CN110903347A - Antibacterial peptide L7 and application thereof - Google Patents
Antibacterial peptide L7 and application thereof Download PDFInfo
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- CN110903347A CN110903347A CN201911236961.1A CN201911236961A CN110903347A CN 110903347 A CN110903347 A CN 110903347A CN 201911236961 A CN201911236961 A CN 201911236961A CN 110903347 A CN110903347 A CN 110903347A
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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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- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
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Abstract
The invention relates to an antibacterial peptide L7 and application thereof, which have the characteristics of short peptide chain length, good stability, convenient artificial synthesis and the like. The amino acid sequence of the antimicrobial peptide L7 was searched and aligned with NCBI protein database, and no identical polypeptide was found. The antibacterial peptide L7 has broad-spectrum antibacterial activity and strong bactericidal effect, and can exert antibacterial effect by acting on cell membrane. In addition, the antibacterial peptide L7 can inhibit the formation of bacterial biofilms in a dose-dependent manner, has the characteristics of low hemolytic activity, low cytotoxicity and the like, and can be used as a new therapeutic drug for treating bacterial infections.
Description
Technical Field
The invention belongs to the technical field of biomedicine, and relates to antibacterial peptide L7 and application thereof.
Background
In recent years, with the use and abuse of antibiotics in large quantities, a large number of drug-resistant bacteria and multi-drug-resistant bacteria are continuously appeared, and great difficulty is brought to clinical treatment. In particular, the recent emergence of superbacteria in south Asia and the United states has marked the worldwide epidemic of drug-resistant bacteria. However, in recent decades, the development of novel antibiotics is scarce, and only 3 novel antibiotics against gram-positive bacteria have been developed. Therefore, the search for new antibacterial strategies is a challenge to be solved.
The antibacterial peptide is a small molecular polypeptide widely existing in organisms and is a main component of natural immunity. The antibacterial peptide has the functions of broad-spectrum antibacterial activity, antivirus, antitumor, anti-inflammatory, immunoregulation, signal transduction and the like. The traditional antibiotics mainly play an antibacterial role aiming at specific targets and metabolic pathways of bacteria, so that the bacteria are easy to mutate to obtain drug resistance. The antibacterial peptide is mainly used for killing bacteria by exosmosis of bacterial contents through physical destruction of cell membrane structures of the bacteria. Because the composition and the structure of all cell membranes of the bacteria are difficult to change to generate drug resistance on the antibacterial peptide, the antibacterial peptide serving as a new antibiotic substitute is expected to solve the problem of drug resistance of the bacteria and has wide application value.
The natural antibacterial peptide has the defects of difficult separation and purification, weak antibacterial activity, high hemolytic activity and cytotoxicity, poor stability and the like, and limits the mass production and clinical application of the natural antibacterial peptide. Therefore, the improvement of the structure of the antibacterial peptide, the design of a class of antibacterial peptide with small molecular weight, strong antibacterial activity, high stability and safety and mass production is a key factor for realizing the clinical treatment by partially replacing antibiotics.
Disclosure of Invention
In view of this, the present invention aims to provide an antibacterial peptide L7 and its application, which has a small molecular weight, is safe and efficient, has a relatively low cost, and can provide a new therapeutic drug for resisting bacterial infection.
In order to achieve the purpose, the invention provides the following technical scheme:
1. the amino acid sequence of the antibacterial peptide L7 is RWKWFK, as shown in SEQ ID NO.1, the molecular weight is 1136.4Da, and the antibacterial peptide L7 can be synthesized by a polypeptide synthesizer according to the shown sequence.
2. The antibacterial peptide L7 is applied to the preparation of medicines for destroying bacterial cell membranes or inhibiting the formation of bacterial biofilms.
Preferably, the bacterium is a gram-negative or gram-positive bacterium.
3. The application of the antibacterial peptide L7 in preparing broad-spectrum antibacterial drugs for treating bacterial infections.
Preferably, the bacterium is a gram-negative or gram-positive bacterium.
The invention has the beneficial effects that:
the antibacterial peptide L7 designed and synthesized by the invention is an alpha helical cationic polypeptide, and has the characteristics of short peptide chain length, good stability, convenient manual synthesis and the like. The amino acid sequence of the antimicrobial peptide L7 was searched and aligned with NCBI protein database, and no identical polypeptide was found.
