CN114349826A - Antibacterial peptide CGS7 and preparation method and application thereof - Google Patents
Antibacterial peptide CGS7 and preparation method and application thereof Download PDFInfo
- Publication number
- CN114349826A CN114349826A CN202210133652.7A CN202210133652A CN114349826A CN 114349826 A CN114349826 A CN 114349826A CN 202210133652 A CN202210133652 A CN 202210133652A CN 114349826 A CN114349826 A CN 114349826A
- Authority
- CN
- China
- Prior art keywords
- cgs7
- antibacterial peptide
- arg
- peptide
- antibacterial
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Granted
Links
Classifications
-
- 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
Landscapes
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
Abstract
An antibacterial peptide CGS7, wherein the antibacterial peptide CGS7 is an artificially synthesized non-natural peptide which consists of 16 amino acid residues, the molecular weight is 2038.51Da, the net charge number is +6, the isoelectric point is 12.70, and the amino acid sequence is Leu-Ala-Arg-Val-Ile-Arg-Phe‑Ile‑Arg‑Arg‑Ala‑Trp‑NH2. The antibacterial peptide CGS7 has the advantages of small molecular weight, simple artificial synthesis, low hemolytic activity and remarkable antibacterial effect, particularly plays a strong inhibiting effect on staphylococcus aureus and methicillin-resistant staphylococcus aureus, and has wide application prospect.
Description
Technical Field
The invention belongs to the technical field of biochemistry, and particularly relates to preparation of antibacterial peptide CGS7 and application of the antibacterial peptide in preparation of antibacterial drugs.
Background
The antibacterial peptide is a kind of antimicrobial and some malignant cell short peptide produced in the defense process of organism against pathogenic microorganism. It is an important component of the innate immune system of the body and has a broad inhibitory effect on bacteria, fungi, parasites, viruses, tumor cells and the like. The natural antibacterial peptide is a micromolecular cationic polypeptide consisting of 12-60 amino acids, is rich in basic amino acids such as lysine, arginine, histidine and the like, generally has 2-8 positive charges, has an isoelectric point more than 7 and shows stronger cationic characteristics.
The antibacterial peptide is found to be widely present in different types of organisms, such as immune cells, phagocytic cells and mucosal epithelial cells of animals and plants. The antibacterial mechanism of the antibacterial peptide is complex, and an important action mechanism is that the antibacterial peptide can be well combined with an electronegative cell membrane consisting of amphoteric molecules, which is the structural basis of the interaction between the antibacterial peptide and the cell membrane, so that the membrane permeability is changed, or pores are formed on the lipid membrane, and important contents leak out to die. In addition, researches show that the antibacterial peptide not only can play a role in sterilization by changing the permeability of bacterial cell membranes, but also can be combined with target proteins of bacteria, so that the expression of bacterial biofilms and genes related to virulence factors is reduced, the formation of the bacterial biofilms is inhibited, the inflammatory reaction caused by the virulence factors is reduced, and the antibacterial effect is played in multiple ways. Therefore, the efficiency of antibacterial peptides in killing bacteria is much higher than that of conventional antibiotics.
At present, various antibacterial peptides are found in organisms such as insects, fishes, mammals, amphibians and plants. With the further understanding of the antibacterial mechanism of the antibacterial peptide and the discovery of new antibacterial peptide, the natural antibacterial peptide can be directly obtained by separation and purification from the organism, and the natural or non-natural antibacterial peptide can be synthesized in a large amount in a short time by utilizing genetic engineering and chemical synthesis methods. In recent years, scientists have also begun to modify the existing natural antibacterial peptides while searching for novel antibacterial peptides in order to obtain antibacterial peptides with higher antibacterial activity, lower toxic and side effects and more pertinence.
By aligning with 3257 antibacterial peptide sequences in the APD (antimicrobial peptide) database, no complete repeat with CGS7 sequence was found. The antimicrobial peptide with the highest similarity to CGS7 was UCLL1 (RPILIRVRRIRVI) with a similarity of 42.1%, reported to UCLL1 for the beneficial bacterium Bacillus subtilisBacillus subtilis168 has good effect (MIC 9.70 μ M) on Escherichia coliEscherichia coli MG1655 also had a weak bacteriostatic effect (MIC 77.10. mu.M).
