CN114149487A - Antibacterial peptide WR and hyaluronic acid coating substance and application thereof - Google Patents
Antibacterial peptide WR and hyaluronic acid coating substance and application thereof Download PDFInfo
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- CN114149487A CN114149487A CN202111332538.9A CN202111332538A CN114149487A CN 114149487 A CN114149487 A CN 114149487A CN 202111332538 A CN202111332538 A CN 202111332538A CN 114149487 A CN114149487 A CN 114149487A
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- 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
- C07K7/06—Linear peptides containing only normal peptide links having 5 to 11 amino acids
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
- A61K47/50—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates
- A61K47/51—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent
- A61K47/56—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an organic macromolecular compound, e.g. an oligomeric, polymeric or dendrimeric molecule
- A61K47/61—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an organic macromolecular compound, e.g. an oligomeric, polymeric or dendrimeric molecule the organic macromolecular compound being a polysaccharide or a derivative thereof
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
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- B—PERFORMING OPERATIONS; TRANSPORTING
- B82—NANOTECHNOLOGY
- B82Y—SPECIFIC USES OR APPLICATIONS OF NANOSTRUCTURES; MEASUREMENT OR ANALYSIS OF NANOSTRUCTURES; MANUFACTURE OR TREATMENT OF NANOSTRUCTURES
- B82Y40/00—Manufacture or treatment of nanostructures
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- B—PERFORMING OPERATIONS; TRANSPORTING
- B82—NANOTECHNOLOGY
- B82Y—SPECIFIC USES OR APPLICATIONS OF NANOSTRUCTURES; MEASUREMENT OR ANALYSIS OF NANOSTRUCTURES; MANUFACTURE OR TREATMENT OF NANOSTRUCTURES
- B82Y5/00—Nanobiotechnology or nanomedicine, e.g. protein engineering or drug delivery
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
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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
Abstract
The invention provides an antibacterial peptide WR and a hyaluronic acid coating and application thereof, wherein the sequence of the antibacterial peptide WR is shown as SEQID No. 1; simultaneously provides the application of the antibacterial peptide in preparing the medicine for treating gram-negative bacteria or/and gram-positive bacteria infectious diseases; adding anionic hyaluronic acid into the solution containing the antibacterial peptide WR with the self-assembled nano structure to perform electrostatic bonding to prepare the coating. Simultaneously provides the application of the coating material in preparing the medicine for treating the infectious diseases of gram-negative bacteria or/and gram-positive bacteria in the environment of protease. The antibacterial peptide has very low hemolytic activity and eukaryotic cytotoxicity, and the enzymatic stability of the antibacterial peptide coated with the anionic hyaluronic acid is detected, and the antibacterial peptide is not completely inactivated in the presence of 0.1mg/ml papain. In conclusion, the antibacterial peptide has higher application value and has the prospect of replacing feed antibiotics.
Description
Technical Field
The invention belongs to the field of application of agriculture, livestock husbandry and veterinarians, and particularly relates to antibacterial peptide WR, a hyaluronic acid coating of the antibacterial peptide WR and application of the antibacterial peptide WR.
Background
Under the large background of feed banning, the antibacterial peptide has become a potential substance for replacing feed antibiotics due to the characteristics of broad-spectrum antibiosis and no drug resistance. The antibacterial peptide has a unique bacteriostatic mechanism, namely, the amphipathy of the peptide (the amino acid residue of the peptide has positive charge and hydrophobic property) is utilized to physically destroy the bacterial membrane, so that the antibacterial peptide is inserted into a lipid membrane component to disturb the membrane conformation, the normal metabolism of bacteria is interfered, and finally, a cell membrane hole is formed, so that the cytosol of the bacteria flows out and dies. This bactericidal mechanism is not involved in intracellular anabolism and therefore does not develop broad spectrum resistance to bacteria. However, as a small molecule polypeptide, the antimicrobial peptide is very sensitive to various proteases in animal gastrointestinal tract, which is also a bottleneck problem in the development of feeding type antimicrobial peptides. Therefore, there is an urgent need to develop a method capable of resisting hydrolysis by protease to prolong the half-life of the antimicrobial peptide in vivo.
Disclosure of Invention
Based on the defects, the invention aims to provide the antibacterial peptide WR which is a cationic antibacterial peptide. The antibacterial peptide WR not only has high-efficiency inhibiting effect on six strains such as escherichia coli, staphylococcus aureus, staphylococcus epidermidis, salmonella typhimurium and the like, but also has very low hemolytic activity and eukaryotic cytotoxicity.
