CN104140458A - Para-cecropin antibacterial peptide and application thereof - Google Patents
Para-cecropin antibacterial peptide and application thereof Download PDFInfo
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- CN104140458A CN104140458A CN201410320218.5A CN201410320218A CN104140458A CN 104140458 A CN104140458 A CN 104140458A CN 201410320218 A CN201410320218 A CN 201410320218A CN 104140458 A CN104140458 A CN 104140458A
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- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
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Abstract
The invention discloses a para-cecropin antibacterial peptide and application thereof and belongs to the technical field of molecular biology. The para-cecropin antibacterial peptide consists of 31 amino acids and has the molecular weight of 3833.7Da. The antibacterial peptide can be used for inhibiting the growth of bacteria, such as staphylococcus aureus, avian pasteurella multocida, salmonella gallinarum and avian escherichia coli, has a better bacteriostasis effect compared with the commonly-used antibiotics, such as penicillin, streptomycin, cefazolin sodium and azithromycin, and has stronger bacteriostasis activity compared with the conventional cecropin antibacterial peptides, such as Cecropin B, Cecropin A and Cecropin P1. The antibacterial peptide has the minimum salmonella gallinarum bacteriostasis concentration of 625 micrograms per milliliter, has good thermal stability and has good application prospect in the research and development of antibacterial drugs.
Description
Technical field
The present invention relates to a kind cecropin antimicrobial peptides, and the application of this antibacterial peptide, technical field of molecular biology belonged to.
Background technology
Antibacterial peptide (Antibacterial peptide) is the small molecule polypeptide being produced through ambient conditions induction by multiple biomass cells specific gene coding, and molecular weight is 2000～7000Da, is made up of 20～60 amino-acid residues.First antibacterial peptide is found in 1980 by people such as Sweden scientist G.Boman from sky silkworm chrysalis in the world.After this, people find successively and have separated multiple antibacterial peptide in the multiple organisms such as bacterium, fungi, plant, insect, amphibian animal, birds, fish, Mammals and even the mankind.Up to now, report that nearly more than 2000 kinds of antibacterial peptides are identified both at home and abroad, separate, the simulating peptide of carrying out synthetic as template with natural antibacterial peptide has reached thousands of kinds.These antibacterial peptides mostly have wide spectrum antibacterium, fungi, virus, protozoon and press down tumor killing cell isoreactivity, and in the natural immunity, also playing the part of key player, some antibacterial peptide have regulate immunity, centrotaxis granulocyte, T cell chemical chemotactic, promote many-sided biological functions such as wound healing, cell death inducing, arrestin kinase c, inhibition thyroliberin.
For a long time, use antibiotic medicine to cause degradation series of problems under drug residue, bacterial drug resistance enhancing, body autoimmunity extensive, indiscriminately, bring great trouble and difficulty to the control of bacteriosis, bring potential threat also to the mankind's health simultaneously.And the antibacterial peptide with the feature such as wide spectrum, efficient disease-resistance pathogenic microorganism is different from traditional antibiotic medicine, its unique bactericidal mechanism makes bacterium be difficult for producing resistance, this is found to be and solves bacterium this thorny global difficult problem of resistance that traditional microbiotic is strengthened day by day new approach is provided, and prompting antibacterial peptide can be used as the substitute that microbiotic is good and is used widely clinically and will be trend of the times.
At present, antibacterial peptide has caused people's extensive concern, and its research and application have become the focus in field of biological pharmacy.Along with deepening continuously of research, many antibacterial peptides are being developed to medicine, and wherein cecropin antimicrobial peptides is to study at present the clearest, the most obvious antibacterial peptide of effect.But compared with traditional microbiotic, the yield of antibacterial peptides of natural origin is low, anti-microbial activity is not ideal enough, even there is cytotoxicity in what have.Therefore, disclosing on the basis of antibacterial peptide structure-function relationship and mechanism of action, taking the good antibacterial peptide of character as template, existing antibacterial peptide is being carried out to artificial reconstructed and design novel antimicrobial peptide molecule and become an important content of antibacterial peptide exploitation.Compared with the antibacterial peptide of natural origin, the antibacterial peptide of artificial design often has better target cell specificity and anti-microbial activity, and has the feature such as low hemolytic activity and the Wheat Protein to proteasome degradation effect.Therefore, exploitation have simple in structure, anti-microbial activity is high, chemosynthesis is easy to antibacterial peptide becomes current antibacterials and develop urgent demand.
