CN115010791B - Antibacterial peptide GW18 and application thereof - Google Patents
Antibacterial peptide GW18 and application thereof Download PDFInfo
- Publication number
- CN115010791B CN115010791B CN202210470151.8A CN202210470151A CN115010791B CN 115010791 B CN115010791 B CN 115010791B CN 202210470151 A CN202210470151 A CN 202210470151A CN 115010791 B CN115010791 B CN 115010791B
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- CN
- China
- Prior art keywords
- polypeptide
- antibacterial
- antimicrobial
- staphylococcus aureus
- acinetobacter baumannii
- Prior art date
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Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/08—Linear peptides containing only normal peptide links having 12 to 20 amino acids
-
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Abstract
The invention provides an antibacterial polypeptide GW18 and application thereof, and relates to the technical field of antibacterial peptides. The amino acid sequence of the antibacterial polypeptide GW18 is shown as SEQ ID NO.1, and the embodiment proves that the antibacterial polypeptide GW18 has a strong antibacterial function and good antibacterial activity on staphylococcus aureus, escherichia coli and acinetobacter baumannii; the antibacterial polypeptide GW18 can directly kill pathogenic bacteria, has obvious functions and quick action; the GW18 has low hemolytic activity, no cytotoxicity and high stability, and can be applied to antibacterial infection medicines or medical products.
Description
Technical Field
The invention belongs to the technical field of antibacterial peptides, and particularly relates to an antibacterial polypeptide GW18 and application thereof.
Background
The host's own natural immune system is an important guarantee against the invasion of external pathogens, and it depends on various immune cells and active small molecular substances to play a role. The antibacterial peptide is an important polypeptide in the active defense system of animals, is encoded by host genes and is widely distributed in various organisms. As an important material basis for the natural immune response, antibacterial peptides can rapidly respond to infection by external bacteria before the initiation of the host's acquired immunity. The natural antibacterial peptide has good solubility in water environment, and can still maintain structural stability and antibacterial activity under extreme temperature conditions and in strong acid and alkali environments. Related studies have shown that the bactericidal mechanism of antibacterial peptides is usually applied to the surface of bacterial cell membranes to cause the membrane to be sunken or to form holes, so that bacterial contents leak out to cause bacterial death, and the antibacterial peptides are adsorbed on the surface of bacterial cell membranes by electrostatic action and then inserted into a hydrophobic region to change the conformation of the membrane, and further cause the ion channels to open ions to leak out for sterilization.
Antibiotics are one of the biggest drug inventions, and the occurrence of the antibiotics saves lives of countless patients, but as the antibiotics are increasingly used, the number of drug-resistant strains is increased, and the selection of drugs for clinical treatment is difficult, so the development of novel antibacterial drugs is urgent. The antibacterial peptide has the characteristics of high sterilization speed, good thermal stability and acid-base stability, and difficulty in generating drug resistance, and has wide application prospect in the aspect of drug development of infection. However, the conventional antibacterial peptide has the defects of side effects such as hemolysis and cytotoxicity, poor in vivo stability and the like, and is difficult to realize clinical application although the conventional antibacterial peptide has biological activity.
Disclosure of Invention
Accordingly, the present invention aims to provide an antibacterial polypeptide GW18 and application thereof, wherein the antibacterial polypeptide GW18 has high antibacterial effect, low hemolytic activity, no cytotoxicity, high stability and good advantage and application prospect.
In order to achieve the above object, the present invention provides the following technical solutions:
the invention provides an antibacterial polypeptide GW18, and the amino acid sequence of the antibacterial polypeptide GW18 is shown as SEQ ID NO. 1.
Preferably, the antimicrobial polypeptide GW18 is a linear polypeptide and is C-terminally amidated.
Preferably, the molecular weight of the antibacterial polypeptide GW18 is 2365.70Da, and the isoelectric point is 6.84.
