CN106749532A - Multiply β hair fasteners small peptide and preparation method and application with tolerance protein enzyme - Google Patents
Multiply β hair fasteners small peptide and preparation method and application with tolerance protein enzyme Download PDFInfo
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- CN106749532A CN106749532A CN201611059715.XA CN201611059715A CN106749532A CN 106749532 A CN106749532 A CN 106749532A CN 201611059715 A CN201611059715 A CN 201611059715A CN 106749532 A CN106749532 A CN 106749532A
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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
- C07K7/08—Linear peptides containing only normal peptide links having 12 to 20 amino acids
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- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
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Abstract
The present invention provides a kind of multiply β hair fasteners small peptide and preparation method and application with tolerance protein enzyme, and its sequence is as shown in sequence table SEQ ID No.1.The present invention gives full play to β hairpin structure structural advantages, obtain multiply β hairpin structure antibacterial peptides, further improve stability while ensureing activity using common amino, and change the composition of corner amino acid, finally give a series of multiply β hair fastener antibacterial peptides of brand news：(WRXxRW) n NH2, wherein n=1,2,3,4；PG is chosen for corner is illustrated, as n=2, antibacterial peptide is named as W2；As n=3, antibacterial peptide is named as W3.The peptide shows cell selective and salt ion tolerance higher, also, on the basis of Stability Analysis of Structures antibacterial peptide activity, because gained antibacterial peptide is shorter, also shows the tolerance of stronger vivo protein enzyme.
Description
Technical field
The invention belongs to biological technical field, and in particular to a kind of multiply β-hair fastener small peptide and system with tolerance protein enzyme
Preparation Method and application.
Background technology
Antibiotic is formally approved as since additive applies in feed, not only having effectively reduced disease from nineteen fifty
Infection rate, improve the survival rate of piglet, also show it is obvious promote growth of animal, improve feedstuff-meat ratio, improve breeding
The superperformances such as rate.However, since vancomycin-resistant bacteria in 1996 is since Japan finds, caused by the abuse of antibiotic
The increase of antibody-resistant bacterium, and its caused livestock and poultry immunity of organisms decline takes place frequently with animal and bird intestines flora is unbalance, in recent years
A series of problems, such as appearance of superbacteria etc. so that people much surpass for the degree of concern of the harm of antibiotic resistance
The economic benefit of its generation is crossed.Therefore, the novel antibacterial medicines different from the antibiotic mechanism of action are searched out extremely urgent.
In past decades, people research and develop the substitute products of a large amount of feeding antibiotics, wherein the exploitation of antibacterial peptide be developed into
It is the study hotspot of animal husbandry.
Antibacterial peptide is the extraneous pathogen invasion of animal body natural immune system resistance, detrimental mutation cell in removing machine body
Small molecule polypeptide, and itself be protein, with the characteristic such as noresidue, pollution-free, along with heat endurance is good, add
Plus dosage it is small the advantages of, comply fully with the need for livestock products green safety produces, also, antibacterial peptide can effectively improve piglet pair
The resistance of diarrhoea and breathing problem, is adapted to be used in feed preparation.And the antifungal mechanism and antibiosis of antibacterial peptide
Plain different, antibacterial peptide is intracellular molten beyond the region of objective existence is let out so as to kill cell by destroying the cell membrane of bacterium, so bacterium is difficult
Produce drug resistance.What is more important, antibacterial peptide is not almost acted on eukaryotic, acts only on prokaryotic and disease occurs
The eukaryotic of change.Substitution antibiotic is entirely possible to according to above-mentioned reason antibacterial peptide and turn into a new, efficient class, low toxicity, nothing
The antibacterial material of residual, has broad application prospects.But natural cationic antibacterial peptide is not flawless, most of day
Right antibacterial peptide has antibacterial activity, and strong, antimicrobial spectrum relative narrower, relatively costly, the part antibacterial peptide of synthesis do not have one to eucaryote
Fixed toxicity, it is usually associated with while with killing activity high to pathogenic microorganism to Eukaryotic haemocylolysis and right
The deficiencies such as protease-sensitive.Therefore how to improve its activity and at utmost reduce its toxicity and keep its effect in vivo steady
The qualitative purpose as antibacterial peptide molecular modification is also the difficult point of current antimicrobial peptide medicaments exploitation and wishes place.
