CN104140458B - One kind cecropin antimicrobial peptides and application thereof - Google Patents
One kind cecropin antimicrobial peptides and application thereof Download PDFInfo
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- CN104140458B CN104140458B CN201410320218.5A CN201410320218A CN104140458B CN 104140458 B CN104140458 B CN 104140458B CN 201410320218 A CN201410320218 A CN 201410320218A CN 104140458 B CN104140458 B CN 104140458B
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4723—Cationic antimicrobial peptides, e.g. defensins
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Abstract
The invention discloses kind cecropin antimicrobial peptides and an application thereof, belong to technical field of molecular biology. Class cecropin antimicrobial peptides is made up of 31 amino acid, and its molecular weight is 3833.7Da. This antibacterial peptide can suppress the growth of the bacteriums such as staphylococcus aureus, fowl pasteurella multocida, Salmonella gallinarum and chicken colibacillosis, compared with the common antibiotics such as penicillin, streptomysin, brizolina, azithromycin, fungistatic effect is relatively better, with Cecropin? B, Cecropin? A, Cecropin? the cecropin antimicrobial peptides of the routines such as P1 is compared, and has stronger bacteriostatic activity. This antibacterial peptide is 625 μ g/mL to the minimal inhibitory concentration of Salmonella gallinarum, has good heat endurance simultaneously, in the research and development of antibiotic property medicine, has a good application prospect.
Description
Technical field
The present invention relates to a kind cecropin antimicrobial peptides, and the application of this antibacterial peptide, Protocols in Molecular Biology neck belonged toTerritory.
Background technology
Antibacterial peptide (Antibacterialpeptide) is to be lured through external condition by multiple biological cell specific gene codingThe small molecule polypeptide that artificial delivery is raw, molecular weight is 2000～7000Da, is made up of 20～60 amino acid residues. In the worldAn antibacterial peptide is found in 1980 by people such as Sweden scientist G.Boman from sky silkworm chrysalis. After this, people bacterium,In the multiple organisms such as fungi, plant, insect, amphibian animal, birds, fish, mammal and even the mankind, find also successivelySeparate multiple antibacterial peptide. Up to now, report that nearly more than 2000 kinds of antibacterial peptides are identified both at home and abroad, separate, with skyRight antibacterial peptide carries out artificial synthetic simulating peptide as template and has reached thousands of kinds. These antibacterial peptides have wide spectrum antibacterium, true mostlyBacterium, virus, protozoon and press down tumor killing cell isoreactivity, and in the innate immunity, also playing the part of key player, some antibacterial peptideThere is the chemical chemotactic, promotion wound healing, cell death inducing, the CKIs that regulate immunity, centrotaxis granulocyte, T cellMany-sided biological functions such as kinase c, inhibition corticotropin.
For a long time, use antibiotic medicine to cause medicament residue, bacterial drug resistance enhancing, body extensive, indiscriminatelyDegradation series of problems under autoimmunity, has brought great trouble and difficulty to the control of bacteriosis, also gives simultaneouslyThe mankind's health is brought potential threat. And the antibacterial peptide with the feature such as wide spectrum, efficient disease-resistance pathogenic microorganism is different from traditionAntibiotic medicine, its unique bactericidal mechanism makes bacterium be difficult for producing drug resistance, this is found to be, and to solve bacterium anti-to traditionRaw generally this thorny global difficult problem of drug resistance that benefit strengthens provides new approach, and prompting antibacterial peptide can be used as antibioticGood substitute 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 in field of biological pharmacyFocus. Along with deepening continuously of research, many antibacterial peptides are being developed to medicine, and wherein cecropin antimicrobial peptides is current researchThe clearest, the most obvious antibacterial peptide of effect. But, compared with traditional antibiotic, low, the antibacterial work of the yield of antibacterial peptides of natural originProperty is not ideal enough, and what have even exists cytotoxicity. Therefore, at the base that discloses antibacterial peptide structure-function relationship and mechanism of actionOn plinth, taking the good antibacterial peptide of character as template, existing antibacterial peptide is carried out artificial reconstructed and designs novel antimicrobial peptide molecule and becomeFor an important content of antibacterial peptide exploitation. Compared with the antibacterial peptide of natural origin, the antibacterial peptide of artificial design often has moreGood target cell specificity and antibacterial activity, and there is the spy such as low hemolytic activity and the hyposensitivity to proteasome degradation effectPoint. Therefore, exploitation have simple in structure, antibacterial activity is high, chemical synthesis is easy to antibacterial peptide becomes the exploitation of current antibacterialsUrgent 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 amino acid sequence is as shown in SEQIDNO.1. The molecular weight of antibacterial peptide is3833.7Da. Described antibacterial peptide comprises cecropin S-W-L-S-K-T-A-K-K-L-F antibacterial activity structure, is rich in arginine(Arg) and lysine (Lys), arginine (Arg) and lysine (Lys) residue are positively charged, can attract the negative electricity of bacterium surfaceLotus. Meanwhile, R-P-R-P-W-P-R-P basic structural unit forms bilateral hydrophobicity α-helixstructure.
