CN111944020A - Antibacterial peptide and application thereof - Google Patents
Antibacterial peptide and application thereof Download PDFInfo
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- CN111944020A CN111944020A CN202010831482.0A CN202010831482A CN111944020A CN 111944020 A CN111944020 A CN 111944020A CN 202010831482 A CN202010831482 A CN 202010831482A CN 111944020 A CN111944020 A CN 111944020A
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- 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
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- A61P31/04—Antibacterial agents
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Abstract
The invention provides an antibacterial peptide and application thereof, belonging to the technical field of biology. The antibacterial peptide is obtained by rational molecular design based on an antibacterial peptide Indolicidin separated from bovine neutrophils, wherein the antibacterial peptide is an antibacterial peptide Indo-1 with an amino acid sequence shown in SEQ ID NO.1 or an antibacterial peptide Indo-2 with an amino acid sequence shown in SEQ ID NO. 2. The antibacterial peptide provided by the invention has good structural characteristics, can remarkably improve the antibacterial effect on staphylococcus aureus, salmonella and aspergillus flavus, effectively reduces the hemolysis rate and cytotoxicity of chicken red blood cells, and can be effectively used in animal-related production activities.
Description
Technical Field
The invention belongs to the technical field of biology, and particularly relates to an antibacterial peptide and application thereof.
Background
With the use of antibiotics in large quantities, the resistance of microorganisms to antibiotics is getting worse and worse, and many pathogenic bacteria produce resistant strains ("super bacteria"). According to data, more than 16 ten thousand tons of antibiotics are invested in 2013 in China, wherein the veterinary antibiotics account for more than 50 percent. Some domestic farmers blindly improve the breeding benefit, and excessively depend on the use of antibiotics in the breeding process, so that the drug effect is greatly reduced, and even the pathogenic condition of pathogenic bacteria is enhanced.
The antibacterial peptide has broad-spectrum and high-efficiency antibacterial property and cell selectivity, has a unique membrane damage or intracellular sterilization mechanism, is not easy to cause drug resistance mutation of pathogens, and has the characteristics that the antibacterial peptide is expected to become a new generation of effective 'antibiotics' for controlling the pathogens in the present embarrassment.
However, the natural antibacterial peptide has low yield, long period and high extraction cost, and the artificial extraction cannot meet the large-scale production and popularization, so that the antibacterial peptide and the derivative polymer thereof are synthesized by a chemical synthesis method, and the current chemical synthesis technology is relatively mature. The bacteriostatic effect of the antibacterial peptide is the key of research, most of the current domestic research is still in the preclinical stage, the prepared antibacterial peptide is relatively few, and the main difficulties comprise higher production cost, lack of systematic long-term toxicological evaluation data, easy degradation of the antibacterial peptide by protease and other self defects. Therefore, the modification of the existing antibacterial peptide has become one of the hot spots of the current research.
Disclosure of Invention
The antibacterial peptide has good structural characteristics, can remarkably improve the bacteriostatic effect on staphylococcus aureus, salmonella and aspergillus flavus, effectively reduces the hemolysis rate and cytotoxicity of chicken red blood cells, and can be effectively used in animal-related production activities.
In order to achieve the above object, the present invention provides an antimicrobial peptide, which is obtained by rational molecular design based on an antimicrobial peptide indolcidin isolated from bovine neutrophils, wherein the antimicrobial peptide is an antimicrobial peptide Indo-1 having an amino acid sequence shown in SEQ ID No.1 or an antimicrobial peptide Indo-2 having an amino acid sequence shown in SEQ ID No. 2.
Preferably, the antibacterial peptide Indolicidin has an amino acid sequence shown as SEQ ID NO. 3.
The invention also provides application of the antibacterial peptide in inhibiting staphylococcus aureus, salmonella and vibrio parahaemolyticus according to the technical scheme.
Preferably, the minimum inhibitory concentration of the antibacterial peptide Indo-1 to staphylococcus aureus is 500 mug/mL, and the minimum inhibitory concentration of the antibacterial peptide Indo-2 to staphylococcus aureus is 400 mug/mL.
Preferably, the minimum inhibitory concentration of the antibacterial peptide Indo-1 and the antibacterial peptide Indo-2 to the salmonella is 600 mu g/mL.