The invention provides an antibacterial composition, which comprises the antibacterial polypeptide GW18 and auxiliary materials.
Preferably, the auxiliary materials comprise one or more of a filler, a wetting agent, a binding agent, a disintegrating agent, a lubricant and a surfactant.
Preferably, pharmaceutical raw materials comprising one or more of antibiotics, proteins, polypeptides, plant extracts and cytokines are also included.
The invention also provides application of the antibacterial polypeptide GW18 or the antibacterial composition in preparation of medicines for killing bacteria.
Preferably, the bacteria include staphylococcus aureus (Staphylococcus aureus), escherichia coli (Escherichia coli) and acinetobacter baumannii (Acinetobacter baumannii).
The invention also provides application of the antibacterial polypeptide GW18 or the antibacterial composition in preparing medical products for regulating skin microorganisms.
The invention also provides a medical product for regulating skin microorganisms, which comprises the antibacterial polypeptide GW18 or the antibacterial composition.
The beneficial effects are that: the invention provides an antibacterial polypeptide GW18 with an amino acid sequence shown as SEQ ID NO.1, and the embodiment proves that the antibacterial polypeptide GW18 has a strong antibacterial function, and the minimum antibacterial concentrations of a staphylococcus aureus standard strain (Staphylococcus aureus, ATCC 2592), an Escherichia coli standard strain (Escherichia coli, ATCC 25922) and acinetobacter baumannii (Acinetobacter baumannii, ATCC 22933) are respectively 2.38 mug/ml, 4.76 mug/ml and 9.52 mug/ml; the antibacterial polypeptide GW18 can directly kill pathogenic bacteria, has obvious functions and quick action; the GW18 has low hemolytic activity, no cytotoxicity and high stability, and can be applied to antibacterial infection medicines or medical products.
Drawings
Fig. 1 is a graph showing the results of a study on the sterilization kinetics of the antibacterial polypeptide GW18 on acinetobacter baumannii, co: polymyxin, GW: GW18;
FIG. 2 shows the measurement results of the hemolytic activity of the antimicrobial polypeptide GW18 of the present invention;
FIG. 3 shows the results of measurement of cytotoxic activity of the antimicrobial polypeptide GW18 of the present invention;
fig. 4 shows the plasma stability results of the antimicrobial polypeptide GW18 of the present invention.
Detailed Description
The invention provides an antibacterial polypeptide GW18, wherein the amino acid sequence of the antibacterial polypeptide GW18 is shown as SEQ ID NO. 1: gly-Trp-Gly-Ala-Lys-Arg-Trp-Gly-Lys-Arg-Gly-Trp-Lys-Trp-Lys-Arg-His-Trp.
The antibacterial polypeptide GW18 is a linear polypeptide and is amidated at the C terminal, thus the complete sequenceIs Gly-Trp-Gly-Ala-Lys-Arg-Trp-Gly-Lys-Arg-Gly-Trp-Lys-Trp-Lys-Arg-His-Trp-NH 2 Or GWGAKRWGKRGWKWKRHW-NH 2 . The molecular weight of the antibacterial polypeptide is preferably 2365.70Da, which is measured by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MAL DI-TO F); the isoelectric point of the purified polypeptide was determined to be 6.84 by isoelectric focusing.
The method for preparing the antimicrobial polypeptide GW18 is not particularly limited, and preferably includes direct synthesis, prokaryotic expression, eukaryotic expression, etc., and the antimicrobial polypeptide GW18 is prepared by a solid phase synthesis method in the examples, but is not to be construed as being the full scope of the present invention. In the embodiment of the invention, the crude polypeptide is preferably synthesized according TO the sequence solid-phase synthesis method shown in SEQ ID NO.1, then desalted and purified by HPLC reverse phase column chromatography, the purity of the polypeptide is identified until the purity of the polypeptide is not lower than 95%, the molecular weight of the polypeptide is measured by matrix-assisted laser desorption ionization time of flight mass spectrometry (MAL DI-TO F), and the isoelectric point of the purified polypeptide is measured by isoelectric focusing electrophoresis; and finally, determining whether the amino acid sequence structure of the purified polypeptide is consistent with the structure shown in SEQ ID NO.1 by adopting an automatic amino acid sequencer.