Disclosure of Invention
The invention aims to provide a novel antibacterial peptide CGS7 with medicinal value and a preparation method thereof.
The invention also aims to provide application of the antibacterial peptide in preparation of a methicillin-resistant staphylococcus aureus medicament, an external dressing or mouthwash.
An antibacterial peptide CGS7, wherein the amino acid sequence of the antibacterial peptide CGS7 is as follows: Leu-Ala-Arg-Val-Ala-Arg-Arg-Val-Ile-Arg-Phe-Ile-Arg-Arg-Ala-Trp-NH2
(leucine-alanine-arginine-valine-alanine-arginine-valine-isoleucine-arginine-phenylalanine-isoleucine-arginine-alanine-tryptophan-NH2）。
The full sequence of the antibacterial peptide CGS7 is amidated at the C-terminal.
The scheme is characterized in that the antibacterial peptide CGS7 comprises 16 amino acid residues, the molecular weight is 2038.51Da, the net charge number is +6, and the isoelectric point is 12.70.
According to the amino acid sequence, the full sequence of the antibacterial peptide CGS7 is synthesized by an automatic polypeptide synthesizer, and is desalted and purified by HPLC reverse phase column chromatography.
An application of the antibacterial peptide CGS7 is to prepare a methicillin-resistant staphylococcus aureus medicament or an external dressing or mouthwash.
The invention has the beneficial effects that: antimicrobial peptide CGS7 for staphylococcus aureusStaphylococcus aureus(S. Aureus) And drug-resistant Staphylococcus aureus (methicillin-resistant)Staphylococcus aureusMRSA) has stronger bacteriostatic action (MIC 3.06 mu M), and has weak hemolysis and low cytotoxicity, which shows that the antimicrobial peptide CGS7 has good antimicrobial selectivity and low toxic and side effects. In a mouse wound infection model, the antibacterial peptide CGS7 shows good epidermal antibacterial activity and has no obvious toxic reaction. The antibacterial peptide CGS7 can affect the integrity of bacterial cell membranes, and is combined with formate-tetrahydrofolate ligase (binding constant Kd2.24 mu M) in the drug-resistant staphylococcus aureus, so that the formation of a staphylococcus aureus biofilm is regulated, the expression of genes related to bacterial virulence factors is regulated, and the antibacterial effect is exerted in multiple ways. The antibacterial peptides with the similar sequence to the antibacterial peptide CGS7 have no report of a dual-function antibacterial mechanism. The antibacterial peptide CGS7 is artificially synthesized, has the advantages of small molecular weight, convenient artificial synthesis, strong bactericidal action and the like, and in addition, the antibacterial peptide CGS7 is synthesized artificiallyCGS7 is also characterized by very low hemolytic activity and eukaryotic cytotoxicity.
Detailed Description
The present invention will be better understood from the following examples. However, those skilled in the art will readily appreciate that the description of the embodiments is only for illustrating the present invention and should not be taken as limiting the invention as detailed in the claims.
Example 1: preparation of antibacterial peptide CGS7
I, chemical synthesis method of antibacterial peptide CGS 7: the full sequence was synthesized from the corresponding L-amino acid (available from Merck Sigma) and an automated polypeptide synthesizer (433A, applied biosystems, USA) based on the amino acid sequence described in the summary. The extract was purified by desalting by HPLC reverse phase column (WelchXB C184.6X 150 mm) chromatography with pure water (0.1% trifluoroacetic acid) -60% acetonitrile (0.1% trifluoroacetic acid) as mobile phase at a flow rate of 1mL/min and detection at a wavelength of 220nm, and the eluted peak was collected and lyophilized. The L-amino acid does not need to be preserved.
And II, identifying the molecular weight of the synthesized antibacterial peptide CGS7 by using electrospray mass spectrometry. Sample introduction is carried out by using a liquid phase system, and the mobile phase is 50% H2O/50% ACN, flow rate of 0.2mL/min, flow rate of protective gas of 1.5L/min, and collision energy of 4.5 kV.
III, the purity of the purified antibacterial peptide CGS7 is identified by a high performance liquid chromatography HPLC method (Welch XB C184.6 multiplied by 250 mm), the molecular weight is measured by electrospray mass spectrometry, the isoelectric point is measured by isoelectric focusing electrophoresis, and the amino acid sequence structure is measured by an automatic amino acid sequencer.
HPLC is a single symmetrical peak.