Above-mentioned class cecropin antimicrobial peptides can be by artificial synthetic, and synthetic method or the gene engineering method of Solid-phase Polypeptide obtains.
The application of one kind cecropin antimicrobial peptides, comprises that class cecropin antimicrobial peptides is answering aspect preparation antibiotic property medicineWith. In antibiotic property medicine, class cecropin antimicrobial peptides can be made different pharmaceutical formulation according to a conventional method, as tablet, powder, injectionInjection etc. Class cecropin antimicrobial peptides is the Antibacterial Constituents of antibacterials, in medicine, and the content model of class cecropin antimicrobial peptidesEnclose is 0.2～50%.
Described bacterium is one in staphylococcus aureus, fowl pasteurella multocida, Salmonella gallinarum, chicken colibacillosisKind or multiple.
Concrete, the application of class cecropin antimicrobial peptides aspect the anti-Salmonella gallinarum medicine of preparation. Class cecropin antimicrobial peptidesEspecially good to the antibiotic property of Salmonella gallinarum, minimal inhibitory concentration is 625 μ g/mL, and after 121 DEG C of high temperature high pressure process still to chickenSalmonella has bacteriostasis, good thermal stability.
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, simultaneously with reference to CecropinP1 sterilizationFeature, design one kind cecropin antimicrobial peptides, is made up of 31 amino acid, and molecular weight is 3833.7Da. This antibacterial peptide can press downThe growth of the bacteriums such as staphylococcus aureus processed, Pasteurella, Salmonella gallinarum and chicken colibacillosis, with penicillin, streptomysin,The common antibiotics such as brizolina, azithromycin is compared, and fungistatic effect is relatively better, with CecropinB, CecropinA,The cecropin antimicrobial peptides of the routines such as CecropinP1 is compared, and has stronger bacteriostatic activity. This antibacterial peptide is to Salmonella gallinarumMinimal inhibitory concentration is 625 μ g/mL, and good thermal stability has before good application in the research and development of antibiotic property medicineScape.
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 result of the tests;
Fig. 2 is class cecropin antimicrobial peptides and common antibiotics In Vitro Bacteriostatic result of the test;
Fig. 3 is that class cecropin antimicrobial peptides is to salmonella minimal inhibitory concentration measurement result;
Fig. 4 is class cecropin antimicrobial peptides thermal stability determination result.
Detailed description of the invention
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 amino acid sequence is:SWLSKTAKKLFKKIPKKRFPRPRPWPRPNMI (shown in SEQIDNO.1), molecular weight is 3833.7Da. Described antibacterialPeptide comprises cecropin S-W-L-S-K-T-A-K-K-L-F antibacterial activity structure, is rich in arginine (Arg) and lysine (Lys), essencePropylhomoserin (Arg) and the positively charged negative electrical charge that attracts bacterium surface of lysine (Lys) residue. R-P-R-P-W-P-R-P simultaneouslyBasic structural unit forms bilateral hydrophobicity α-helixstructure.