The HPLC reversed phase column chromatography desalination and purification method of the invention preferably comprises the following steps: dissolving 0.1mg of a sample to be tested in 1mL of ultrapure water containing 0.1% trifluoroacetic acid, filtering with a 0.45 mu m filter membrane if undissolved impurities exist, wherein a mobile phase A is 0.1% trifluoroacetic acid-water, a mobile phase B is 0.1% trifluoroacetic acid-acetonitrile, and starting to sample after a base line is stable, wherein the sample loading amount is 50 mu L; the chromatographic column is a silica gel alkyl bonding phase C18 column (4.6mm×300mm, colloidal particle size 5 μm, pore size 100A), a binary mobile phase gradient elution system is adopted to perform gradient elution, namely the content of mobile phase B in the eluent is increased from 0% -80% in a linear relation within 30min, the flow rate is 1mL/min, the detection wavelength 215nm, and the detection temperature is 25 ℃. The method for measuring the matrix-assisted laser desorption ionization time-of-flight mass spectrum preferably comprises the following steps of: the purified polypeptide was dissolved in deionized water to prepare a 1. Mu. Mol/mL solution, 10. Mu.L of the solution was mixed with an equal volume of saturated matrix solution (prepared by dissolving. Alpha. -cyano-4-hydroxycinnamic acid in 50% acetonitrile containing 0.1% trifluoroacetic acid to prepare a saturated solution, centrifuging, collecting the supernatant), and the molecular weight was determined to be 2365.70Da. The isoelectric point of the purified polypeptide is 6.84 by isoelectric focusing electrophoresis, and the amino acid sequence structure of the purified polypeptide is determined by adopting an automatic amino acid sequencer, so that the amino acid sequence is identical to the amino acid sequence shown in SEQ ID NO. 1.
The invention provides an antibacterial composition, which comprises the antibacterial polypeptide GW18 and auxiliary materials.
The auxiliary materials preferably comprise one or more of a filler, a wetting agent, a binding agent, a disintegrating agent, a lubricant and a surfactant. The filler of the present invention preferably comprises one or more of starch, powdered sugar, dextrin, lactose, compressible starch, microcrystalline cellulose, calcium sulfate, dibasic calcium phosphate, and mannitol. The humectants and binders of the present invention preferably include one or more of distilled water, ethanol, starch slurry, sodium carboxymethyl cellulose, hydroxypropyl cellulose, methyl cellulose and ethyl cellulose, hydroxypropyl methyl cellulose, gelatin solution, sucrose solution, aqueous or alcoholic solutions of polyvinylpyrrolidone (pVp). The disintegrating agent of the present invention preferably comprises one or more of dry starch, sodium methyl starch, low-substituted hydroxypropyl cellulose, crosslinked polyvinylpyrrolidone and crosslinked sodium carboxymethyl cellulose. The lubricant preferably comprises one or more of magnesium stearate, micro silica gel, talcum powder, hydrogenated vegetable oil, polyethylene glycol and magnesium laurylsulfate. The surfactant of the present invention preferably comprises sodium dodecyl sulfate. The specific selection and proportion of the auxiliary materials are not particularly limited, and conventional selection and proportion can be carried out based on the formulation, the composition and the functions of the antibacterial composition.
Preferably, the antibacterial composition of the present invention further comprises a pharmaceutical raw material, wherein the pharmaceutical raw material preferably comprises one or more of antibiotics, other proteins, other polypeptides, plant extracts and cytokines. The composition preferably comprises a plurality of medicine raw materials with different compositions and different auxiliary materials.