Identifying by electrospray mass spectrometry: the molecular weight of the antibacterial peptide CGS7 is 2038.51 Da.
Through HPLC and mass spectrum identification, the antibacterial peptide CGS7 comprises 16 amino acid residues, the molecular weight is 2038.51Da, the net charge number is +6, the isoelectric point is 12.70, and the complete sequence is as follows:
Leu-Ala-Arg-Val-Ala-Arg-Arg-Val-Ile-Arg-Phe-Ile-Arg-Arg-Ala-Trp-NH2. The full sequence of the antibacterial peptide CGS7 is amidated at the C-terminal.
(leucine-alanine)-arginine-valine-alanine-arginine-valine-isoleucine-arginine-phenylalanine-isoleucine-arginine-alanine-tryptophan-NH2）。
Example 2: antibacterial experiment of antibacterial peptide CGS7
Minimum Inhibitory Concentration (MIC): the lowest sample concentration at which no bacterial growth was detected. A double dilution method is adopted, and the specific method is as follows:
the bacteria were inoculated on Luria-Bertani (LB) solid medium and cultured in an inverted state in an incubator at 37 ℃. After the bacterial colony grows out, a single bacterial colony is picked by an inoculating loop and transferred into an LB liquid culture medium, and the single bacterial colony is shake-cultured in a 37 ℃ incubator to logarithmic phase. Detecting bacterial liquid OD on ultraviolet spectrophotometer600According to OD600=1×108CFU/ml bacterial liquid diluted to 2X 10 with liquid LB medium5CFU/ml. Adding 100 microliter LB liquid culture medium into each hole of a sterile 96-hole plate in advance, then adding 100 microliter of antibacterial peptide sample which is diluted to a certain concentration and is subjected to filtration sterilization by a 0.22-micrometer microporous membrane into the first hole, uniformly mixing, adding 100 microliter into the 2 nd hole, sequentially diluting by multiple times, sucking 100 microliter from the 12 th hole, and discarding until a sample with double concentration gradient is prepared.
Adding 100 mu L of diluted bacterial liquid into each hole, mixing uniformly, culturing for 16h at 37 ℃ by slow shaking, and measuring the light absorption value at 600 nm. And (4) calculating a result: the average value of the sum of the concentrations of the samples in the wells in which no bacterial growth was detected and the wells adjacent thereto in which bacterial growth was present was taken as the minimum inhibitory concentration of the sample.
Table 1 is a table of the antimicrobial activity test data for antimicrobial peptide CGS 7. Wherein CGS7 MIC: namely the minimum inhibitory concentration of the antimicrobial peptide CGS7, and the result is the average value of three independent repeated experiments.
As can be seen from Table 1, the antimicrobial peptide CGS7 has very strong inhibitory effect on tested strains, for example, the minimum MIC value of Staphylococcus aureus and methicillin-resistant Staphylococcus aureus can reach 6.25 μ g/mL (3.06 μ M), which indicates that the antimicrobial peptide CGS7 can inhibit the growth of Staphylococcus under very low concentration.
Example 3: hemolytic activity assay of antimicrobial peptide CGS7
Blood is collected from the heart of a mouse, collected blood is mixed with Ash Solution (Alsever Solution, 8.0g of sodium citrate, 0.55g of citric acid, 20.5g of glucose and 4.2g of sodium chloride, deionized water is added to 1L, the pH is adjusted to 6.1, the mixture is stored at 4 ℃ after autoclaving) according to the proportion of 1:1 and is placed in a centrifuge tube, the centrifuge tube is centrifuged at 1000rpm for 5min, and normal saline is washed until the supernatant is no longer red. Diluting the washed red blood cells with physiological saline to 108Suspension of concentration. The diluted erythrocyte suspension and samples with different concentrations dissolved in normal saline are insulated at 37 ℃ for 30min, then centrifuged at 1000rpm for 5min, and the supernatant is measured for the absorption value at 540 nm. Physiological saline was used as a negative control, and Triton X-100 was used as a positive control. Hemolytic activity is proportional to the 540nm absorbance.
The antimicrobial peptide CGS7 did not cause hemolysis in the mouse blood even at a high concentration of 320. mu.g/mL.