The technical scheme adopted by the invention is as follows: an antibacterial peptide WR, the sequence of which is shown in SEQ ID No. 1.
The invention also aims to provide the application of the antibacterial peptide WR in preparing a medicament for treating gram-positive bacteria or/and gram-negative bacteria infectious diseases.
The invention also aims to provide a hyaluronic acid coating of antibacterial peptide WR, which is prepared by the following method: adding anionic hyaluronic acid into the solution containing the antibacterial peptide WR with the self-assembled nano structure, enabling the solution to generate electrostatic bonding, and coating the antibacterial peptide WR to obtain the antibacterial peptide WR hyaluronic acid coating. The invention achieves the purpose of coating the antibacterial peptide by utilizing the electrostatic combination of the anion characteristic of the hyaluronic acid and the cationic antibacterial peptide residue on the basis of not influencing the antibacterial activity of the antibacterial peptide, and the coated antibacterial peptide can effectively resist the hydrolysis of protease without losing the antibacterial activity.
Further, the hyaluronic acid coating of the antibacterial peptide WR is prepared by adopting the following method: diluting the antibacterial peptide WR to a self-assembly critical concentration, incubating for 18-24 hours at 37 ℃ to form a self-assembly nano structure, adding an anionic hyaluronic acid solution into the antibacterial peptide diluent, stopping dripping after the solution is turbid, stirring until the solution is clear, and refrigerating at 4 ℃ for later use.
Further, the hyaluronic acid coating of the antibacterial peptide WR is prepared by adopting the following method: uniformly dissolving antibacterial peptide WR freeze-dried powder in ultrapure water, performing ultrasonic treatment for 5 minutes, quickly subpackaging and diluting to a self-assembly critical concentration, incubating antibacterial peptide WR diluent at 37 ℃ for 18-24 hours to form a self-assembly nano structure, dissolving 3.6mg of anionic hyaluronic acid freeze-dried powder in 5ml of ultrapure water, and performing ultrasonic treatment to obtain uniform and clear solution, wherein the concentration of the anionic hyaluronic acid is 0.72 mg/ml; and then dropwise adding an anionic hyaluronic acid solution into the solution of the self-assembled nano-structure antibacterial peptide WR, stopping dropwise adding after the solution is turbid, wherein the dropwise adding of the anionic hyaluronic acid solution is as follows: solution of self-assembled nanostructured antimicrobial peptide WR in volume ratio 3: 1, continuously stirring until the solution is uniform and clear, and refrigerating at 4 ℃ for later use; finally, the final concentration of the anionic hyaluronic acid is 0.18mg/ml, and the final concentration of the antibacterial peptide WR is 640 mu M.
The invention also aims to provide application of the hyaluronic acid coating of the antibacterial peptide WR in preparing a medicament for treating gram-negative bacteria or/and gram-positive bacteria infectious diseases in the environment of protease.
The invention has the following beneficial effects and advantages: the antibacterial peptide WR is a cationic antibacterial peptide, and can generate electrostatic combination after anionic hyaluronic acid is added into a solution with a self-assembled nano structure, so as to achieve the purpose of coating the antibacterial peptide. The antibacterial peptide WR not only has high-efficiency inhibiting effect on six strains such as escherichia coli, staphylococcus aureus, staphylococcus epidermidis, salmonella typhimurium and the like, but also has very low hemolytic activity and eukaryotic cytotoxicity, the antibacterial peptide causes 1% of erythrocyte hemolysis under the concentration of 64 mu M, 10% of erythrocyte hemolysis cannot be caused, and the survival rate of macrophage RAW264.7 of a mouse reaches 100%. In addition, the enzymatic stability of the antibacterial peptide of hyaluronic acid coated with anions was examined, and it was not completely inactivated in the presence of 0.1mg/ml of papain. In conclusion, the hyaluronic acid coated self-assembled antibacterial peptide is an antibacterial peptide with high application value, and has the potential of being developed as a feeding antibacterial peptide.
Drawings
FIG. 1 is a high performance liquid chromatogram of the antimicrobial peptide of the present invention.
FIG. 2 is a matrix-assisted laser desorption/ionization time-of-flight mass spectrum of the antimicrobial peptide of the present invention.
FIG. 3 is a graph showing hemolytic activity of the antimicrobial peptide of the present invention.
FIG. 4 is a cytotoxicity diagram of the antibacterial peptide of the present invention.