The invention also provides application of the antibacterial peptide in inhibiting the fungus Aspergillus flavus.
Preferably, the minimum inhibitory concentration of the antibacterial peptide Indo-1 and the antibacterial peptide Indo-2 to the fungus Aspergillus flavus is 1 mg/mL.
The invention also provides a biological antibacterial agent which takes the antibacterial peptide Indo-1 in the technical scheme as a main component, or takes the antibacterial peptide Indo-2 in the technical scheme as a main component, or takes a mixture of the antibacterial peptide Indo-1 and the antibacterial peptide Indo-2 as a main component.
The invention also provides animal feed which takes the antibacterial peptide Indo-1 in the technical scheme as a main component, or takes the antibacterial peptide Indo-2 in the technical scheme as a main component, or takes a mixture of the antibacterial peptide Indo-1 and the antibacterial peptide Indo-2 as a main component.
Preferably, the antibacterial peptide Indo-1 and the antibacterial peptide Indo-2 have hemolysis rates of less than 40% in the concentration range of 1-50 mg/mL; the survival rates of the antibacterial peptide Indo-1 and the antibacterial peptide Indo-2 are both more than 99.7 percent in the concentration range of 0.2-3.2 mg/mL.
Compared with the prior art, the invention has the advantages and positive effects that:
1. the invention successfully carries out rational molecular design on the antibacterial peptide, screens 2 antibacterial peptides based on the rational design, and obtains the 2 antibacterial peptides with good structural characteristics through biological parameter prediction, thereby determining the important guiding significance of bioinformatics software on the design and optimization of the antibacterial peptide.
2. The invention carries out biological activity detection on the synthesized antibacterial peptide, and proves that the antibacterial peptide with rational molecular design can obviously improve the bacteriostatic effect on staphylococcus aureus, salmonella and aspergillus flavus to a certain extent.
3. The antibacterial peptide sequence designed by the invention can reduce the hemolysis rate of chicken red blood cells and reduce cytotoxicity based on the replacement of hydrophobic amino acid, so that the antibacterial peptide sequence can be effectively used in animal-related production activities.
Drawings
FIG. 1 is a schematic diagram showing that the antibacterial peptide Indo-1 and the antibacterial peptide Indo-2 provided by the present invention contain an alpha helical form and an irregular coil form;
FIG. 2 is a schematic diagram showing the inhibition of the antimicrobial peptides Indo-1 and Indo-2 and the antimicrobial peptide Indolicidin provided by the present invention against Staphylococcus aureus at a concentration of 500. mu.g/mL;
FIG. 3 is a schematic diagram showing the inhibition of the antibacterial peptide Indo-1 and the antibacterial peptide Indo-2 provided by the present invention and the antibacterial peptide Indolicidin against Salmonella at a concentration of 800 μ g/mL, wherein the antibacterial peptide Indolicidin is shown on the upper left, the antibacterial peptide Indo-1 is shown on the lower left, and the antibacterial peptide Indo-2 is shown on the lower right;
FIG. 4 is a schematic diagram showing the inhibition and comparison of the antimicrobial peptide Indo-2 and the antimicrobial peptide Indolicidin provided by the present invention against Aspergillus flavus at a concentration of 1mg/mL, wherein the left diagram is the antimicrobial peptide Indolicidin, and the right diagram is the antimicrobial peptide Indo-2;
FIG. 5 is a schematic diagram showing the comparison of the antibacterial peptide Indo-1, the antibacterial peptide Indo-2 and the antibacterial peptide Indolicidin provided by the present invention for inhibiting the fungus Aspergillus flavus under the conditions of 1mg/mL concentration and 1.5 ten thousand times amplification, wherein A is the antibacterial peptide Indolicidin, C is the antibacterial peptide Indo-1, and D is the antibacterial peptide Indo-2.
Detailed Description
The technical solutions in the embodiments of the present invention will be clearly and completely described below, and it is obvious that the described embodiments are only a part of the embodiments of the present invention, and not all embodiments. All other embodiments, which can be derived by a person skilled in the art from the embodiments given herein without making any creative effort, shall fall within the protection scope of the present invention.