The bacteria of the present invention preferably include Staphylococcus aureus (Staphylococcus aureus), escherichia coli (Escherichia coli) and Acinetobacter baumannii (Acinetobacter. Baumannii). In the embodiment of the invention, the minimum inhibitory concentration of the antibacterial polypeptide GW18 on the standard strains of a plurality of bacteria is verified, and the minimum inhibitory concentrations of the antibacterial polypeptide GW18 on the standard strains of staphylococcus aureus (Staphylococcus aureus ATCC 2592), the standard strains of escherichia coli (Escherichia coliATCC 25922) and acinetobacter baumannii (Acinetobacter baumanniiATCC 22933) are respectively 2.38 mug/ml, 4.76 mug/ml and 9.52 mug/ml. The invention also proves that the antibacterial polypeptide GW18 has stronger bacteriostasis effect on more colistin E, the polypeptide GW18 can sterilize rapidly, the obvious bacteriostasis can be shown in 10min at the time of 1 xMIC (9.52 mu g/ml), the growth of Acinetobacter baumannii is almost avoided after the GW18 acts for 1min at the concentration of 5 xMIC and 10 xMIC, the effect of the GW18 on bacteria is fatal, and the number of the bacteria can not be increased continuously within 3 h.
According to the invention, the hemolytic activity of the antibacterial polypeptide is determined by utilizing a method of co-incubating erythrocytes and the antibacterial polypeptide GW18, and according to the determination, the hemolytic activity of the GW18 is lower even if the concentration of the antibacterial polypeptide GW18 reaches 320 mug/ml. The invention also utilizes the human embryo kidney cell strain HEK293T to measure the cytotoxicity of the antibacterial polypeptide GW18, and even when the concentration of the antibacterial polypeptide GW18 reaches 200 mug/ml, the antibacterial polypeptide GW18 does not show cytotoxicity. The antibacterial activity can still be detected by incubating the antibacterial polypeptide GW18 with serum for more than 10 hours, which indicates that the antibacterial polypeptide GW18 has stable antibacterial performance, and can be applied to preparing medicines with sterilizing function or medical and aesthetic products for regulating skin microorganisms.
The invention also provides application of the antibacterial polypeptide GW18 or the antibacterial composition in preparation of medicines for killing bacteria.
The dosage form of the pharmaceutical product is not particularly limited in the present invention, and the application is preferably the same as that described above, and will not be described here again.
The invention also provides application of the antibacterial polypeptide GW18 or the antibacterial composition in preparing medical products for regulating skin microorganisms.
The type of the medical product is not particularly limited in the present invention, and preferably includes application, cleansing and/or mask, etc.
The invention also provides a medical product for regulating skin microorganisms, which comprises the antibacterial polypeptide GW18 or the antibacterial composition.
The medical product of the present invention is preferably the same as described above, and will not be described in detail herein.
The antibacterial polypeptide GW18 and its application provided in the present invention will be described in detail with reference to examples, but they should not be construed as limiting the scope of the present invention.
Example 1
Solid phase synthesis of antibacterial polypeptide GW18
1. According to the designed amino acid sequence: gly-Trp-Gly-Ala-Lys-Arg-Trp-Gly-Lys-Arg-Gly-Trp-Lys-Trp-Lys-Arg-His-Trp-NH 2 Synthesizing to obtain crude polypeptide by solid phase synthesis;
2. desalting and purifying the crude polypeptide by HPLC reversed phase column chromatography, and identifying the purity until the purity of the polypeptide is not lower than 95%;
HPLC purification and identification method: dissolving 0.1mg of a sample to be tested in 1mL of ultrapure water containing 0.1% trifluoroacetic acid, filtering with a 0.45 mu m filter membrane if undissolved impurities exist, wherein a mobile phase A is 0.1% trifluoroacetic acid-water, a mobile phase B is 0.1% trifluoroacetic acid-acetonitrile, and starting to sample after a base line is stable, wherein the sample loading amount is 50 mu L; the chromatographic column is a silica gel alkyl bonding phase C18 column (4.6mm×300mm, colloidal particle size 5 μm, pore size 100A), a binary mobile phase gradient elution system is adopted to perform gradient elution, namely the content of mobile phase B in the eluent is increased from 0% -80% in a linear relation within 30min, the flow rate is 1mL/min, the detection wavelength 215nm, and the detection temperature is 25 ℃.