Summary of the invention
The object of this invention is to provide a kind cecropin antimicrobial peptides.
Meanwhile, the present invention also provides the application of a kind cecropin antimicrobial peptides.
In order to realize above object, the technical solution adopted in the present invention is:
One kind cecropin antimicrobial peptides, its aminoacid sequence is as shown in SEQ ID NO.1.The molecular weight of antibacterial peptide is 3833.7Da.Described antibacterial peptide comprises cecropin S-W-L-S-K-T-A-K-K-L-F anti-microbial activity structure, be rich in arginine (Arg) and Methionin (Lys), arginine (Arg) and Methionin (Lys) residue are positively charged, can attract the negative charge of bacterium surface.Meanwhile, R-P-R-P-W-P-R-P basic structural unit forms bilateral hydrophobicity α-helixstructure.
Above-mentioned class cecropin antimicrobial peptides can pass through synthetic, and synthetic method or the gene engineering method of Solid-phase Polypeptide obtains.
The application of one kind cecropin antimicrobial peptides, comprises the application of class cecropin antimicrobial peptides aspect preparation germ resistance medicine.In germ resistance medicine, class cecropin antimicrobial peptides can be made different pharmaceutical formulation according to a conventional method, as tablet, powder, injection etc.Class cecropin antimicrobial peptides is the Antibacterial Constituents of antibacterials, and in medicine, the content range of class cecropin antimicrobial peptides is 0.2～50%.
Described bacterium is one or more in streptococcus aureus, fowl pasteurella multocida, Salmonella gallinarum, chicken colibacillosis.
Concrete, the application of class cecropin antimicrobial peptides aspect the anti-Salmonella gallinarum medicine of preparation.Class cecropin antimicrobial peptides is especially good to the germ resistance of Salmonella gallinarum, and minimal inhibitory concentration is 625 μ g/mL, and still Salmonella gallinarum is had to bacteriostatic action, good thermal stability after 121 DEG C of high temperature high pressure process.
Beneficial effect of the present invention:
The present invention is according to the feature of the mechanism of action of antibacterial peptide and amino acid composition, and simultaneously with reference to Cecropin P1 sterilization feature, design one kind cecropin antimicrobial peptides, is made up of 31 amino acid, and molecular weight is 3833.7Da.This antibacterial peptide can suppress the growth of the bacteriums such as streptococcus aureus, pasteurellosis bacillus, Salmonella gallinarum and chicken colibacillosis, compared with the common antibiotics such as penicillin, Streptomycin sulphate, cephazolin sodium, Azythromycin, fungistatic effect is relatively better, compared with the cecropin antimicrobial peptides conventional with Cecropin B, Cecropin A, Cecropin P1 etc., there is stronger bacteriostatic activity.This antibacterial peptide is 625 μ g/mL to the minimal inhibitory concentration of Salmonella gallinarum, and good thermal stability has a good application prospect in the research and development of germ resistance medicine.
Brief description of the drawings
Fig. 1 be in test example 1 of the present invention class cecropin antimicrobial peptides to four kinds of bacterium In Vitro Bacteriostatic test-results;
Fig. 2 is class cecropin antimicrobial peptides and common antibiotics In Vitro Bacteriostatic test-results;
Fig. 3 is that class cecropin antimicrobial peptides is to Salmonellas minimal inhibitory concentration measurement result;
Fig. 4 is class cecropin antimicrobial peptides thermal stability determination result.
Embodiment
Following embodiment is only described in further detail the present invention, but does not form any limitation of the invention.