Example 1
Indolicidin is an antibacterial peptide isolated from bovine neutrophils, consists of 13 amino acids, is rich in tryptophan and has a distinct extended structure. Indolicidin has a broad antibacterial spectrum and has antibacterial activity against various gram-positive bacteria, gram-negative bacteria and fungi. The rational molecular design provided by the invention comprises the design of increasing the number of electropositive amino acids, increasing the proportion of hydrophobic amino acids, increasing the proportion of alpha-helix and properly introducing unnatural amino acids (such as ornithine) and D-type amino acids for the antibacterial peptide Indolicidin, and specifically comprises the following steps:
the method comprises the steps of sequentially replacing 8 amino acids including alanine, proline, leucine, lysine, arginine, glycine, valine and histidine from a first amino acid in a de novo replacement mode, then performing pairwise combined replacement to construct an optimized peptide library, inputting a replaced amino acid sequence into analysis software to predict the molecular weight, the charge number, the average hydrophilic value, the average hydrophobic value, the hydrophilic and hydrophobic residue number and the instability index of the antibacterial peptide, and predicting the secondary structure, the amphipathy and the charge distribution which may be formed by the antibacterial peptide, and selecting the optimal antibacterial peptide (Table 1). The software used was as follows:
physical and chemical characteristic analysis website: ExPASy (http:// www.expasy.ch /)
Secondary structure prediction website: NPS @
(https://npsa-prabi.ibcp.fr/cgi-bin/npsa_automat.pl？page＝/NPSA/npsa_server.html)
Secondary structure analysis website: NetSurfP-2.0
(https://services.healthtech.dtu.dk/service.php？NetSurfP-2.0)
Hydrophobicity analysis website: HeliQuest (https:// helix. ipmc. cnrs. fr.)
The amino acid sequences of the structurally optimized antimicrobial peptides obtained in the above manner are shown in table 1, and the physicochemical properties thereof are shown in table 2.
TABLE 1 rational molecular design of amino acid sequences of antimicrobial peptides
Through rational molecular design, on the basis of the original antibacterial peptide Indolicidin, through increasing the number of electropositive amino acids, improving the proportion of hydrophobic amino acids, improving the proportion of alpha-helix and properly introducing unnatural amino acids (such as ornithine) and D-type amino acids, compared with the Indolicidin, Indo-1 and Indo-2 obviously increase electrostatic charges, so that the antibacterial peptide can conveniently pass through cell membranes and enter cytoplasm to play an antibacterial role; among them, Indo-2 also increases the proportion of D-form amino acids appropriately, so that it can more stably act in cells.
In addition, in the 2 predicted novel antimicrobial peptides, Indo-1 and Indo-2 both had an amino acid length of 13, and both of the predicted results contained an alpha helical morphology and an irregular coil shape, as shown in FIG. 1.
Example 2 bacteriostatic Activity
Antibacterial peptides were synthesized by gill biochemical (shanghai) ltd.
Transferring the activated bacteria into LB liquid culture medium, shake culturing at 37 deg.C for 10-12h, centrifuging at 5000r/min for 5min, discarding supernatant, washing thallus with 0.85% sterile physiological saline once, centrifuging at the same speed (5000r/min) for 5min, discarding supernatant, diluting the precipitate with LB liquid culture medium to 1 × 108CFU/mL as the bacterial liquid to be tested.
Measurement of Minimum Inhibitory Concentration (MIC) in liquid culture Medium
Adding bacterial liquid (staphylococcus aureus, vibrio parahaemolyticus, salmonella or aspergillus flavus) cultured to logarithmic growth phase into a 96-well plate, adding 50 mu L of each antibacterial peptide into each well according to gradient concentration (mu g/mL), and respectively making a negative control group and a positive control group. After incubation at 37 ℃ for 6h, the OD at 630nm was determined. When the OD value of the antibacterial peptide corresponding to a certain concentration in the pore plate is measured to have no obvious difference from the initial value, the Minimum Inhibitory Concentration (MIC) measured by the antibacterial peptide is the concentration, and the test results are shown in tables 3-6.