3. The molecular weight of the sample is 2365.70Da by the determination of matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TO F);
the method comprises the following steps: the purified polypeptide was dissolved in deionized water to prepare a 1. Mu. Mol/mL solution, and 10. Mu.L of the solution was mixed with an equal volume of saturated matrix solution (prepared by dissolving α -cyano-4-hydroxycinnamic acid in 50% acetonitrile containing 0.1% trifluoroacetic acid, and then subjecting the mixture to centrifugation, and collecting the supernatant).
4. The isoelectric point of the purified polypeptide is 6.84 by isoelectric focusing electrophoresis, and the amino acid sequence structure of the purified polypeptide is determined by an automatic amino acid sequencer, and the polypeptide is determined to be Gly-Trp-Gly-Ala-Lys-Arg-Trp-Gly-Lys-Arg-Gly-Trp-Lys-Arg-His-Trp.
Example 2
Antibacterial Activity of antibacterial polypeptide GW18 prepared in example 1
The experiment adopts a two-fold gradient dilution method, and the minimum inhibitory concentration, namely the minimum drug concentration capable of inhibiting the growth and reproduction of bacteria, is measured.
1. MIC value determination
The specific experimental operation is as follows: preparing fresh bacterial liquid, and detecting OD of the bacterial liquid by using an ultraviolet spectrophotometer 600 According to 1OD 600 ＝1×10 9 CFU/ml, diluting the bacterial liquid concentration to 2X 10 with fresh LB liquid culture medium 5 CFU/ml. Then 100 μl of physiological saline is added into the sterile 96-well plate in advance, the sample to be tested is added into the first well, the sample to be tested is subjected to double gradient dilution in sequence, and 100 μl of 2×10 concentration is added into each well 5 And (3) blowing and mixing CFU/ml bacterial liquid by using a pipetting gun, placing the mixed bacterial liquid in a constant-temperature incubator at 37 ℃ for overnight culture, and finally detecting the light absorption value of the bacterial liquid at 600nm by using an enzyme-labeling instrument to detect the average value of the sample concentrations of a hole where bacteria cannot grow and an adjacent hole as the minimum inhibitory concentration, namely the MIC value. The antibacterial activity of the antibacterial polypeptide GW18 is shown in Table 1, and the minimum antibacterial concentrations of the antibacterial polypeptide GW18 to staphylococcus aureus standard strain (Staphylococcus aureus ATCC 2592), escherichia coli standard strain (Escherichia coliATCC 25922) and acinetobacter baumannii (Acinetobacter baumanniiATCC 22933) are respectively 2.38 mug/ml, 4.76 mug/ml and 9.52 mug/ml.
2. Inhibition of bacterial reproduction performance assay
Preparing fresh Acinetobacter baumannii bacterial solution, and diluting and adjusting concentrationUp to 1X 10 6 CFU/mL. And adding a sample to be tested into the bacterial liquid, wherein the positive control is polymyxin E, the negative control is physiological saline, the final concentrations of the polymyxin E and the GW18 are respectively 1 xMIC, 5 xMIC and 10 xMIC, the MIC value of the polymyxin E is 1.17 mug/ml, and the MIC value of the GW18 is 9.52 mug/ml. Rapidly placing the bacterial liquid added with the sample into a constant temperature incubator at 37 ℃, carrying out shaking culture at 160rpm, taking 10 mu l of bacterial liquid from each point at 6 time points of 0min, 1min, 10min, 30min, 1h, 3h and the like, diluting 100 times with sterile normal saline, then taking 100 mu l of bacterial liquid to coat on LB solid medium, placing a flat plate into the constant temperature incubator at 37 ℃ for inversion culture for 16h, and then carrying out colony counting.