Embodiment 1
Class cecropin antimicrobial peptides in the present embodiment, its aminoacid sequence is: SWLSKTAKKLFKKIPKKRFPRPRPWPRPNMI (shown in SEQ ID NO.1), molecular weight is 3833.7Da.Described antibacterial peptide comprises cecropin S-W-L-S-K-T-A-K-K-L-F anti-microbial activity structure, be rich in arginine (Arg) and Methionin (Lys), arginine (Arg) and the positively charged negative charge that attracts bacterium surface of Methionin (Lys) residue.R-P-R-P-W-P-R-P basic structural unit forms bilateral hydrophobicity α-helixstructure simultaneously.
In the present embodiment, class cecropin antimicrobial peptides adopts solid-phase synthesis synthetic by Chu Tai bio tech ltd, Shanghai, and purity is greater than 95%.
Embodiment 2
The application of class cecropin antimicrobial peptides aspect preparation germ resistance medicine in the present embodiment, the aminoacid sequence of described antibacterial peptide is: SWLSKTAKKLFKKIPKKRFPRPRPWP RPNMI, molecular weight is 3833.7Da.Adopt ordinary method that class cecropin antimicrobial peptides is made to class cecropin circulin tablet, every content of main ingredient class cecropin antimicrobial peptides is 0.2g, and the quality percentage composition of main ingredient is 50%, and auxiliary material is made up of starch, sucrose, talcum powder.
Embodiment 3
The application of class cecropin antimicrobial peptides aspect preparation germ resistance medicine in the present embodiment, the aminoacid sequence of described antibacterial peptide is: SWLSKTAKKLFKKIPKKRFPRPRPWP RPNMI, molecular weight is 3833.7Da.Adopt ordinary method that class cecropin antimicrobial peptides is made to class cecropin circulin sodium chloride injection, every 100mL injection liquid is composed of the following components: main ingredient class cecropin antimicrobial peptides 0.2g, and sodium-chlor 0.9g, surplus is water for injection.
Embodiment 4
The application of class cecropin antimicrobial peptides aspect preparation germ resistance medicine in the present embodiment, the aminoacid sequence of described antibacterial peptide is: SWLSKTAKKLFKKIPKKRFPRPRPWP RPNMI, molecular weight is 3833.7Da.Adopt ordinary method that class cecropin antimicrobial peptides is made to class cecropin circulin glucose injection, every 100mL injection liquid is composed of the following components: class cecropin antimicrobial peptides 0.2g, and glucose 5g, surplus is water for injection.
Test example
(1) class cecropin antimicrobial peptides In Vitro Bacteriostatic test
Adopt paper disk method to measure the In Vitro Bacteriostatic of class cecropin antimicrobial peptides.In paper disk method, drug sensitive test paper is prepared according to ordinary method.Select No. 1 qualitative filter paper of Xinhua, break into the roundlet scraps of paper that diameter is 6mm with punch tool, scraps of paper paper using is bundled into bag, is placed in bottle or plate, in 120 DEG C of sterilizing 15min put 100 DEG C of loft drier again, dries.The filter paper of sterilizing is distributed in sterilizing plate with aseptic nipper stand, calculates taking every filter paper saturated water adsorptive value as 0.01mL, 50 filter paper add dose 0.5mL, and the compound method of liquid sees the following form 1.Otherwise in time, is stirred, make filter paper fully absorb liquid, generally soak 30min, take out the pastille scraps of paper and be put in gauze bag, make it dry with vacuum air pump, or the scraps of paper are spread out in 37 DEG C of incubators and dried, in case drug failure.Should use low-temperature vacuum drying method to the dry of the penicillin scraps of paper, after being dried, put into immediately bottle and jump a queue, put in moisture eliminator and preserve, also can be placed in-20 DEG C of refrigerators.Make as stated above the susceptibility sheet of penicillin, Streptomycin sulphate, Azythromycin, cephazolin sodium, class cecropin antimicrobial peptides, for subsequent use in dress bottle.