The content of the invention
It is an object of the invention to provide a kind of multiply β-hair fastener small peptide with tolerance protein enzyme and preparation method and should
With；The antibacterial peptide has selectively acting higher to Gram-negative bacteria and gram-positive bacteria, with more the resistance to of protease
By ability.
The purpose of the present invention is realized by following technology：A kind of multiply β with tolerance protein enzyme-hair fastener small peptide W2, its
Sequence is as shown in sequence table SEQ ID No.1.
The present invention also has following technical characteristic：
1st, a kind of preparation method of the multiply β with tolerance protein enzyme-hair fastener small peptide W2 is as follows：
(1) wherein the lamella area of each β-hairpin structure is constituted using common amino Trp, Arg, it is ensured that while active
Further improve stability, and change the composition of corner amino acid, finally give the multiply β-hair fastener antibacterial peptide of brand new：
(WRXxRW) n-NH2, it is L-type proline and glycine to choose wherein corner, and as n=2, antibacterial peptide is named as W2, and sequence is such as
Shown in sequence table SEQ ID No.1；
(2) peptide resin is obtained by Peptide synthesizer using solid-state chemical reaction method method, the peptide resin that will be obtained is cut by TFA
After cutting, two polypeptides are obtained；
(3) by after RPLC purifying and Mass Spectrometric Identification, that is, completing the preparation of polypeptide.
3rd, a kind of multiply β with tolerance protein enzyme-hair fastener small peptide W2 as described above, in treatment Gram-negative bacteria and
Application in gram positive bacteria infection disease medicament.
The experimental technique of the antibacterial peptide prepared by this method is simple, and Stability Analysis of Structures, and the antibacterial peptide to obtaining is carried out
Antibacterial and hemolytic activity detect that small peptide W2 is to Escherichia coli, salmonella typhimurium, staphylococcus aureus, withered grass bud for discovery
Various strains such as spore bacillus have obvious inhibitory action, and with very low hemolytic activity, the peptide shows cell higher
Selectivity and salt ion tolerance, also, on the basis of Stability Analysis of Structures antibacterial peptide activity, because gained antibacterial peptide is shorter,
Show the tolerance of stronger vivo protein enzyme.In sum, small peptide W2 is a kind of antibacterial peptide with application value higher.
Brief description of the drawings
Fig. 1 is the mass spectrogram of antibacterial peptide W2.
Specific embodiment
With reference to embodiment and accompanying drawing, the present invention is described in further detail, but embodiments of the present invention are not limited
In this.
Embodiment 1
The design of antibacterial peptide
Having the excellent results of more preferable antibacterial activity and cell selective according to β-hairpin structure, and increase number has
Beneficial to stability is improved, this method gives full play to β-hairpin structure structural advantage, obtains multiply β-hairpin structure antibacterial peptide, wherein
Using common amino acid Trp, Arg ensures further to improve stability while activity, and changes the composition of corner amino acid,
A series of multiply β-hair fastener antibacterial peptide of brand news is finally given：(WRXxRW) n-NH2, wherein n=1,2,3,4；Choose
PG is illustrated for corner, and as n=2, antibacterial peptide is named as W2；As n=3, antibacterial peptide is named as W3；Its amino acid sequence
As shown in table 1.
The amino acid sequence of the derived peptide of table 1
The charge number of W2 and W3 is respectively+5 and+7.By W2, two terminal-carboxy amidations of peptide of W3 are improving one just
Electric charge simultaneously increases the stability of peptide.By the method in the case where antiseptic peptide stability and bactericidal activity is improved, reduce anti-
The hemolytic activity of bacterium peptide, improves selectivity of the antibacterial peptide between bacterial cell and mammalian cell, and improve it turns into
The development potentiality of antibiotic substitute.