The antibacterial peptide L7 has broad-spectrum antibacterial activity and strong bactericidal effect, and can exert antibacterial effect by acting on cell membrane. In addition, the antibacterial peptide L7 can inhibit the formation of bacterial biofilms in a dose-dependent manner, has the characteristics of low hemolytic activity, low cytotoxicity and the like, and can be used as a new therapeutic drug for treating bacterial infections.
Drawings
In order to make the object, technical scheme and beneficial effect of the invention more clear, the invention provides the following drawings for explanation:
FIG. 1 is a transmission electron microscope observation of the effect of 1/4MIC antimicrobial peptide on cell morphology; wherein, (A) Pseudomonas aeruginosa ATCC27853 blank control group; (B) pseudomonas aeruginosa ATCC27853 antimicrobial peptide treated group; (C) staphylococcus aureus ATCC29213 blank control group; (D) staphylococcus aureus ATCC29213 antimicrobial peptide-treated group;
FIG. 2 shows the effect of sub-inhibitory concentrations of antimicrobial peptides on the ability of bacterial biofilms to form (P <0.05,. P <0.01vs. control), wherein A is Pseudomonas aeruginosa ATCC27853, B is Acinetobacter baumannii aba659, C is Staphylococcus aureus ATCC29213, and D is Staphylococcus epidermidis ATCC 35984;
FIG. 3 is the hemolytic activity of antimicrobial peptides on defibrinated sheep red blood cells;
fig. 4 shows the LDH release rate of the antibacterial peptide from human bronchial epithelial cells HBE.
Detailed Description
Preferred embodiments of the present invention will be described in detail below with reference to the accompanying drawings.
The standard strains used in the following examples of the present invention, Pseudomonas aeruginosa ATCC27853, Escherichia coli ATCC25922, Staphylococcus aureus ATCC29213, Staphylococcus epidermidis ATCC12228 and ATCC35984, were purchased from the American type culture Collection; the others are all clinical strains provided by the southwestern hospital clinical laboratory of army and military medical university. Human bronchial epithelial cells HBE were purchased from ATCC cell bank, usa. Defibrinated sheep blood, Triton X-100, was obtained from Beijing Solebao technologies, Inc., penicillin-streptomycin was obtained from Shanghai Biyuntian biotechnology, Inc., and fetal bovine serum was obtained from Hyclone, Inc., USA.
Example (b):
synthesis of antibacterial peptide L7
The antibacterial peptide L7 contains 7 amino acid residues, the sequence of the antibacterial peptide is arginine-tryptophan-lysine-tryptophan-phenylalanine-lysine, the fluorenylmethyloxycarbonyl (Fmoc) solid phase chemical synthesis method is adopted, the polypeptide (finished by Shanghai biological engineering Co., Ltd.) shown in SEQ ID NO.1 is synthesized one by one from the C end to the N end on a polypeptide synthesizer, the solid phase supporting agent is chloromethyl polystyrene resin, and the mobile phase is dimethylformamide/dichloromethane (volume ratio 1: 1). The synthetic peptide was purified by LC6000 HPLC (Inertsil ODS-SP 4.6 mm 250mm 5 μm) using a C18 column, and the peak of the product was collected to obtain L7 polypeptide with a purity of 97.0%, which was vacuum-dried, weighed, dispensed into 20 mg/bottle, and stored at-20 ℃ for further use. Mass spectrum identification is carried out, the molecular weight is 1136.4Da, and the result shows that ESI-MS M/z, 1137.5[ M + H ] and 569.25[ M +2H ], and the molecular ion peak of L7 is consistent with the expected result of synthesis.
Minimum Inhibitory Concentration (MIC) determination of antimicrobial peptide L7
The results of MIC of antibacterial peptide L7 to gram-positive bacteria and gram-negative bacteria were determined by broth dilution. The antimicrobial peptide was first dissolved in dimethyl sulfoxide and then diluted in MH broth in multiple 10 concentration gradients (512. mu.g/mL-1. mu.g/mL). The strain was streaked on a Columbia blood agar plate, cultured in a 37 ℃ incubator for 18 hours, diluted to 0.5 McLeod turbidimetric unit with physiological saline, and then diluted 1000-fold with MH broth. Adding 100 mu L of antibacterial peptide solution with serial concentrations into each hole of a 96-hole plate, and then adding 100 mu L of diluted bacterium solution into each hole to ensure that the final concentration of the medicine is 256 mu g/mL-0.5 mu g/mL; growth control wells were added with 100. mu.L MH broth and 100. mu.L of diluted bacterial solution. The 96-well plate was placed in a 37 ℃ incubator for 20 hours and MIC results were read, as detailed in table 1.