The compound method of table 1 liquid
By streptococcus aureus, fowl pasteurella multocida, Salmonella gallinarum and four kinds of microbial culture of chicken colibacillosis to logarithmic phase, getting respectively tetra-kinds of bacterium logarithmic phase bacterium liquid of 100 μ L evenly coats in 4 LB solid mediums, culture medium prescription is as follows: Tryptones (Tryptone) 10g/L, yeast extract (Yeast extract) 5g/L, sodium-chlor (NaCl) 10g/L, agar powder 10g.In each LB solid medium, put a class cecropin antimicrobial peptides susceptibility sheet.Four flat boards are placed in to 37 DEG C and cultivate 24h, observe and record result, see the following form 2 and Fig. 1, in Fig. 1, class cecropin antimicrobial peptides susceptibility sheet is all affixed on each culture dish central authorities, do not make special sign, " bar " represents pasteurellosis bacillus, and " gold " represents streptococcus aureus, " chicken " represents chicken colibacillosis, and " sramana " represents Salmonella gallinarum.
The antibacterial circle diameter of table 2 class cecropin antimicrobial peptides to four kinds of bacteriums
Result demonstration, class cecropin antimicrobial peptides all has stronger anti-microbial activity to streptococcus aureus, fowl pasteurella multocida, Salmonella gallinarum, chicken colibacillosis.
(2) class cecropin antimicrobial peptides and the comparison of common antibiotics bacteriostatic activity
By streptococcus aureus, fowl pasteurella multocida, Salmonella gallinarum and four kinds of microbial culture of chicken colibacillosis to logarithmic phase, get respectively tetra-kinds of bacterium logarithmic phase bacterium liquid of 100 μ L and evenly coat in 4 LB solid mediums (the same), each one of the mycin of putting out to graze respectively in each solid medium, Streptomycin sulphate, cephazolin sodium, Azythromycin and class cecropin antimicrobial peptides susceptibility sheet (being labeled as successively 1,2,3,4,5).Four flat boards are placed in to 37 DEG C and cultivate 24h, observe and record result, see the following form 3 and Fig. 2, in Fig. 2, " bar " represents pasteurellosis bacillus, " gold " represents streptococcus aureus, " chicken " represents chicken colibacillosis, and " sand " represents Salmonella gallinarum, and 1～5 represents penicillin, Streptomycin sulphate, cephazolin sodium, Azythromycin and class cecropin antimicrobial peptides successively.
Table 3 class cecropin antimicrobial peptides and the common antibiotics antibacterial circle diameter to four kinds of bacteriums
Result demonstration, penicillin, Streptomycin sulphate, cephazolin sodium and class cecropin antimicrobial peptides all have bacteriostatic action to chicken colibacillosis, a little less than the fungistatic effect of class cecropin antimicrobial peptides is compared with cephazolin sodium, are more or less the same with the fungistatic effect of penicillin, Streptomycin sulphate; Only Azythromycin and class cecropin antimicrobial peptides have bacteriostatic action to Salmonellas, the fungistatic effect of class cecropin antimicrobial peptides relatively a little less than; Penicillin, Streptomycin sulphate, cephazolin sodium and class cecropin antimicrobial peptides all have bacteriostatic action to pasteurellosis bacillus, and the fungistatic effect of class cecropin antimicrobial peptides is more or less the same compared with penicillin, Streptomycin sulphate, cephazolin sodium, all stronger; Penicillin, Streptomycin sulphate, cephazolin sodium, Azythromycin and class cecropin antimicrobial peptides all have bacteriostatic action to streptococcus aureus, the fungistatic effect of class cecropin antimicrobial peptides is more or less the same compared with penicillin, Streptomycin sulphate, cephazolin sodium, and is weaker than the fungistatic effect of Azythromycin.Known in sum: class cecropin antimicrobial peptides all has restraining effect to four kinds of bacteriums, and to compare each bacterium fungistatic effect relative better with microbiotic.