Embodiment 2
Solid-state chemical reaction method method synthesizes two antibacterial peptides of W2 and W3
1st, the preparation of antibacterial peptide is carried out one by one from C-terminal to N-terminal, is completed by Peptide synthesizer.First by Fmoc-X (X
It is first amino acid of C-terminal of each antibacterial peptide) Wang resins are linked into, obtain X-Wang trees after then sloughing Fmoc groups
Fat；Again by Fmoc-Y-Trt-OH (9- fluorenes methoxy carboxyl-trimethyl-Y, Y is second amino acid of each antibacterial peptide C-terminal)；According to
This program is synthesized to N-terminal from C-terminal successively, until synthesis is finished, the resin of the side chain protected for obtaining sloughing Fmoc groups；
2nd, in peptide resin obtained above, cutting reagent is added, 2h is reacted under 20 DEG C of lucifuges, filtered；Precipitation TFA (three
Fluoroacetic acid) washing, washing lotion is mixed with above-mentioned filtrate, Rotary Evaporators concentration, the precooling for adding 10 times or so volumes is anhydrous
Ether, -20 DEG C of precipitation 3h, separates out white powder thing, and 10min is centrifuged with 2500g, collects precipitation, then wash heavy with absolute ether
Form sediment, vacuum drying obtains polypeptide, wherein cutting reagent by TFA, water and TIS (tri isopropyl chlorosilane) according to mass ratio 95:
2.5:2.5 mix；
3rd, column equilibration 30min is carried out using 0.2mol/L sodium sulphate (phosphoric acid is adjusted to pH7.5), uses 90% acetonitrile solution
Dissolving polypeptide, filtering, the anti-phase normal pressure posts of C18, (eluant, eluent is methyl alcohol and aqueous sodium persulfate solution according to volume ratio to use gradient elution
It is 30:70~70:30 mixing), flow velocity is 1mL/min, and detection ripple is 220nm, collects main peak, is freezed；Recycle anti-phase C18 posts
It is further purified, eluent A is the 0.1%TFA/ aqueous solution；Eluent B is 0.1%TFA/ acetonitrile solutions, and wash-out concentration is 25%
B~40%B, elution time is 12min, and flow velocity is 1mL/min, then ibid collects main peak, is freezed；
4th, the identification of antibacterial peptide：Antibacterial peptide obtained above is analyzed by electron spray mass spectrometry, the purity of antibacterial peptide is big
In 95%.
Embodiment 3：The measure of antibacterial peptide antibacterial activity
1st, the measure of antibacterial activity：Peptide is configured as certain storing liquid in case using.Surveyed using micro broth dilution method
The minimal inhibitory concentration of fixed several antibacterial peptides.Doubling dilution, as dilution, is used using 0.01% acetic acid (containing 0.2%BSA)
The antibacterial peptide solution of graded series is configured successively.Take the μ L of above-mentioned solution 100 to be placed in 96 porocyte culture plates, then add respectively
Isometric bacterium solution to be measured (~105Individual/mL) in each hole.It is respectively provided with positive control (antibacterial peptide is not contained containing bacterium solution)
With negative control (both without bacterium solution or without peptide).37 DEG C of incubated 20h, with naked eyes have no bottom hole portion have research of chaotic phenomenon i.e.
It is minimal inhibitory concentration.Testing result is as shown in table 2.
The bacteriostatic activity of the antibacterial peptide of table 2
It can be seen from Table 2 that, W2 and W3 is fine for the fungistatic effect of Gram-negative bacteria and gram-positive bacteria,
And the peptide chain length of W2 is shorter, in hgher efficiency, therefore W2 has the potentiality for turning into antibacterials of new generation.
2nd, the measure of hemolytic activity：The new blood 1mL of people is gathered, is dissolved into after anticoagulant heparin in 2mLPBS solution,
1000g is centrifuged 5min, collects red blood cell；Washed with PBS 3 times, then it is resuspended with 10mL PBS；Take 50 μ L red cell suspensions and 50 μ L
The antibacterial peptide solution of the various concentrations dissolved with PBS is well mixed, the constant-temperature incubation 1h in 37 DEG C of incubators；Taken out after l h, 4
DEG C, 1000g centrifugation 5min；Take out supernatant ELIASA light-metering absorption value at 570nm；Every group is averaged, and is compared point
Analysis.Wherein 50 μ L red blood cells add 50 μ LPBS as negative control；50 μ L red blood cells add 50 μ L0.1%Tritonx-100 as sun
Property control.Minimum hemolytic concentration is antibacterial peptide concentration when antibacterial peptide causes 10% hemolysis rate.Testing result is as shown in table 3.
The measure of the antibacterial peptide hemolytic activity of table 3
It can be seen from Table 3 that, improved not significantly as sequence increases its antibacterial activity, and hemolytic activity is improved and more shown
Write.The antibacterial and hemolytic activity of comprehensive analysis antibacterial peptide, can be by therapeutic index (ratio of hemolytic concentration and Mlc)
More fully to evaluate the BA of each antibacterial peptide.As can be seen from Table 3, W2 has therapeutic index higher, shows
The W2 antibacterial peptides that design is obtained have the development potentiality of substitute antibiotics higher.