TABLE 1 antibacterial Activity of antibacterial peptide L7
As shown in table 1, the antimicrobial peptide L7 has strong antimicrobial activity against gram-negative bacteria (acinetobacter baumannii, pseudomonas aeruginosa, escherichia coli, klebsiella pneumoniae) and gram-positive bacteria (staphylococcus aureus, staphylococcus epidermidis, enterococcus) to be tested.
Effect of antimicrobial peptide L7 on bacterial cell morphology
Since 1/2MIC has an effect on bacterial growth, the invention adopts a transmission electron microscope to observe the effect of 1/4MIC antibacterial peptide on bacterial cell morphology. Single colonies of pseudomonas aeruginosa ATCC27853 and staphylococcus aureus ATCC29213 are respectively picked by using a sterile inoculating loop into 10mL of LB broth, and shake culture is carried out for 18 hours at 37 ℃ and 180rpm, so as to obtain bacterial liquid. Blank control 100. mu.L of the inoculum and 9.9mL of LB broth were added to an Erlenmeyer flask. 100 mu L of bacterial liquid, 100 mu L of antibacterial peptide and 9.8mL of LB broth are added into the antibacterial peptide group, so that the final concentration of the medicine reaches 1/4 MIC. After the samples were cultured with shaking at 37 ℃ and 180rpm for 18 hours, 1mL of each sample was centrifuged at 10000rpm for 15 minutes. Discarding the supernatant, adding 1mL of glutaraldehyde with the mass concentration of 2.5% for fixation, and then sending the fixed solution into an endoscope chamber for sample treatment, embedding, slicing and dyeing. And finally, observing and photographing by adopting a transmission electron microscope at 50000 times magnification.
As can be seen from FIG. 1, the cell structure of the Pseudomonas aeruginosa ATCC27853 blank control group is complete, the cytoplasm density is uniform, and a plurality of flagella can be seen around the periphery of the cells; the cytoplasm of the antibacterial peptide treated group is light in color, the cell membrane structure is loose, and no obvious flagella are seen outside the cells. The staphylococcus aureus ATCC29213 blank control group has an intact cell structure, and a large number of cells in the antibacterial peptide treatment group are swelled, broken and dead, and cytoplasm leaks outwards.
Effect of antimicrobial peptide L7 on bacterial biofilm formation
And detecting the forming capability of the bacterial biofilm by adopting a 96-pore plate crystal violet staining method. Single bacterial colonies were picked up in 10mL LB broth, and shake-cultured at 37 ℃ and 180rpm for 18 hours to obtain an overnight bacterial culture. The overnight culture of the bacteria was diluted 1000-fold with LB broth to obtain a diluted bacterial solution. The experiment is divided into a blank control group, an 1/4MIC antibacterial peptide group, a 1/8MIC antibacterial peptide group, a 1/16MIC antibacterial peptide group and a 1/32MIC antibacterial peptide group. Adding 100 mu L of antibacterial peptide and 100 mu L of diluted bacterial liquid into each hole of the drug treatment group; blank controls 100. mu.L LB broth and 100. mu.L of diluted broth per well were added. The samples were incubated at 37 ℃ for 24 hours. The planktonic bacteria were carefully removed, 200. mu.L of PBS buffer (pH 7.4) was added to each well, gently washed 2 times, and then placed in a ventilated and cool place and air-dried by inversion. Then adding 200 mu L of 1% crystal violet solution with mass concentration into each hole for dyeing for 10 minutes, removing the crystal violet solution, washing the holes with tap water until no obvious color is seen by naked eyes in blank control holes, and pouring the holes in a ventilated and cool place again for air drying. After air drying, 100 mu L of glacial acetic acid solution with the mass concentration of 30% is added into each hole, and the absorbance value is measured at the wavelength of 590nm of an enzyme-labeling instrument.
As can be seen from fig. 2, the antimicrobial peptides inhibited biofilm formation by gram-negative and gram-positive bacteria in a concentration-dependent manner, with 1/4MIC antimicrobial peptides having the strongest inhibitory ability against biofilm formation by bacteria.