Detailed Description
The invention is further illustrated by way of example in the accompanying drawings of the specification:
example 1
Design of antimicrobial peptides
The amino acid sequence of antibacterial peptide WR is as follows:
WWRRRRWW；
an antibacterial peptide is designed and constructed by taking a tryptophan zipper as a basic motif and a bola structure as a basic unit, and is named as WR. The sequences of the antimicrobial peptides are shown in table 1.
TABLE 1 amino acid sequence
The charge number of WR is +4 and the hydrophobic value is-0.15. The antibacterial peptide not only can be self-assembled to form a nano micelle, but also can wrap a layer of hyaluronic acid by taking the micelle as a core so as to protect the antibacterial peptide from being hydrolyzed by protease; has high-efficiency antibacterial activity and lower hemolytic activity, improves the selectivity of the antibacterial peptide between bacterial cells and mammalian cells, and has the development potential of becoming an antibiotic substitute.
Example 2
Determination of antibacterial Activity of antibacterial peptides
1. The minimum inhibitory concentration of the antibacterial peptide WR and the antibacterial peptide WR coated by the hyaluronic acid is determined by a broth dilution method. Serial gradients of antimicrobial peptide solutions were prepared sequentially using a two-fold dilution method using 2mg/ml BSA (containing 0.01% acetic acid) as the diluent. Taking 100 mu L of the solution, placing the solution into a 96-hole cell culture plate, and then respectively adding the bacterial liquid to be detected (10-10) with the same volume5one/mL) in each well. Positive controls (containing the bacterial solution but not the antimicrobial peptide) and negative controls (containing neither the bacterial solution nor the antimicrobial peptide) were set separately. Culturing at 37 deg.C for 14-18h, and measuring with ELISA reader at 492nm (OD)492nm) And (4) measuring the light absorption value, and determining the minimum inhibitory concentration. The results are shown in Table 2.
TABLE 2 bacteriostatic Activity of antimicrobial peptides
As can be seen from table 2, WR shows higher bacteriostatic activity against gram-negative and positive bacteria.
2. Determination of hemolytic Activity: collecting 1mL of fresh human blood, dissolving heparin into 2mL of PBS solution after anticoagulation, centrifuging at 3000rpm for 10min, and collecting erythrocytes; washing with PBS solution for 3 times, and then resuspending with 10mL PBS solution; uniformly mixing 50 mu L of erythrocyte suspension with 50 mu L of antibacterial peptide solutions with different concentrations, and incubating for 1h at constant temperature in an incubator at 37 ℃; then centrifuging at 4 ℃ and 3000rpm for 10 min; the supernatant was removed and the absorbance was measured at 570nm using a microplate reader. The negative control consisted of 50. mu.L of red blood cells plus 50. mu.L of PBS solution, and the positive control consisted of 50. mu.L of red blood cells plus 50. mu.L of 0.1% Tritonx-100. The minimum hemolytic concentration is the concentration of antimicrobial peptide at which the antimicrobial peptide causes a 10% hemolytic rate.
As shown in FIG. 3, it can be seen from FIG. 3 that WR showed no hemolytic activity in the detection range, caused hemolysis of 1% of erythrocytes at a concentration of 64. mu.M, failed to cause hemolysis of 10% of erythrocytes, and was significantly different from the control melittin. As can be seen from Table 3, the selection index of the antibacterial peptide WR is higher than that of melittin with strong toxicity, which indicates that the antibacterial peptide WR has the potential of being developed into a feeding type antibacterial peptide.
TABLE 3 MHC (. mu.M), GM (. mu.M) and SI values of the antimicrobial peptides
3. Determination of eukaryotic cytotoxicity: cytotoxicity assays were performed using MTT and the mouse macrophage RAW 264.7.
(1) Preparation of culture medium and culture of cells: DMEM (culture medium) and fetal calf serum are mixed according to a ratio of 9:1 to prepare a complete culture medium, and mouse macrophage RAW264.7 in liquid nitrogen is recovered, wherein cells grow over the bottom of a bottle (80% -90%).
(2) Experimental treatment of the cells to be used: the cells were washed and resuspended 3 times using sterile PBS solution, and the cells were digested with pancreatin digest to be detached at the bottom of the flask, followed by rinsing with complete medium to obtain a single cell suspension while filling a 96-well plate with 50. mu.L of a final concentration of about 2X 104The cell suspension of (3).