3rd, stability of the antibacterial peptide under physiological salt concentration
By the salt ion peptide diluted of antibacterial peptide to be measured containing different physiological concentrations, its salt ionic concentration difference
It is 150mM NaCl, 4.5mM KCl, 2.5mM CaCl2, 1mM MgCl2, 8 μM of ZnCl2, 6 μM of NH4Cl, and 4 μM of FeCl3.So
Antibacterial peptide is cultivated together with bacterium solution to be measured at 37 DEG C afterwards, then according to the minimum that antibacterial peptide is determined described in bacteriostatic activity step
Mlc；As a control group, to detect stability of the antibacterial peptide to different salt ions without salt ion treatment group.Result such as table
Shown in 4.
Tolerance under the antibacterial peptide physiological salt concentration of table 4
Be can be seen that under physiological concentration by the result of table 4, the MIC of antibacterial peptide W2 and W3 does not have too big change, especially
It is Escherichia coli ATCC 25922, monovalence salt ion (K+and NH4 +), divalence salt ion (Mg2+, Ca2+, and Zn2+) and trivalent
Salt ion (Fe3+) little for the minimal inhibitory concentration influence of antibacterial peptide, or even there are a few cases to be favorably improved antibacterial peptide
Bacteriostatic activity, only salt ion Na+There is significantly influence on its antibacterial activity.And only act on staphylococcus aureus
Small peptide W2 just has certain reduction receiving MIC under the influence of ion during ATCC 29213, illustrates that the method helps to provide antibacterial
The stability of peptide, small peptide W2 still has certain salt ion tolerance.
<110>Northeast Agricultural University
<120>Multiply β-hair fastener small peptide and preparation method and application with tolerance protein enzyme
<160> 2
<210> 1
<211> 12
<212> PRT
<213>Artificial sequence
<400> 1
Trp Arg Pro Gly Arg Trp Trp Arg Pro Gly Arg Trp -NH2
1 5 10
<210> 2
<211> 18
<212> PRT
<213>Artificial sequence
<400>2
Trp Arg Pro Gly Arg Trp Trp Arg Pro Gly Arg Trp Trp Arg Pro Gly Arg Trp -NH2
1 5 10 18
Claims (3)
1. a kind of multiply β with tolerance protein enzyme-hair fastener small peptide W2, it is characterised in that sequence such as sequence table SEQ ID No.1
It is shown.
2. a kind of preparation method of the multiply β with tolerance protein enzyme-hair fastener small peptide W2, it is characterised in that method is as follows：
(1) wherein the lamella area of each β-hairpin structure is constituted using common amino Trp, Arg, it is ensured that enter one while active
Step raising stability, and change the composition of corner amino acid, finally give the multiply β-hair fastener antibacterial peptide of brand new：
(WRXxRW)n-NH2, it is L-type proline and glycine to choose wherein corner, and as n=2, antibacterial peptide is named as W2, and sequence is such as
Shown in sequence table SEQ ID No.1；
(2) peptide resin is obtained by Peptide synthesizer using solid-state chemical reaction method method, the peptide resin that will be obtained cuts by TFA
Afterwards, two polypeptides are obtained；
(3) by after RPLC purifying and Mass Spectrometric Identification, that is, completing the preparation of polypeptide.
3. a kind of multiply β-hair fastener small peptide W2 with tolerance protein enzyme according to claim 1 is in treatment Gram-negative
Application in bacterium and gram positive bacteria infection disease medicament.