Hemolytic Activity of antimicrobial peptide L7
Fresh sterile defibrinated sheep blood was centrifuged at 1000rpm for 10 minutes and the supernatant was discarded. The lower layer of red blood cells were washed 3 times with PBS buffer (pH 7.4), and finally a certain amount of sheep red blood cells were diluted with PBS to make a final concentration (mass concentration) of 3% diluted solution. 50 mu L of antibacterial peptide diluted by times is added into each hole of a 96-hole plate, and then 50 mu L of erythrocyte diluent is added, so that the final concentration of the antibacterial peptide is 8 mu g/mL-512 mu g/mL. Triton X-100 with a mass concentration of 1% was used as a positive control, and PBS buffer (pH 7.4) was used as a negative control. The 96-well plate was placed in a cell incubator, incubated at 37 ℃ for 30 minutes, centrifuged at 1000rpm for 5 minutes, and the supernatant was taken to measure the absorbance at 450 nm. The positive control group was set to 100% hemolysis rate, and the negative control group was set to 0% hemolysis rate. The hemolysis rate of the antimicrobial peptide is calculated by the formula: hemolysis rate (test group OD)450nmNegative control group OD450nm) /(Positive control OD450nmNegative control group OD450nm)*100％
From FIG. 3, it is understood that the hemolysis rate is slightly increased with the increase of the concentration of the antimicrobial peptide, but the hemolysis rate is not more than 5% at a concentration of 512. mu.g/mL, and therefore the antimicrobial peptide of the present invention is considered to have no hemolysis in the effective drug concentration range.
Cytotoxicity of antibacterial peptide L7
Human bronchial epithelial cells HBE are cultured in RPMI 1640 medium, and 10% by volume fetal bovine serum and 1% by volume penicillin-streptomycin are added at 37 deg.C and 5% by volume CO2Culturing in the environment. Diluting cultured HBE cells to 1 × 10 with culture medium6Cells were seeded at 90. mu.L/well in 96-well plates, and the 96-well plates were placed at 37 ℃ in 5% CO2After 4 hours of culture in the environment, 10. mu.L of antimicrobial peptides with different concentrations were added to the test groups to give final drug concentrations of 8. mu.g/mL-512. mu.g/mL, respectively. A background control well (100. mu.L of RPMI 1640 medium), a negative control well (90. mu.L of cell suspension + 10. mu.L of PBS), and a positive control well (90. mu.L of cell suspension + 10. mu.L of 20% Triton X-100) were also provided. CO 22After 24 hours of incubation in an incubator, positive control wells were formedAdding 10 mu L of Triton X-100 with the mass concentration of 20%, blowing and mixing uniformly by using a pipette, incubating for 15 minutes in an incubator, centrifuging, taking 60 mu L of cell supernatant from each well to a new 96-well plate, adding 30 mu L of diluted LDH detection reagent into each well, shaking and culturing for 30 minutes at room temperature in a dark place, and measuring the OD value at 490nm, wherein the LDH release rate is (△ OD test group- △ OD negative control group)/(△ OD positive control group- △ OD negative control group) × 100%
As shown in FIG. 4, the LDH release rate of the antibacterial peptide to HBE cells is less than 10% at a concentration of not more than 256. mu.g/mL, and less than 15% at a concentration of 512. mu.g/mL, which indicates that the cytotoxicity of the antibacterial peptide L7 is very low.
Finally, it is noted that the above-mentioned preferred embodiments illustrate rather than limit the invention, and that, although the invention has been described in detail with reference to the above-mentioned preferred embodiments, it will be understood by those skilled in the art that various changes in form and detail may be made therein without departing from the scope of the invention as defined by the appended claims.
Sequence listing
<110> first subsidiary hospital of China civil liberation army, military and medical university
<120> antibacterial peptide L7 and application thereof
<160>1
<170>SIPOSequenceListing 1.0
<210>1
<211>7
<212>PRT
<213> Artificial Sequence (Artificial Sequence)
<400>1
Arg Trp Trp Lys Trp Phe Lys
1 5
Claims (5)
1. The antibacterial peptide L7 is characterized in that the amino acid sequence of the antibacterial peptide L7 is RWKWFK, and is shown as SEQ ID NO. 1.
2. Use of the antibacterial peptide L7 of claim 1 in the preparation of a medicament for disrupting a bacterial cell membrane or inhibiting the formation of a bacterial biofilm.
3. Use according to claim 2, wherein the bacteria are gram-negative or gram-positive bacteria.
4. Use of the antimicrobial peptide L7 of claim 1 in the manufacture of a broad spectrum antimicrobial medicament for the treatment of bacterial infections.