In the present embodiment, class cecropin antimicrobial peptides adopts solid-phase synthesis synthetic by Chu Tai bio tech ltd, Shanghai,Purity is greater than 95%.
Embodiment 2
The application of class cecropin antimicrobial peptides aspect preparation antibiotic property medicine in the present embodiment, the amino acid of described antibacterial peptideSequence is: SWLSKTAKKLFKKIPKKRFPRPRPWPRPNMI, molecular weight is 3833.7Da. Adopt conventional method by class giant silkwormElement antibacterial peptide is made class cecropin circulin tablet, and every content of main ingredient class cecropin antimicrobial peptides is 0.2g, the quality of main ingredientPercentage composition is 50%, and auxiliary material is made up of starch, sucrose, talcum powder.
Embodiment 3
The application of class cecropin antimicrobial peptides aspect preparation antibiotic property medicine in the present embodiment, the amino acid of described antibacterial peptideSequence is: SWLSKTAKKLFKKIPKKRFPRPRPWPRPNMI, molecular weight is 3833.7Da. Adopt conventional method by class giant silkwormElement antibacterial peptide is made class cecropin circulin sodium chloride injection, and every 100mL parenteral solution is composed of the following components: main ingredient class skySbombycin antibacterial peptide 0.2g, sodium chloride 0.9g, surplus is water for injection.
Embodiment 4
The application of class cecropin antimicrobial peptides aspect preparation antibiotic property medicine in the present embodiment, the amino acid of described antibacterial peptideSequence is: SWLSKTAKKLFKKIPKKRFPRPRPWPRPNMI, molecular weight is 3833.7Da. Adopt conventional method by class giant silkwormElement antibacterial peptide is made class cecropin circulin glucose injection, and every 100mL parenteral solution is composed of the following components: class cecropinAntibacterial peptide 0.2g, 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 according to routine sideLegal system is standby. Select No. 1 qualitative filter paper of Xinhua, break into the roundlet scraps of paper that diameter is 6mm with card punch, scraps of paper paper using is bundled into bag, putsIn bottle or plate, in putting 100 DEG C of drying boxes again, 120 DEG C of sterilizing 15min dry. By the filter paper aseptic nipper of sterilizingStand is distributed in sterilizing plate, calculates taking every filter paper saturated water adsorptive value as 0.01mL, and 50 filter paper add dose 0.5mL, medicineThe 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 paperBe 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. RightThe dry of the penicillin scraps of paper should be used low-temperature vacuum drying method, puts into immediately bottle and jump a queue after being dried, and puts in drier and preserves, and also canBe placed in-20 DEG C of refrigerators. Make as stated above penicillin, streptomysin, azithromycin, brizolina, class cecropin antibacterialThe susceptibility sheet of peptide, for subsequent use in dress bottle.
The compound method of table 1 liquid
By staphylococcus aureus, fowl pasteurella multocida, Salmonella gallinarum and four kinds of Bacteria Culture of chicken colibacillosisTo logarithmic phase, get respectively tetra-kinds of bacterium logarithmic phase bacterium liquid of 100 μ L and evenly coat in 4 LB solid mediums, culture medium prescriptionAs follows: tryptone (Tryptone) 10g/L, yeast extract (Yeastextract) 5g/L, sodium chloride (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 of cultivations24h, observes and records result, sees the following form 2 and Fig. 1, and 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 Pasteurella, and " gold " represents staphylococcus aureus, and " chicken " represents chicken colibacillosis, " sandDoor " represent Salmonella gallinarum.
The antibacterial circle diameter of table 2 class cecropin antimicrobial peptides to four kinds of bacteriums
Result shows, class cecropin antimicrobial peptides to staphylococcus aureus, fowl pasteurella multocida, Salmonella gallinarum,Chicken colibacillosis all has stronger antibacterial activity.