The results are shown in FIG. 1: the polypeptide GW18 can sterilize rapidly, and can show obvious sterilization effect within 10min at 1 xMIC (9.52 mu g/ml), and at 5 xMIC and 10 xMIC concentration, the growth of Acinetobacter baumannii is almost avoided after the GW18 acts for 1min, meanwhile, the effect of the GW18 on bacteria is fatal, and the number of the bacteria can not be increased continuously within 3 h. In contrast, polymyxin E at a concentration of 1 XMIC (1.17. Mu.g/ml) still grew with Acinetobacter baumannii at 10min, and bacteria at a concentration of 5 XMIC at 1 min.
Example 3
The antibacterial polypeptide GW18 described in example 1 has no hemolytic activity and cytotoxicity
1. Determination of haemolytic Activity
Diluting the washed red blood cells with physiological saline to 10 7 -10 8 Simultaneously preparing samples to be tested into different gradient concentrations, placing the samples and the samples at a constant temperature of 37 ℃ for co-incubation for 30min, centrifuging at 1000rpm for 5min, and detecting the light absorption value of the supernatant at 540nm by using an enzyme-labeling instrument. In this experiment, physiological saline was used as a negative control, the same volume of Triton X-100 (10%) was used as a positive control, and the hemolytic activity was proportional to the light absorption at 540 nm.
As shown in FIG. 2, GW18 hemolytic activity was low even at a concentration of 320. Mu.g/ml.
2. Cytotoxicity assays
Cytotoxicity was determined using the human embryonic kidney cell line HEK 293T. To be treatedDiscarding the culture medium when the cell growth state is good and the density is 80% of the bottle bottom, washing with sterile PBS for 3 times, then digesting the adherent cells with pancreatin, adding fresh DMEM culture medium containing 10% FBS after stopping, blowing and mixing, and adjusting the cell suspension concentration to 5×10 5 Each ml was subjected to an experiment using a sterile 96-well plate, 200. Mu.l of the above cell suspension was added to each well, and the mixture was placed in a cell incubator for overnight culture. The next day, samples to be tested were added at different concentrations, the concentration gradients were set at 7.25. Mu.g/ml, 12.5. Mu.g/ml, 25. Mu.g/ml, 50. Mu.g/ml, 100. Mu.g/ml, 200. Mu.g/ml, 3 replicates each, the control group was sterilized with the same volume of PBS, and then placed at 37℃with 5% CO 2 The culture was continued for 24 hours in a constant temperature incubator. 10. Mu.l of MTT solution (5 mg/ml) was added to each well, and the mixture was placed in an incubator under dark conditions for 4 hours. Finally, the wells were carefully aspirated and discarded, DMSO (dimethyl sulfoxide) μl was added, the 96-well plates were placed on a shaker and slowly shaken for 10 minutes to dissolve the crystals, and the absorbance of each well at 490nm was measured using an microplate reader. The results are shown in FIG. 3, wherein the antimicrobial polypeptide GW18 is non-cytotoxic.
Example 4
Stability of the antimicrobial polypeptide GW18 described in the examples
10mL of human blood is obtained by a sterile syringe and stored in an anticoagulant tube, and centrifuged at 3500rpm at 4℃for 30min, and the yellow supernatant is carefully aspirated to obtain the desired plasma. The above plasma was diluted twice with sterile physiological saline, and the antibacterial polypeptide GW18 was added thereto, controlling the final concentration of the antibacterial polypeptide GW18 to 10mg/ml. Subsequently, the plasma in which the antibacterial polypeptide GW18 was dissolved was placed in a constant temperature incubator at 37℃for incubation, 10. Mu.l each was taken at 8 time points of 0, 1, 2, 3, 6, 10, 12, 24 hours, etc., and the antibacterial activity against Acinetobacter baumannii was detected by the inhibition zone method after the incubation of the antibacterial polypeptide GW18 with the plasma, and two replicates were set for each time point. As a result, as shown in FIG. 4, the antibacterial activity of the antibacterial polypeptide GW18 was still detectable after incubation with serum for more than 10 hours.