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Cited By (10)
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|---|---|---|---|---|
| CN109810178A (en) * | 2019-01-10 | 2019-05-28 | 东北农业大学 | A kind of resistance to enzymolysis antibacterial peptide I9H12 and its preparation method and application |
| CN111423492A (en) * | 2020-03-30 | 2020-07-17 | 东北农业大学 | β hairpin antibacterial peptide containing D-type proline and glycine corner and preparation method thereof |
| CN111423493A (en) * | 2020-03-30 | 2020-07-17 | 东北农业大学 | Palmitic acid anti-enzymolysis antibacterial peptide and preparation method and application thereof |
| CN111454334A (en) * | 2020-03-30 | 2020-07-28 | 东北农业大学 | Enzymolysis-resistant antibacterial peptide II4II, and preparation method and application thereof |
| CN111454330A (en) * | 2020-03-30 | 2020-07-28 | 东北农业大学 | β hairpin antibacterial peptide with tryptophan and histidine interaction across chains and preparation method thereof |
| CN111484546A (en) * | 2020-03-30 | 2020-08-04 | 东北农业大学 | β hairpin antibacterial peptide containing asparagine and glycine corner and preparation method thereof |
| CN111533789A (en) * | 2020-03-30 | 2020-08-14 | 东北农业大学 | Tryptophan and lysine chain-crossing interaction beta-hairpin antibacterial peptide and preparation method thereof |
| CN111533786A (en) * | 2020-03-30 | 2020-08-14 | 东北农业大学 | Beta-hairpin antibacterial peptide with tryptophan and arginine cross-chain interaction and preparation method thereof |
| CN114989254A (en) * | 2022-06-17 | 2022-09-02 | 中山大学 | Polypeptide, design method thereof and application of polypeptide in preparation of fusobacterium nucleatum inhibiting product or colorectal cancer preventing medicine |
| CN116789854A (en) * | 2023-06-08 | 2023-09-22 | 东北农业大学 | Nanometer antibacterial peptide with bacteria capturing and antibacterial functions, preparation method and application |
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2016
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Cited By (15)
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| CN109810178A (en) * | 2019-01-10 | 2019-05-28 | 东北农业大学 | A kind of resistance to enzymolysis antibacterial peptide I9H12 and its preparation method and application |
| CN109810178B (en) * | 2019-01-10 | 2021-12-14 | 东北农业大学 | Anti-enzymolysis antibacterial peptide I9H12, and preparation method and application thereof |
| CN111533789A (en) * | 2020-03-30 | 2020-08-14 | 东北农业大学 | Tryptophan and lysine chain-crossing interaction beta-hairpin antibacterial peptide and preparation method thereof |
| CN111454334A (en) * | 2020-03-30 | 2020-07-28 | 东北农业大学 | Enzymolysis-resistant antibacterial peptide II4II, and preparation method and application thereof |
| CN111454330A (en) * | 2020-03-30 | 2020-07-28 | 东北农业大学 | β hairpin antibacterial peptide with tryptophan and histidine interaction across chains and preparation method thereof |
| CN111484546A (en) * | 2020-03-30 | 2020-08-04 | 东北农业大学 | β hairpin antibacterial peptide containing asparagine and glycine corner and preparation method thereof |
| CN111423493A (en) * | 2020-03-30 | 2020-07-17 | 东北农业大学 | Palmitic acid anti-enzymolysis antibacterial peptide and preparation method and application thereof |
| CN111533786A (en) * | 2020-03-30 | 2020-08-14 | 东北农业大学 | Beta-hairpin antibacterial peptide with tryptophan and arginine cross-chain interaction and preparation method thereof |
| CN111423492A (en) * | 2020-03-30 | 2020-07-17 | 东北农业大学 | β hairpin antibacterial peptide containing D-type proline and glycine corner and preparation method thereof |
| CN111423492B (en) * | 2020-03-30 | 2021-12-14 | 东北农业大学 | Beta-hairpin antibacterial peptide containing D-type proline and glycine corner and preparation method thereof |
| CN111533786B (en) * | 2020-03-30 | 2022-02-08 | 东北农业大学 | Beta-hairpin antibacterial peptide with tryptophan and arginine cross-chain interaction and preparation method thereof |
| CN114989254A (en) * | 2022-06-17 | 2022-09-02 | 中山大学 | Polypeptide, design method thereof and application of polypeptide in preparation of fusobacterium nucleatum inhibiting product or colorectal cancer preventing medicine |
| CN114989254B (en) * | 2022-06-17 | 2023-11-03 | 中山大学 | Polypeptide, design method thereof and application of polypeptide in preparation of medicines for inhibiting Fusobacterium nucleatum products or preventing colorectal cancer |
| CN116789854A (en) * | 2023-06-08 | 2023-09-22 | 东北农业大学 | Nanometer antibacterial peptide with bacteria capturing and antibacterial functions, preparation method and application |
| CN116789854B (en) * | 2023-06-08 | 2024-04-02 | 东北农业大学 | Nanometer antibacterial peptide with bacteria capturing and antibacterial functions, preparation method and application |
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Application publication date: 20170531 |