(2) class cecropin antimicrobial peptides and the comparison of common antibiotics bacteriostatic activity
By staphylococcus aureus, fowl pasteurella multocida, Salmonella gallinarum and four kinds of Bacteria Culture of chicken colibacillosisTo 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), eachPut out to graze respectively in solid medium mycin, streptomysin, brizolina, azithromycin and class cecropin antimicrobial peptides susceptibility sheet (complied withInferiorly be labeled as 1,2,3,4,5) each one. By four flat boards be placed in 37 DEG C cultivate 24h, observe and record result, see the following form 3 and figureIn 2, Fig. 2, " bar " represents Pasteurella, and " gold " represents staphylococcus aureus, and " chicken " represents chicken colibacillosis, and " sand " represents chickenSalmonella, 1～5 represents penicillin, streptomysin, brizolina, azithromycin 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, streptomysin, brizolina and class cecropin antimicrobial peptides all have antibacterial to chicken colibacillosisEffect, a little less than the fungistatic effect of class cecropin antimicrobial peptides is compared with brizolina, with the fungistatic effect phase of penicillin, streptomysinPoor little; Only azithromycin and class cecropin antimicrobial peptides have bacteriostasis to salmonella, the antibacterial effect of class cecropin antimicrobial peptidesFruit relatively a little less than; Penicillin, streptomysin, brizolina and class cecropin antimicrobial peptides all have bacteriostasis, class to PasteurellaThe fungistatic effect of cecropin antimicrobial peptides is more or less the same compared with penicillin, streptomysin, brizolina, all stronger; Penicillin, chainMycin, brizolina, azithromycin and class cecropin antimicrobial peptides all have bacteriostasis to staphylococcus aureus, class cecropinThe fungistatic effect of antibacterial peptide is more or less the same compared with penicillin, streptomysin, brizolina, and is weaker than the antibacterial effect of azithromycinReally. Known in sum: class cecropin antimicrobial peptides all has inhibitory action to four kinds of bacteriums, and with antibiotic compare each bacterium press downBacterium effect is relatively better.
(3) class cecropin antimicrobial peptides and conventional cecropin antimicrobial peptides bacteriostatic activity comparison
For further illustrating class cecropin antimicrobial peptides antibacterial effect, by antibacterial to class cecropin antimicrobial peptides and conventional cecropinPeptide bacteriostatic activity compares. Select three kinds of conventional cecropin antimicrobial peptides, its amino acid sequence is as follows respectively:
CecropinA:KWKLFKKIEKVGQNIRDGIIKAGPAVAVVGQATQIAK (as shown in SEQIDNO.2);
CecropinB:KWKVFKKIEKMGRNIRNGIVKAGPAIAVLGEAKAL (as shown in SEQIDNO.3);
CecropinP1:SWLSKTAKKLENSAKKRISEGIAIAIQGGPR (as shown in SEQIDNO.4).
Above-mentioned antibacterial peptide adopts solid-phase synthesis synthetic by Chu Tai bio tech ltd, Shanghai, and purity is greater than95%. And prepare antibacterial peptide susceptibility sheet (the same) according to conventional method.
By staphylococcus aureus, fowl pasteurella multocida, Salmonella gallinarum and four kinds of Bacteria Culture of chicken colibacillosisTo logarithmic phase, get respectively tetra-kinds of bacterium logarithmic phase bacterium liquid of 100 μ L and evenly coat in 4 LB solid mediums, each LB solidIn culture medium, put respectively each one of CecropinA, CecropinB, CecropinP1 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, CecropinA, CecropinB and class cecropin antimicrobial peptides have bacteriostasis to chicken colibacillosis,The fungistatic effect of class cecropin antimicrobial peptides is relatively strong; Only CecropinB and class cecropin antimicrobial peptides have antibacterial to salmonellaEffect; Four kinds of antibacterial peptides all have bacteriostasis to fowl pasteurella multocida and staphylococcus aureus, but class cecropin is antibacterialPeptide is relatively strong to the fungistatic effect of fowl pasteurella multocida. Known in sum: class cecropin antimicrobial peptides and CecropinThe cecropin antimicrobial peptides of the routines such as B, CecropinA, CecropinP1 is compared, and has stronger bacteriostatic activity.