5. Use according to claim 4, wherein the bacteria are gram-negative or gram-positive bacteria.
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Cited By (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN113024663A (en) * | 2021-03-05 | 2021-06-25 | 集美大学 | Arca granosa hemoglobin alpha helical antibacterial peptide and application thereof |
| CN113461781A (en) * | 2021-07-14 | 2021-10-01 | 中国药科大学 | Antibacterial peptide GS18 and application thereof |
| CN113896767A (en) * | 2021-09-27 | 2022-01-07 | 中国农业大学 | Self-assembled antibacterial peptide nanoparticles and application thereof |
| CN114634553A (en) * | 2022-04-27 | 2022-06-17 | 贵州医科大学 | Cationic peptide C9 and application thereof |
| CN115819516A (en) * | 2022-12-29 | 2023-03-21 | 中国人民解放军空军军医大学 | Polypeptide and application thereof |
| CN115850368A (en) * | 2022-07-05 | 2023-03-28 | 青岛大学 | Short-chain antibacterial peptide and application thereof |
| CN116813713A (en) * | 2023-07-31 | 2023-09-29 | 中国医学科学院医学生物学研究所 | Modified antibacterial peptide RI-18 and application thereof |
| CN116870132A (en) * | 2023-07-31 | 2023-10-13 | 中国医学科学院医学生物学研究所 | Antibacterial peptide RH-16 and application thereof in preparation of drug-resistant antibacterial drugs |
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| WO2015038339A1 (en) * | 2013-08-27 | 2015-03-19 | The University Of British Columbia | Small cationic anti-biofilm and idr peptides |
| CN104628829A (en) * | 2015-02-06 | 2015-05-20 | 浙江大学 | Antibacterial peptide WY-21 and application thereof |
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| WO2008022444A1 (en) * | 2006-08-21 | 2008-02-28 | The University Of British Columbia | Small cationic antimicrobial peptides |
| CN102432672A (en) * | 2011-12-13 | 2012-05-02 | 重庆理工大学 | Novel synthesis antibacterial peptides and application thereof |
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Cited By (14)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN113024663B (en) * | 2021-03-05 | 2022-08-05 | 集美大学 | Arca granosa hemoglobin alpha helical antibacterial peptide and application thereof |
| CN113024663A (en) * | 2021-03-05 | 2021-06-25 | 集美大学 | Arca granosa hemoglobin alpha helical antibacterial peptide and application thereof |
| CN113461781A (en) * | 2021-07-14 | 2021-10-01 | 中国药科大学 | Antibacterial peptide GS18 and application thereof |
| CN113896767A (en) * | 2021-09-27 | 2022-01-07 | 中国农业大学 | Self-assembled antibacterial peptide nanoparticles and application thereof |
| CN114634553B (en) * | 2022-04-27 | 2024-03-08 | 贵州医科大学 | Cationic peptide C9 and application thereof |
| CN114634553A (en) * | 2022-04-27 | 2022-06-17 | 贵州医科大学 | Cationic peptide C9 and application thereof |
| CN115850368A (en) * | 2022-07-05 | 2023-03-28 | 青岛大学 | Short-chain antibacterial peptide and application thereof |
| CN115850368B (en) * | 2022-07-05 | 2024-04-30 | 青岛大学 | Short-chain antibacterial peptide and application thereof |
| CN115819516A (en) * | 2022-12-29 | 2023-03-21 | 中国人民解放军空军军医大学 | Polypeptide and application thereof |
| CN115819516B (en) * | 2022-12-29 | 2024-04-16 | 中国人民解放军空军军医大学 | Polypeptide and application thereof |
| CN116813713A (en) * | 2023-07-31 | 2023-09-29 | 中国医学科学院医学生物学研究所 | Modified antibacterial peptide RI-18 and application thereof |
| CN116870132A (en) * | 2023-07-31 | 2023-10-13 | 中国医学科学院医学生物学研究所 | Antibacterial peptide RH-16 and application thereof in preparation of drug-resistant antibacterial drugs |
| CN116813713B (en) * | 2023-07-31 | 2024-04-19 | 中国医学科学院医学生物学研究所 | Modified antibacterial peptide RI-18 and application thereof |
| CN116870132B (en) * | 2023-07-31 | 2024-04-26 | 中国医学科学院医学生物学研究所 | Antibacterial peptide RH-16 and application thereof in preparation of drug-resistant antibacterial drugs |
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Application publication date: 20200324 |