(3) And (3) antibacterial peptide treatment: adding 10 mu L of antibacterial peptide into a first hole of a 96-hole plate, taking out 50 mu L of antibacterial peptide, adding the antibacterial peptide into 1-10 holes of the original 96-hole plate, diluting by multiple times, adding 50 mu L of complete culture medium into 11 holes, adding 100 mu L of complete culture medium into 12 holes, and culturing for 4 hours at constant temperature;
(4) and (3) toxicity detection: adding 50 μ L of 5mg/mL MTT solution into 96-well plate, culturing for 3-4h, adding 150 μ L DMSO (dimethyl sulfoxide), and OD (OD) with microplate reader570nmThe absorbance was measured. Higher absorbance values demonstrate less toxicity and vice versa.
The results are shown in FIG. 4. As can be seen from FIG. 4, WR showed no toxicity to mouse macrophage in the detection range, and the survival rate of mouse macrophage RAW264.7 at 64 μ M concentration reached 100%, which is significantly different from the control group melittin.
Preparation of hyaluronic acid coating of antibacterial peptide WR: dissolving the antibacterial peptide WR freeze-dried powder in ultrapure water filtered by 0.22 mu m, and fully oscillating and dissolving uniformly. Following sonication for 5 minutes and rapid aliquot dilution to a critical concentration for self-assembly of 16 μ M, the dilutions were incubated at 37 ℃ for 18-24 hours to form self-assembled nanostructures. Dissolving 3.6mg of anion hyaluronic acid freeze-dried powder in 5ml of ultrapure water filtered by 0.22 mu m, and carrying out ultrasonic treatment until the solution is uniform and clear, wherein the concentration of the anion hyaluronic acid solution is 0.72 mg/ml. And then dropwise adding an anionic hyaluronic acid solution into the solution of the self-assembled nano-structure antibacterial peptide WR, stopping dropwise adding after the solution is turbid, wherein the dropwise adding of the anionic hyaluronic acid solution is as follows: solution of self-assembled nanostructured antimicrobial peptide WR in volume ratio 3: 1, continuously rotating under a magnetic stirrer until the solution is uniform and clear, and then placing the solution in a refrigerator at 4 ℃ for later use; the final concentration of the anionic hyaluronic acid is 0.18mg/ml, and the final concentration of the antibacterial peptide WR is 640 mu M.
4. Determination of enzymatic stability: 0.1% papain and hyaluronic acid coatings of antimicrobial peptide WR at different concentrations were incubated at 37 ℃ for 120 minutes, 30 minutes and 5 minutes, and then the antimicrobial activity of the hyaluronic acid-coated antimicrobial peptide WR was measured according to the method for measuring the antimicrobial activity of the antimicrobial peptide in step 1 of this example. The results are shown in Table 4.
TABLE 4 MIC values of hyaluronic acid coatings of antimicrobial peptide WR incubated with or without papain
Table 4 shows that the enzymolysis resistance of the hyaluronic acid coating of the antimicrobial peptide WR is significantly enhanced, and the antimicrobial peptide WR can still maintain high antimicrobial activity within 2 hours of incubation with papain, which proves that the antimicrobial peptide WR coated by the anionic hyaluronic acid can be further developed and applied in vivo.
Sequence listing
<110> northeast university of agriculture
<120> antibacterial peptide WR and hyaluronic acid coating substance and application thereof
<160> 1
<170> SIPOSequenceListing 1.0
<210> 1
<211> 8
<212> PRT
<213> Artificial Sequence (Artificial Sequence)
<400> 1
Trp Trp Arg Arg Arg Arg Trp Trp
1 5
Claims (6)
1. An antibacterial peptide WR is characterized in that the sequence is shown as SEQ ID No. 1.
2. The hyaluronic acid coating of antibacterial peptide WR is characterized by being prepared by the following method: adding anionic hyaluronic acid into the antibacterial peptide WR solution containing the self-assembled nano structure as claimed in claim 1, and allowing the solution to generate electrostatic binding, so as to coat the antibacterial peptide WR, thereby preparing the antibacterial peptide WR hyaluronic acid coating.
3. The hyaluronic acid coating of antibacterial peptide WR according to claim 2, wherein the coating is prepared by the following method: diluting the antibacterial peptide WR to a self-assembly critical concentration, incubating for 18-24 hours at 37 ℃ to form a self-assembly nano structure, adding an anionic hyaluronic acid solution into the antibacterial peptide diluent, stopping dripping after the solution is turbid, stirring until the solution is clear, and refrigerating at 4 ℃ for later use.