The results of the combination of the embodiments 2 to 4 show that the antibacterial polypeptide GW18 can directly kill pathogenic bacteria, has obvious functions and quick action; the antibacterial polypeptide GW18 has low hemolytic activity, no cytotoxicity and high stability, and can be applied to antibacterial infection medicines or medical products.
The foregoing is merely a preferred embodiment of the present invention and it should be noted that modifications and adaptations to those skilled in the art may be made without departing from the principles of the present invention, which are intended to be comprehended within the scope of the present invention.
Sequence listing
<110> laboratory of southern ocean science and engineering Guangdong province (Guangzhou)
<120> an antibacterial peptide GW18 and its application
<160> 1
<170> SIPOSequenceListing 1.0
<210> 1
<211> 18
<212> PRT
<213> Artificial sequence (Artificial Sequence)
<400> 1
Gly Trp Gly Ala Lys Arg Trp Gly Lys Arg Gly Trp Lys Trp Lys Arg
1 5 10 15
His Trp
Claims (8)
1. An antibacterial polypeptide GW18, which is characterized in that the amino acid sequence of the antibacterial polypeptide GW18 is shown as SEQ ID NO. 1.
2. The antimicrobial polypeptide GW18 of claim 1 wherein the antimicrobial polypeptide GW18 is a linear polypeptide and C-terminally amidated.
3. An antimicrobial composition comprising the antimicrobial polypeptide GW18 of claim 2 and an adjuvant.
4. The antimicrobial composition of claim 3, wherein the adjuvant comprises one or more of a filler, a wetting agent, a binder, a disintegrant, a lubricant, and a surfactant.
5. The antimicrobial composition of claim 3, further comprising a pharmaceutical raw material comprising one or more of antibiotics, proteins, polypeptides, plant extracts, and cytokines.
6. Use of the antimicrobial polypeptide GW18 of claim 2 or the antimicrobial composition of any of claims 3-5 in the preparation of a medicament for killing bacteria;
the bacteria are staphylococcus aureus, escherichia coli and acinetobacter baumannii.
7. Use of the antimicrobial polypeptide GW18 of claim 2 or the antimicrobial composition of any of claims 3-5 in the preparation of a medical product for modulating skin microorganisms;
the skin microorganism is staphylococcus aureus, escherichia coli and acinetobacter baumannii.
8. A medical product for regulating skin microorganisms, comprising the antimicrobial polypeptide GW18 of claim 2 or the antimicrobial composition of any of claims 3-5;
the skin microorganism is staphylococcus aureus, escherichia coli and acinetobacter baumannii.
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| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6040291A (en) * | 1998-03-25 | 2000-03-21 | Seikagaku Corporation | Antimicrobial peptide |
| CN113754784A (en) * | 2021-09-27 | 2021-12-07 | 中国农业大学 | Cell-penetrating antibacterial peptide and application thereof |
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| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6040291A (en) * | 1998-03-25 | 2000-03-21 | Seikagaku Corporation | Antimicrobial peptide |
| CN113754784A (en) * | 2021-09-27 | 2021-12-07 | 中国农业大学 | Cell-penetrating antibacterial peptide and application thereof |
Non-Patent Citations (2)
| Title |
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| A designed antimicrobial peptide with potential ability against methicillin resistant Staphylococcus aureus;Bingqian Yuan et al;Front. Microbiol.;第13卷;全文 * |
| 基因工程表达内含肽介导的抗菌肽MME及其酰胺化;叶若柏等;福建农业学报;全文 * |
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