonia mice.
18 healthy male BALB/c mice (6-8 weeks, 20.+ -.2 g) were intraperitoneally injected with 150mg/kg and 100mg/kg cyclophosphamide 4 days before and 1 day before molding, respectively, to obtain a neutropenia mouse model.Modeling mice were anesthetized on day with isoflurane and then tracheal instilled with 40 μl of XDR klebsiella pneumoniae 325016 in log phase (washed three times with PBS and adjusted to 1×10) 6 CFU/mL).
Mice were then randomly divided into 3 groups of 6 mice each. 10mg/kg AI18, indolicidin or an equivalent amount of PBS was injected intraperitoneally at 2h and 12h after infection, respectively.
All mice were euthanized 24h after molding, lung tissue was weighed under sterile conditions and homogenized with 1mL of sterile PBS. Lung homogenates were diluted ten-fold in sterile PBS and dropped onto MH agar plates, incubated at 37 ℃ for 18-24h, colony counts were performed and lung tissue bacterial loads were calculated.
As shown in fig. 5, the lung tissue bacterial load of the mice in the AI18 group is significantly lower than that of the PBS group in the blank group, and the treatment effect is equivalent to that of the antimicrobial peptide indicidin in the positive control group. The AI18 has good in vivo antibacterial activity.
Lung tissue from 3 treatment groups and healthy male BALB/c mice (6-8 weeks, 20±2 g) were fixed with 4% paraformaldehyde for 24h, rinsed with running water for about 2h, gradient ethanol dehydrated, xylene clear, paraffin embedded. After the paraffin block is cooled, trimming the paraffin block by using a blade, slicing the paraffin block with the thickness of 5 mu m by using a rotary slicing machine, spreading the tissue in warm water at the temperature of 40 ℃ for flattening, fishing the tissue out on an anti-drop slide glass, and placing the slide glass on a slide baking machine for baking until no water exists, so that the tissue is attached to the slide glass. Dewaxing and rehydration, hematoxylin staining for 5min, running water washing for 5min,1% ethanol hydrochloride differentiation for about 30s, and running water washing for 5min. Blue is reversed in 1% weak ammonia water for 1min, and the water is washed for 5min. Alcoholizing 80% ethanol for 2min, and dyeing in eosin dye solution for 2min. And (5) dehydrating the transparent sealing piece.
The results are shown in FIG. 6, in which the inflammatory cells in the AI18 group were significantly reduced compared to the PBS-treated group, and slightly better than the positive control group, i.e., endolicidin. Compared with the lung tissue of Normal mice (Normal group), the lung tissue of AI18 is not different from the lung tissue after AI18 administration, which indicates that the AI18 has good biological safety.
Claims (9)
1. An antibacterial peptide AI18 is characterized in that the amino acid sequence is shown as SEQ ID NO.1, and the C terminal end of the antibacterial peptide AI is amidated.
2. The use of the antibacterial peptide AI18 of claim 1 for the preparation of a medicament for inhibiting escherichia coli, pseudomonas aeruginosa, acinetobacter baumannii, klebsiella pneumoniae, staphylococcus aureus, propionibacterium acnes or enterococcus faecalis.
3. The use according to claim 2, wherein the minimum inhibitory concentration of the antimicrobial peptide AI18 against e.coli is 8 μg/mL; the minimum antibacterial concentration for pseudomonas aeruginosa is 8 mug/mL; the minimum antibacterial concentration of Acinetobacter baumannii is 8 mug/mL; the minimum antibacterial concentration for klebsiella pneumoniae is 16 mug/mL; the minimum inhibitory concentration for staphylococcus aureus is 32 mug/mL; the minimum antibacterial concentration of propionibacterium acnes is 16 mug/mL; the minimum inhibitory concentration for enterococcus faecalis was 32. Mu.g/mL.
4. The use of the antibacterial peptide AI18 as claimed in claim 1 for the preparation of preservatives, daily chemicals and medical devices with antibacterial action.
5. A biological antibacterial agent, characterized in that the antibacterial component comprises the antibacterial peptide AI18 according to claim 1.
6. A preservative comprising the antibacterial peptide AI18 of claim 1.
7. The preservative according to claim 6, wherein the preservative is a preservative for foods or a preservative for cosmetics.
8. A daily chemical detergent composition comprising the antibacterial peptide AI18 according to claim 1.
9. A medical dressing comprising the antimicrobial peptide AI18 of claim 1.
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