4. The hyaluronic acid coating of antibacterial peptide WR according to claim 2, wherein the coating is prepared by the following method: uniformly dissolving antibacterial peptide WR freeze-dried powder in ultrapure water, performing ultrasonic treatment for 5 minutes, quickly subpackaging and diluting to a self-assembly critical concentration, incubating antibacterial peptide WR diluent at 37 ℃ for 18-24 hours to form a self-assembly nano structure, dissolving 3.6mg of anionic hyaluronic acid freeze-dried powder in 5ml of ultrapure water, and performing ultrasonic treatment to obtain uniform and clear solution, wherein the concentration of the anionic hyaluronic acid is 0.72 mg/ml; and then dropwise adding an anionic hyaluronic acid solution into the solution of the self-assembled nano-structure antibacterial peptide WR, stopping dropwise adding after the solution is turbid, wherein the dropwise adding of the anionic hyaluronic acid solution is as follows: solution of self-assembled nanostructured antimicrobial peptide WR in volume ratio 3: 1, continuously stirring until the solution is uniform and clear, and refrigerating at 4 ℃ for later use; finally, the final concentration of the anionic hyaluronic acid is 0.18mg/ml, and the final concentration of the antibacterial peptide WR is 640 mu M.
5. Use of the hyaluronic acid coating of the antibacterial peptide WR according to any of claims 2-4 in the preparation of a medicament for treating infectious diseases caused by gram-negative bacteria or/and gram-positive bacteria in the presence of proteases.
6. The use of the antimicrobial peptide WR of claim 1 in the preparation of a medicament for treating infectious diseases caused by gram-negative bacteria and/or gram-positive bacteria.
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Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN116284250A (en) * | 2023-03-02 | 2023-06-23 | 东北农业大学 | Protease hydrolysis resistant high-stability antibacterial peptide HW, and preparation method and application thereof |
Citations (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101939027A (en) * | 2007-10-02 | 2011-01-05 | Mdrna有限公司 | The lipopeptid that is used for nucleic acid delivery |
| CN102391362A (en) * | 2011-12-13 | 2012-03-28 | 重庆理工大学 | Group of animal-derived cationic antibacterial peptides and its application |
| CN111533787A (en) * | 2020-03-30 | 2020-08-14 | 东北农业大学 | Linear antibacterial peptide and preparation method and application thereof |
| CN111748018A (en) * | 2020-05-19 | 2020-10-09 | 东北农业大学 | Biocompatible antibacterial peptide with self-assembly potential, and preparation method and application thereof |
| WO2021042039A1 (en) * | 2019-08-29 | 2021-03-04 | Ajk Pharmaceutical Llc | Synthetic antimicrobial peptides |
| CN113956340A (en) * | 2021-11-11 | 2022-01-21 | 东北农业大学 | Sheep-derived antibacterial peptide RLR and preparation method and application thereof |
-
2021
- 2021-11-11 CN CN202111332538.9A patent/CN114149487B/en active Active
Patent Citations (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101939027A (en) * | 2007-10-02 | 2011-01-05 | Mdrna有限公司 | The lipopeptid that is used for nucleic acid delivery |
| CN102391362A (en) * | 2011-12-13 | 2012-03-28 | 重庆理工大学 | Group of animal-derived cationic antibacterial peptides and its application |
| WO2021042039A1 (en) * | 2019-08-29 | 2021-03-04 | Ajk Pharmaceutical Llc | Synthetic antimicrobial peptides |
| CN111533787A (en) * | 2020-03-30 | 2020-08-14 | 东北农业大学 | Linear antibacterial peptide and preparation method and application thereof |
| CN111748018A (en) * | 2020-05-19 | 2020-10-09 | 东北农业大学 | Biocompatible antibacterial peptide with self-assembly potential, and preparation method and application thereof |
| CN113956340A (en) * | 2021-11-11 | 2022-01-21 | 东北农业大学 | Sheep-derived antibacterial peptide RLR and preparation method and application thereof |
Non-Patent Citations (2)
| Title |
|---|
| 曹宋宋等: "牛溶菌肽线性衍生物Bac8c的抑菌活性及其稳定性", 《中国食品学报》 * |
| 马清泉等: "富含亮氨酸和精氨酸的抗菌肽设计", 《畜牧兽医学报》 * |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN116284250A (en) * | 2023-03-02 | 2023-06-23 | 东北农业大学 | Protease hydrolysis resistant high-stability antibacterial peptide HW, and preparation method and application thereof |
| CN116284250B (en) * | 2023-03-02 | 2023-10-27 | 东北农业大学 | Protease hydrolysis resistant high-stability antibacterial peptide HW, and preparation method and application thereof |
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