(3) class cecropin antimicrobial peptides minimal inhibitory concentration is measured (MIC)
The mensuration of minimal inhibitory concentration (MIC) and heat endurance selects salmonella to carry out. Get 11 test tubes, respectively numbering0～10,0.4g class 4mLLB fluid nutrient medium for cecropin antimicrobial peptides (containing agar powder) is fully dissolved in No. 1 pipe, itsIn his each test tube, add respectively 2mLLB fluid nutrient medium. With rifle head, sucking-off 2mL from No. 1 test tube injects No. 2 pipes, successively classesPush away, be diluted to pipe always No. 9, finally discard 2mL. Each dilution factor all needs to change rifle head. Adding 20mg class cecropin to No. 0 pipe resistsBacterium peptide, concentration is with No. 1 pipe, as aseptic contrast; Add 4mLLB fluid nutrient medium to No. 10 pipes, as contrasting without medicine. By thingFirst cultured salmonella bacterium liquid fully shakes up, and manages one of every pipe for 1～No. 10. Bacteria suspension approximately dilutes 100 times, and every milliliter containsThe 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 bacterial growth containing antibacterial peptideDilution factor, is MIC.
Result shows, 1～No. 5 pipe liquid clarification is similar to No. 0 pipe; And liquid in the test tube (comprising No. 6) after No. 6 pipesBody muddiness, similar to No. 10 pipes, there is bacterial growth. The MIC of class cecropin antimicrobial peptides is class cecropin antimicrobial peptides in No. 5 pipesConcentration, i.e. 625 μ g/mL.
(4) class cecropin antimicrobial peptides stability test
Get 3 test tubes, add respectively 2mLLB fluid nutrient medium (the same), and be labeled as " L ", " O ", " Φ ". " L " andIn " O " pipe, add respectively class cecropin antimicrobial peptides 10mg, fully concussion mixes, and " Φ " pipe is left intact. By 3 test tubes in121 DEG C of HIGH PRESSURE TREATMENT 20min. Prior cultured salmonella 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 trainingsSupport and spend the night, observed result 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, known class skySbombycin antibacterial peptide still has bacteriostasis to salmonella after 121 DEG C of HIGH PRESSURE TREATMENT, shows its good thermal stability.
Claims (5)
1. a kind cecropin antimicrobial peptides, is characterized in that: its amino acid sequence is as shown in SEQIDNO.1.
2. class cecropin antimicrobial peptides according to claim 1, is characterized in that: the molecular weight of described antibacterial peptide is3833.7Da。
3. an application for class cecropin antimicrobial peptides as claimed in claim 1, is characterized in that: described antibacterial peptide is anti-in preparationThe application of bacterium property medicine aspect; Described bacterium is that staphylococcus aureus, fowl pasteurella multocida, Salmonella gallinarum, chicken are largeOne or more in enterobacteria.
4. the application of class cecropin antimicrobial peptides according to claim 3, is characterized in that: described antibacterial peptide is anti-in medicineBacterium active component, its content is 0.2～50%.
5. the application of class cecropin antimicrobial peptides according to claim 3, is characterized in that: described antibacterial peptide is the anti-chicken of preparationThe application of salmonella medicine aspect.
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| CN116143885A (en) * | 2021-11-08 | 2023-05-23 | 中国药科大学 | Antibacterial peptide AMP3 with high antibacterial activity and application thereof |
| 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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| CN103484467A (en) * | 2013-09-11 | 2014-01-01 | 华南农业大学 | Diamondback moth cecropin 3, preparation method and application thereof |
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| WO2010141135A2 (en) * | 2009-03-05 | 2010-12-09 | Trustees Of Boston University | Bacteriophages expressing antimicrobial peptides and uses thereof |
| CN103484467A (en) * | 2013-09-11 | 2014-01-01 | 华南农业大学 | Diamondback moth cecropin 3, preparation method and application thereof |
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