② experiment of zone of inhibition
Preparing an LB solid culture medium, respectively coating staphylococcus aureus, salmonella, vibrio parahaemolyticus or aspergillus flavus in the culture medium, dissolving and diluting the antibacterial peptide, dropwise adding the antibacterial peptide on a filter paper sheet according to different gradients to perform an antibacterial zone experiment by using the antibacterial peptide with different concentration gradients, culturing for 24 hours at 37 ℃, and measuring the diameter of the antibacterial zone, wherein the test result is shown in figures 2-3.
TABLE 3 antibacterial Activity of antibacterial peptides against Staphylococcus aureus
Inhibition of staphylococcus aureus: as can be seen from Table 3 and FIG. 2, the bacteriostatic effect of the novel antibacterial peptides Indo-1 and Indo-2 designed by rational molecules on Staphylococcus aureus is improved by more than 50% compared with the original antibacterial peptide Indolicidin.
TABLE 4 bacteriostatic Activity of antimicrobial peptides against Salmonella
Inhibition of salmonella: as can be seen from Table 4 and FIG. 3, the rational molecular design of the novel antimicrobial peptides Indo-1 and Indo-2 has an improvement of about 50% for Salmonella over the original antimicrobial peptide Indolicidin, but the MIC is slightly lower than that for Staphylococcus aureus.
TABLE 5 antibacterial Activity of antibacterial peptides against Vibrio parahaemolyticus
Inhibition of vibrio parahaemolyticus: as can be seen from Table 5, the new antibacterial peptides Indo-1 and Indo-2 designed by rational molecules have improved values of vibrio parahaemolyticus by about 50% compared with the original antibacterial peptide Indolicidin, and the MIC is higher than that of staphylococcus aureus.
TABLE 6 bacteriostatic activity of antimicrobial peptides against Aspergillus flavus
Inhibition of the fungus Aspergillus flavus: as can be seen from Table 6 and FIG. 4, the inhibitory effect of the antimicrobial peptide Indolicidin on the fungus Aspergillus flavus is general, but the inhibitory effect on the Aspergillus flavus is remarkably improved by the novel antimicrobial peptides Indo-1 and Indo-2 designed by rational molecules, and can be improved by about 50%. It can also be seen from FIG. 5 that at a concentration of 1mg/mL, the growth of Aspergillus flavus could not be inhibited by the propeptide Indolicidin, while Indo-1 and Indo-2 significantly improved the ability to inhibit the growth of Aspergillus flavus, manifested by a slow and abnormal development of hyphae.
Example 3 hemolytic Activity assay
Adding heparin into healthy chicken blood for anticoagulation, centrifuging at 1000 Xg for 10min, collecting precipitate, washing with PBS buffer solution for 3 times, and counting and diluting erythrocytes to 1%. After the antibacterial peptide is diluted twice, adding the antibacterial peptide into a 96-well plate at the dosage of 50 mu L per well; diluted erythrocytes (50. mu.L per well) and antimicrobial peptide were added to a 96-well plate, mixed, incubated at 37 ℃ for 1 hour, centrifuged at 1000 Xg at 4 ℃ to collect the supernatant, and the absorbance was measured at OD 570 nm. mu.L of erythrocyte suspension and 50. mu.L of 0.2% TritonX-100 were added as a 100% hemolytic positive control, and 50. mu.L of erythrocyte suspension and 50. mu.L of phosphate buffer were added as a negative control.
The hemolysis rate is calculated as: hemolysis rate ═ aT-A0)/(AC-A0)×100％。
In the formula: a. theTAbsorbance of the experimental group, ACAbsorbance of the positive control group, A0The absorbance of the negative control group was obtained.
TABLE 7 hemolytic activity of antibacterial peptide (average value of 3 determinations)
As can be seen from the data in Table 7, in the concentration range of 1-50mg/mL, the hemolysis rate of chicken erythrocytes gradually increases with the increase of the concentration of the antimicrobial peptide, but in the concentration range measured, the hemolysis rate of the antimicrobial peptide is less than 40%, which indicates that the novel antimicrobial peptide provided by the present invention can be applied to animal-related production activities, such as animal feed.
Example 4 cytotoxicity assays
The toxicity of the obtained antimicrobial peptide on cells was evaluated by MTT assay using MTT cell proliferation and cytotoxicity assay kit (E606334-0500, Shanghai Biotech Co., Ltd.).