Example 4: cytotoxicity test of antimicrobial peptide CGS7
Human normal cell embryonic kidney HEK293 cells were cultured in Du's modified (DMEM) medium containing 10% fetal bovine serum and diabodies (100U/mL each for penicillin and streptomycin) to log phase, washed three times with PBS buffer, digested with 0.25% trypsin, suspended in fresh DMEM medium, and cell density adjusted to 1X 106After the cells are attached to the plate, samples with different concentrations are added to the plate in a volume of 200. mu.L per well, and the plate is co-cultured for 24 hours at 37 ℃ under 5% carbon dioxide, after the culture is finished, 20. mu.L of 5mg/mL MTT (3- (4,5-dimethyl-2-thiazolyl) -2, 5-diphenyl-2-H-tetrazolium bromide) solution (prepared by cell culture PBS (Phosphate Buffer saline) Buffer solution) is added to each well of the 96-well cell culture plate, the plate is continuously cultured for 4 hours, the liquid in the wells is sucked by a pipette gun, 100. mu.L of dimethyl sulfoxide (DMSO) is added to each well, the plate is gently shaken for 10 minutes at room temperature, and the light absorption at 490nm wavelength is detected by a microplate reader.
The antimicrobial peptide CGS7 exhibited a very low cytotoxic effect of about 10% on human normal cell embryonic kidney HEK293 cells even at a concentration of 1000. mu.g/mL.
Example 5: effect of antimicrobial peptide CGS7 on wound infection
Injecting bacterial liquid into the skin of the back to carry out subcutaneous infection molding. Blank group (blank) is a normal non-molding group, MRSA is a molding group, MRSA + CGS7 group is a CGS7 injected immediately after the molding of the subcutaneous injection bacterial liquid for treatment, MRSA + Vancomycin group is Vancomycin injected immediately after the molding of the subcutaneous injection bacterial liquid for treatment, MRSA + Methicillin group is Methicillin injected immediately after the molding of the subcutaneous injection bacterial liquid for treatment, and the subcutaneous infection conditions of each group are observed after 7 days. Most of the CGS7 treatment groups had no abscess and the effect was comparable to that of the vancomycin group. Obvious abscess infection can be seen subcutaneously in MRSA model building groups and methicillin treatment groups.
Example 6: application of antibacterial peptide CGS7 in mouthwash
The preferred antibacterial peptide-containing mouth wash composition (mass percent): 18% of propylene glycol, 0.3% of aspartame, 15% of edible alcohol, 0.8% of sodium monofluorophosphate, 3% of antibacterial peptide, 1% of essence and the balance of deionized water.
The preparation method of the mouthwash comprises the following steps:
(1) adding the humectant, the sweetener, the anticarious agent and the edible alcohol into deionized water, stirring and forming uniformly dispersed clear liquid;
(2) dissolving antibacterial peptide CGS7 in essence;
(3) adding essence containing antibacterial peptide into water soluble clear solution under stirring, and stirring for 15-25 min;
(4) after all the materials are uniformly mixed, stopping stirring, standing and filtering;
(5) and (5) performing sterile treatment to obtain a finished product.
The results show that the mouthwash can effectively inhibit the propagation of microorganisms such as bacteria and fungi in the oral cavity.
Example 7: application of antibacterial peptide CGS7 in skin health care
The skin health-care composition containing the antibacterial peptide comprises the following components in percentage by mass: NaH2PO4·2H2O 0.05%，Na2HPO4·12H20.82% of O, 0.18% of propylene glycol, 0.18% of lanolin alcohol, 4.0% of xylitol-based glucoside, 2.2% of mannitol erythritol, 2.6% of dehydrated xylitol, 0.02% of antibacterial peptide, 1.8% of sodium polyacrylate and the balance of deionized water.
The preparation method of the skin health care composition comprises the following steps:
(1) reacting NaH with2PO4·2H2O、Na2HPO4·12H2Dissolving O, propylene glycol and lanolin alcohol in deionized water, stirring at 80-90 deg.C for 15-20 min, and cooling to 55 deg.C.
(2) Adding xylitol-based glucoside, mannitol erythritol, anhydroxylitol, antibacterial peptide CGS7, and sodium polyacrylate into the above mixture, and stirring for 30 min.
(3) Filtering and sterilizing the composition to obtain a finished product.
The result shows that the skin health care composition has the effects of bacteriostasis, inflammation diminishing and acne removing.