(3) class cecropin antimicrobial peptides and conventional cecropin antimicrobial peptides bacteriostatic activity comparison
For further illustrating class cecropin antimicrobial peptides antibacterial effect, class cecropin antimicrobial peptides and conventional cecropin antimicrobial peptides bacteriostatic activity are compared.Select three kinds of conventional cecropin antimicrobial peptides, its aminoacid sequence is as follows respectively:
Cecropin A:KWKLFKKIEKVGQNIRDGIIKAGPAVAVVGQATQIAK (as shown in SEQ ID NO.2);
Cecropin B:KWKVFKKIEKMGRNIRNGIVKAGPAIAVLGEAKAL (as shown in SEQ ID NO.3);
Cecropin P1:SWLSKTAKKLENSAKKRISEGIAIAIQGGPR (as shown in SEQ ID NO.4).
Above-mentioned antibacterial peptide adopts solid-phase synthesis synthetic by Chu Tai bio tech ltd, Shanghai, and purity is greater than 95%.And prepare antibacterial peptide susceptibility sheet (the same) according to ordinary method.
By streptococcus aureus, fowl pasteurella multocida, Salmonella gallinarum and four kinds of microbial culture of chicken colibacillosis to logarithmic phase, get respectively tetra-kinds of bacterium logarithmic phase bacterium liquid of 100 μ L and evenly coat in 4 LB solid mediums, in each LB solid medium, put respectively each one of Cecropin A, Cecropin B, Cecropin P1 and class cecropin antimicrobial peptides susceptibility sheet.Four flat boards are placed in to 37 DEG C and cultivate 24h, observe and record the antibacterial result of every kind of antibacterial peptide, see the following form 4.
Table 4 class cecropin antimicrobial peptides and the conventional cecropin antimicrobial peptides antibacterial circle diameter to four kinds of bacteriums
Result demonstration, Cecropin A, Cecropin B and class cecropin antimicrobial peptides have bacteriostatic action to chicken colibacillosis, and the fungistatic effect of class cecropin antimicrobial peptides is relatively strong; Only Cecropin B and class cecropin antimicrobial peptides have bacteriostatic action to Salmonellas; Four kinds of antibacterial peptides all have bacteriostatic action to fowl pasteurella multocida and streptococcus aureus, but class cecropin antimicrobial peptides is relatively strong to the fungistatic effect of fowl pasteurella multocida.Known in sum: compared with the conventional cecropin antimicrobial peptides such as class cecropin antimicrobial peptides and Cecropin B, Cecropin A, Cecropin P1, to there is stronger bacteriostatic activity.
(3) class cecropin antimicrobial peptides minimal inhibitory concentration is measured (MIC)
The mensuration of minimal inhibitory concentration (MIC) and thermostability selects Salmonellas to carry out.Get 11 test tubes, number respectively 0～10,4mL LB liquid nutrient medium for 0.4g class cecropin antimicrobial peptides (not containing agar powder) is fully dissolved in No. 1 pipe, in other each test tubes, add respectively 2mL LB liquid nutrient medium.With rifle head, sucking-off 2mL from No. 1 test tube injects No. 2 pipes, the like, be diluted to pipe No. 9 always, finally discard 2mL.Each extent of dilution all needs to change rifle head.Add 20mg class cecropin antimicrobial peptides to No. 0 pipe, concentration is with No. 1 pipe, as aseptic contrast; Add 4mL LB liquid nutrient medium to No. 10 pipes, as contrasting without medicine.Prior cultured Salmonellas bacterium liquid is fully shaken up, manage one of every pipe for 1～No. 10.Bacteria suspension approximately dilutes 100 times, and every milliliter containing the about 105cfu of bacterium.Test tube is placed in to 37 DEG C of overnight incubation, and sentence read result, is shown in Fig. 3.Minimum and without the extent of dilution of bacterial growth, be MIC containing antibacterial peptide.
Result shows, 1～No. 5 pipe liquid clarification is similar to No. 0 pipe; And liquid muddiness in the test tube (comprising No. 6) after No. 6 pipes is similar to No. 10 pipes, there is bacterial growth.The MIC of class cecropin antimicrobial peptides is the concentration of class cecropin antimicrobial peptides in No. 5 pipes, i.e. 625 μ g/mL.