Add 100. mu.L of DMEM to each well of 96-well plate and then inoculate each well with 5.0X 103Such that the final contents per well are 0.02mg, 0.08mg and 0.32mg, respectively, were subjected to reactions for 12, 24, 48 and 72 hours. The negative control group was DMEM medium containing only chicken embryonic fibroblasts and PBS buffer. At the end of each experiment, the supernatant was removed and MTT reagent was added to each well at a concentration of 0.5mg/mL and the 96-well plate was incubated at 37 ℃ for 4 hours. Finally, the MTT reagent was removed and the absorbance read at 570nm on a microplate reader.
The method for calculating the survival rate comprises the following steps: survival rate ═ aT/A0)×100％。
In the formula: a. theTFor the absorbance of the test cells, A0The absorbance value of the control group cells is shown.
TABLE 8 cytotoxicity of antibacterial peptides (72 hours, 3 determinations, average)
As can be seen from the data in Table 8, no significant cytotoxicity is shown in the concentration range of 0.2-3.2mg/mL after exposure for 72 hours, which indicates that the antibacterial peptide provided by the invention is nontoxic to cells, has no negative effect on cell proliferation and cell activity, does not generate toxic threat to normal cells, and further can be deeply researched, developed and utilized as biological antibacterial peptide.
Sequence listing
<110> China oceanic university
<120> antibacterial peptide and use thereof
<160> 3
<170> PatentIn version 3.3
<210> 1
<211> 13
<212> PRT
<213> antimicrobial peptide Indo-1
<400> 1
ILRRKWPRWPKRR 13
<210> 2
<211> 13
<212> PRT
<213> antimicrobial peptide Indo-2
<400> 2
ILKAKW(D)PRW(D)PKRR(D) 13
<210> 3
<211> 13
<212> PRT
<213> antimicrobial peptide Indolicidin
<400> 3
ILPWKWPWWPWRR 13
Claims (10)
1. The antibacterial peptide is obtained by rational molecular design based on an antibacterial peptide Indolicidin separated from bovine neutrophils, and is antibacterial peptide Indo-1 with an amino acid sequence shown in SEQ ID No.1 or antibacterial peptide Indo-2 with an amino acid sequence shown in SEQ ID No. 2.
2. The antimicrobial peptide according to claim 1, wherein said antimicrobial peptide Indolicidin has the amino acid sequence as shown in SEQ ID No. 3.
3. The use of the antimicrobial peptide of claim 1 for inhibiting staphylococcus aureus, salmonella, and vibrio parahaemolyticus.
4. The use according to claim 3, wherein the minimum inhibitory concentration of the antibacterial peptide Indo-1 against Staphylococcus aureus is 500 μ g/mL, and the minimum inhibitory concentration of the antibacterial peptide Indo-2 against Staphylococcus aureus is 400 μ g/mL.
5. The use as claimed in claim 3, wherein the minimum inhibitory concentration of the antimicrobial peptides Indo-1 and Indo-2 against Salmonella is 600 μ g/mL.
6. The use of the antimicrobial peptide of claim 1 for inhibiting the fungus Aspergillus flavus.
7. The use according to claim 6, characterized in that the minimum inhibitory concentration of the antimicrobial peptides Indo-1 and Indo-2 on the fungus Aspergillus flavus is 1 mg/mL.
8. A biological antibacterial agent comprising the antibacterial peptide Indo-1 according to claim 1 as a main component, or the antibacterial peptide Indo-2 according to claim 1 as a main component, or a mixture thereof.
9. Animal feed comprising the antimicrobial peptide Indo-1 according to claim 1 as the main component, or the antimicrobial peptide Indo-2 according to claim 1 as the main component, or a mixture thereof as the main component.
10. The animal feed according to claim 9, characterized in that said antimicrobial peptides Indo-1 and Indo-2 have a hemolysis rate of < 40% both in the concentration range of 1-50 mg/mL; the survival rates of the antibacterial peptide Indo-1 and the antibacterial peptide Indo-2 are both more than 99.7 percent in the concentration range of 0.2-3.2 mg/mL.