Example 8: application of antibacterial peptide CGS7 in scar repair medicine
50 male rats with a body weight of about 250g were selected. An open circular wound of 2cm diameter was made on the back of the rat, with a full-thickness skin defect, deep in the myofascial layer. The normal skin control group was not treated after topical depilation. The rats were randomly grouped into 10 rats each; the antibacterial peptide is respectively smeared on the wound surface by cotton swabs at the concentration of 2mg/L, 4mg/L, 6mg/L and 8mg/L, and is smeared twice every day. The chitosan antibacterial patch group is a control group.
And on 28 days after the model is made, covering the wound surface with a polyester projection film, marking the area of the wound surface, and calculating the area of the wound surface on a calculation paper to be used as the area of the scar after healing. The results showed that the average scar area of the control group was 20.21 mm2The scar areas of different antibacterial peptide experimental groups are smaller than those of the control group, and the average scar area is the smallest under the antibacterial peptide concentration of 8mg/L and is 9.71 mm2The antibacterial peptide is proved to have the function of reducing the scar formation.
In conclusion, the antibacterial peptide CGS7 has the advantages of small molecular weight, simplicity in artificial synthesis, high efficiency in killing methicillin-resistant staphylococcus aureus and low hemolytic activity, and the antibacterial peptide CGS7 and the composition containing the CGS7 can be used as antibacterial drugs and can also be applied to the fields of health products, mouthwash and the like.
Sequence listing
<110> institute of biological research of academy of sciences of Shandong province
<120> antibacterial peptide CGS7, and preparation method and application thereof
<160> 1
<170> SIPOSequenceListing 1.0
<210> 1
<211> 16
<212> PRT
<213> Artificial Sequence (Artificial Sequence)
<220>
<221> AMIDATION
<222> (1)..(16)
<223> C-terminal amidation of the complete sequence of antimicrobial peptide CGS7
<400> 1
Leu Ala Arg Val Ala Arg Arg Val Ile Arg Phe Ile Arg Arg Ala Trp
1 5 10 15
Claims (4)
1. The antibacterial peptide CGS7 is characterized in that the amino acid sequence of the antibacterial peptide CGS7 is as follows: Leu-Ala-Arg-Val-Ala-Arg-Arg-Val-Ile-Arg-Phe-Ile-Arg-Arg-Ala-Trp-NH2。
2. The antimicrobial peptide CGS7, according to claim 1, comprising 16 amino acid residues, having a molecular weight of 2038.51Da, a net charge number of +6, and an isoelectric point of 12.70.
3. The method for preparing the antibacterial peptide CGS7 as claimed in claim 1, wherein the full sequence of the antibacterial peptide CGS7 is synthesized by an automatic polypeptide synthesizer according to the amino acid sequence, and desalted and purified by HPLC reverse phase column chromatography.
4. The use of the antimicrobial peptide CGS7 as claimed in claim 1 in the preparation of a methicillin-resistant Staphylococcus aureus resistant drug, a topical dressing or a mouthwash.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202210133652.7A CN114349826B (en) | 2022-02-14 | 2022-02-14 | Antibacterial peptide CGS7 and preparation method and application thereof |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202210133652.7A CN114349826B (en) | 2022-02-14 | 2022-02-14 | Antibacterial peptide CGS7 and preparation method and application thereof |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN114349826A true CN114349826A (en) | 2022-04-15 |
| CN114349826B CN114349826B (en) | 2023-05-30 |
Family
ID=81094045
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN202210133652.7A Active CN114349826B (en) | 2022-02-14 | 2022-02-14 | Antibacterial peptide CGS7 and preparation method and application thereof |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN114349826B (en) |
Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2001060162A2 (en) * | 2000-02-15 | 2001-08-23 | Ohio University | Cationic, amphipathic beta-sheet peptides and uses thereof |
| US6342581B1 (en) * | 1997-07-08 | 2002-01-29 | Human Genome Sciences, Inc. | Secreted protein HLHFP03 |
| US20020169279A1 (en) * | 2001-02-16 | 2002-11-14 | Montelaro Ronald C. | Virus derived antimicrobial peptides |
| CN110156875A (en) * | 2019-05-21 | 2019-08-23 | 山东省科学院生物研究所 | Antibacterial peptide H5-p5 and its preparation method and application |