(4) class cecropin antimicrobial peptides stability test
Get 3 test tubes, add respectively 2mL LB liquid nutrient medium (the same), and be labeled as " L ", " O ", " Φ ".In " L " and " O " pipe, add respectively class cecropin antimicrobial peptides 10mg, fully concussion mixes, and " Φ " pipe is left intact.By 3 test tubes in 121 DEG C of autoclaving 20min.Prior cultured Salmonellas bacterium liquid is fully mixed, in " L " and " Φ " pipe, respectively add 1.Bacteria suspension approximately dilutes 100 times, and every milliliter containing the about 105cfu of bacterium." O " pipe is left intact.By 3 test tubes, in 37 DEG C of overnight incubation, observations record, be shown in Fig. 4.
Result shows, relatively 3 test tubes, and the clarification of " L " and " O " pipe, " Φ " manages muddy, has bacterial growth, and known class cecropin antimicrobial peptides still has bacteriostatic action to Salmonellas after 121 DEG C of autoclaving, shows its good thermal stability.
Claims (6)
1. a kind cecropin antimicrobial peptides, is characterized in that: its aminoacid sequence is as shown in SEQ ID NO.1.
2. class cecropin antimicrobial peptides according to claim 1, is characterized in that: the molecular weight of described antibacterial peptide is 3833.7Da.
3. an application for class cecropin antimicrobial peptides as claimed in claim 1, is characterized in that: the application of described antibacterial peptide aspect preparation germ resistance medicine.
4. the application of class cecropin antimicrobial peptides according to claim 3, is characterized in that: described antibacterial peptide is Antibacterial Constituents in medicine, and its content is 0.2～50%.
5. the application of class cecropin antimicrobial peptides according to claim 3, is characterized in that: described bacterium is one or more in streptococcus aureus, fowl pasteurella multocida, Salmonella gallinarum, chicken colibacillosis.
6. the application of class cecropin antimicrobial peptides according to claim 5, is characterized in that: the application of described antibacterial peptide aspect the anti-Salmonella gallinarum medicine of preparation.
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Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
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| CN109266655A (en) * | 2018-09-06 | 2019-01-25 | 浙江大学 | A kind of antibacterial peptide and its prokaryotic expression method and application |
| CN112575581A (en) * | 2020-12-29 | 2021-03-30 | 湖南寐家居科技有限公司 | Antibacterial finishing agent for silk fabric and preparation method thereof |
| CN113912680A (en) * | 2021-11-08 | 2022-01-11 | 中国药科大学 | Antibacterial peptide with high antibacterial activity and application thereof |
| CN116621939A (en) * | 2023-05-17 | 2023-08-22 | 吉林农业大学 | Application of antibacterial peptide LRGG in preparation of fluoroquinolone antibacterial synergist |
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Cited By (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN109266655A (en) * | 2018-09-06 | 2019-01-25 | 浙江大学 | A kind of antibacterial peptide and its prokaryotic expression method and application |
| CN109266655B (en) * | 2018-09-06 | 2021-11-09 | 浙江大学 | Antibacterial peptide and prokaryotic expression method and application thereof |
| CN112575581A (en) * | 2020-12-29 | 2021-03-30 | 湖南寐家居科技有限公司 | Antibacterial finishing agent for silk fabric and preparation method thereof |
| CN113912680A (en) * | 2021-11-08 | 2022-01-11 | 中国药科大学 | Antibacterial peptide with high antibacterial activity and application thereof |
| CN116621939A (en) * | 2023-05-17 | 2023-08-22 | 吉林农业大学 | Application of antibacterial peptide LRGG in preparation of fluoroquinolone antibacterial synergist |
| CN116621939B (en) * | 2023-05-17 | 2024-01-19 | 吉林农业大学 | Application of antibacterial peptide LRGG in preparation of fluoroquinolone antibacterial synergist |
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