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Cited By (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN112898386A (en) * | 2021-03-02 | 2021-06-04 | 集美大学 | Large yellow croaker myosin heavy chain antibacterial peptide LCMHC and application thereof |
| CN112940082A (en) * | 2021-04-23 | 2021-06-11 | 扬州市扬大康源乳业有限公司 | Antibacterial peptide and application thereof |
| CN113336828A (en) * | 2021-06-30 | 2021-09-03 | 中国海洋大学 | Antibacterial peptide YHX-3 and composition and application thereof |
| CN113754784A (en) * | 2021-09-27 | 2021-12-07 | 中国农业大学 | Cell-penetrating antibacterial peptide and application thereof |
| CN114409759A (en) * | 2022-01-28 | 2022-04-29 | 长春普思康医疗科技有限公司 | RP23 protein with antibacterial function |
| CN114516899A (en) * | 2022-01-27 | 2022-05-20 | 中国海洋大学 | Antibacterial peptide YHX-5 and application thereof |
| CN114516900A (en) * | 2022-01-27 | 2022-05-20 | 中国海洋大学 | Antibacterial peptide YHX-4 and application thereof |
| CN115043925A (en) * | 2022-04-29 | 2022-09-13 | 苏州大学 | Modified antibacterial peptide oNCM and application thereof |
| CN116375828A (en) * | 2022-09-08 | 2023-07-04 | 浙江大学 | Antibacterial peptide KTA with high antibacterial activity and application thereof |
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Cited By (17)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN112898386A (en) * | 2021-03-02 | 2021-06-04 | 集美大学 | Large yellow croaker myosin heavy chain antibacterial peptide LCMHC and application thereof |
| CN112898386B (en) * | 2021-03-02 | 2022-06-28 | 集美大学 | Large yellow croaker myosin heavy chain antibacterial peptide LCMHC and application thereof |
| CN112940082A (en) * | 2021-04-23 | 2021-06-11 | 扬州市扬大康源乳业有限公司 | Antibacterial peptide and application thereof |
| CN112940082B (en) * | 2021-04-23 | 2022-05-27 | 扬州市扬大康源乳业有限公司 | Antibacterial peptide and application thereof |
| CN113336828B (en) * | 2021-06-30 | 2022-03-25 | 中国海洋大学 | Antibacterial peptide YHX-3 and composition and application thereof |
| CN113336828A (en) * | 2021-06-30 | 2021-09-03 | 中国海洋大学 | Antibacterial peptide YHX-3 and composition and application thereof |
| CN113754784A (en) * | 2021-09-27 | 2021-12-07 | 中国农业大学 | Cell-penetrating antibacterial peptide and application thereof |
| CN113754784B (en) * | 2021-09-27 | 2023-08-15 | 中国农业大学 | Cell penetrating antibacterial peptide and application thereof |
| CN114516899A (en) * | 2022-01-27 | 2022-05-20 | 中国海洋大学 | Antibacterial peptide YHX-5 and application thereof |
| CN114516900A (en) * | 2022-01-27 | 2022-05-20 | 中国海洋大学 | Antibacterial peptide YHX-4 and application thereof |
| CN114516899B (en) * | 2022-01-27 | 2023-06-16 | 中国海洋大学 | Antibacterial peptide YHX-5 and application thereof |
| CN114516900B (en) * | 2022-01-27 | 2023-06-16 | 中国海洋大学 | Antibacterial peptide YHX-4 and application thereof |
| CN114409759A (en) * | 2022-01-28 | 2022-04-29 | 长春普思康医疗科技有限公司 | RP23 protein with antibacterial function |
| CN114409759B (en) * | 2022-01-28 | 2022-07-12 | 长春普思康医疗科技有限公司 | RP23 protein with antibacterial function |
| CN115043925A (en) * | 2022-04-29 | 2022-09-13 | 苏州大学 | Modified antibacterial peptide oNCM and application thereof |
| CN115043925B (en) * | 2022-04-29 | 2023-08-11 | 苏州大学 | Modified antibacterial peptide oNCM and application thereof |
| CN116375828A (en) * | 2022-09-08 | 2023-07-04 | 浙江大学 | Antibacterial peptide KTA with high antibacterial activity and application thereof |
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| CN111944020B (en) | 2022-05-24 |
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