| CN112724198A (en) * | 2019-10-28 | 2021-04-30 | 于荣敏 | Methicillin-resistant staphylococcus aureus-resistant antibacterial peptide and preparation method and application thereof |
-
2022
- 2022-02-14 CN CN202210133652.7A patent/CN114349826B/en active Active
Patent Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6342581B1 (en) * | 1997-07-08 | 2002-01-29 | Human Genome Sciences, Inc. | Secreted protein HLHFP03 |
| WO2001060162A2 (en) * | 2000-02-15 | 2001-08-23 | Ohio University | Cationic, amphipathic beta-sheet peptides and uses thereof |
| US20020169279A1 (en) * | 2001-02-16 | 2002-11-14 | Montelaro Ronald C. | Virus derived antimicrobial peptides |
| CN110156875A (en) * | 2019-05-21 | 2019-08-23 | 山东省科学院生物研究所 | Antibacterial peptide H5-p5 and its preparation method and application |
| CN112724198A (en) * | 2019-10-28 | 2021-04-30 | 于荣敏 | Methicillin-resistant staphylococcus aureus-resistant antibacterial peptide and preparation method and application thereof |
Non-Patent Citations (1)
| Title |
|---|
| XIONG,F.等: "Effects of the antimicrobial peptide L12 against multidrug‑resistant Staphylococcus aureus", MOLECULAR MEDICINE REPORTS * |
Also Published As
| Publication number | Publication date |
|---|---|
| CN114349826B (en) | 2023-05-30 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| RU2571924C2 (en) | Method and substance for site-activated complex-formation of biological molecules | |
| CN106188265B (en) | A kind of antimicrobial peptide Cm-CATH2 and its gene, preparation method and application | |
| CN101412753A (en) | Bungarus fasciatus antibacterial peptide cathelicidin-BF, and genes and uses thereof | |
| CN102924574B (en) | Antibacterial peptide LZ1 and application of antibacterial peptide in preparation of antibacterial medicament | |
| CN114432276B (en) | Bacterial-responsive microneedle patch and preparation method and application thereof | |
| KR101700603B1 (en) | An anti-microbial peptide, Periplanetasin-1 isolated from Periplaneta americana and its synthetic composition | |
| KR102415725B1 (en) | Novel antimicrobial peptide H123 and uses thereof | |
| CN109810178B (en) | Anti-enzymolysis antibacterial peptide I9H12, and preparation method and application thereof | |
| KR102415734B1 (en) | Novel antimicrobial peptide and uses thereof | |
| CN105566452A (en) | Antibacterial peptide with annular structure and preparation method and application thereof | |
| CN116874613B (en) | Broad-spectrum efficient antibacterial polypeptide APH143 and preparation method and application thereof | |
| CN110156875B (en) | Antibacterial peptide H5-p5, and preparation method and application thereof | |
| WO2015108333A1 (en) | Analogue peptide cma3 derived from cm-ma peptide and use thereof | |
| TWI403330B (en) | Low hemolysis antibacterial peptide pharmaceutical compositions and use thereof | |
| CN114699387A (en) | Drug-loaded nanoparticle with core-shell structure and preparation method and application thereof | |
| CN112625092B (en) | Antibacterial polypeptide compound based on polybia-MPI and synthesis and application thereof | |
| CN111518187B (en) | Antibacterial peptide DN6NH2 and application thereof | |
| CN111423493A (en) | Palmitic acid anti-enzymolysis antibacterial peptide and preparation method and application thereof | |
| CN114349826B (en) | Antibacterial peptide CGS7 and preparation method and application thereof | |
| TWI577697B (en) | Salt and protease-resistance of antimicrobial peptide and the manufacture thereof | |
| CN104592359A (en) | Antibacterial peptide derivative from forest frog and application thereof | |
| EP1519951A2 (en) | Cationic linear peptides having antibacterial and/or antifungal properties | |
| CN112724198A (en) | Methicillin-resistant staphylococcus aureus-resistant antibacterial peptide and preparation method and application thereof | |
| KR101889404B1 (en) | An anti-microbial peptide, Periplanetasin-5 isolated from Periplaneta americana and its synthetic composition | |
| CN110615830A (en) | Application of antibacterial peptide in anti-mycobacterial infection medicine |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PB01 | Publication | ||
| PB01 | Publication | ||
| SE01 | Entry into force of request for substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| GR01 | Patent grant | ||
| GR01 | Patent grant |