CN107141339A - antibacterial peptide and its preparation method and application - Google Patents
antibacterial peptide and its preparation method and application Download PDFInfo
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- CN107141339A CN107141339A CN201710309382.XA CN201710309382A CN107141339A CN 107141339 A CN107141339 A CN 107141339A CN 201710309382 A CN201710309382 A CN 201710309382A CN 107141339 A CN107141339 A CN 107141339A
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- antibacterial peptide
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- chromatography
- antibacterial
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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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
- A61L2/00—Methods or apparatus for disinfecting or sterilising materials or objects other than foodstuffs or contact lenses; Accessories therefor
- A61L2/16—Methods or apparatus for disinfecting or sterilising materials or objects other than foodstuffs or contact lenses; Accessories therefor using chemical substances
Abstract
The present invention provides a kind of antibacterial peptide and its preparation method and application.The amino acid sequence of antibacterial peptide of the present invention is：Tyr‑Ile‑Pro‑Gln‑Pro‑Arg‑Pro‑Pro‑His‑Pro‑Arg‑Leu.The preparation method of the antibacterial peptide includes：Cation-exchange chromatography, hydrophobic chromatography and size exclusion chromatography are carried out to the zymotic fluid containing the antibacterial peptide, the antibacterial peptide is obtained.The antiseptic peptide stability of the present invention is good, and antibacterial activity is high.
Description
Technical field
The present invention relates to a kind of polypeptide, and in particular to a kind of antibacterial peptide and its preparation method and application.
Background technology
Antibacterial peptide is the peptide material that a class has antibacterial activity.At present, had been found that in different animals tissue a variety of
Proteins and peptides with antibacterial action, it is the class broad spectrum antibiotic activity polypeptide being present in organism, is also congenital
Important part in immune system.These antibacterial peptides have that strong antibacterial, has a broad antifungal spectrum, species be more, available model
The features such as wide, target bacterial strain is not likely to produce resistant mutation is enclosed, while in view of many microorganisms develop immunity to drugs to antibiotic, therefore
Antibacterial peptide is expected to the clinical antibacterials as a new generation, and in cosmetics, biological pesticide, animal feed additive, natural
Had broad application prospects in terms of food preservative, animal and plant disease resisting genetic engineering.
Bee peptide (apidaecin, abbreviation AP) is a class from the polypeptide of the rich proline of hymenopteran, earliest from
It is isolated in the lymph of honeybee, 16~19 amino acid residues are typically contained, it is to a variety of Gram-negative bacterias, particularly
Enterobacteriaceae, with the effect of killing of very strong wound, and does not work to the gram-positive bacteria including Lactococcus lactis, and
There is no toxic action to eukaryotic.Because content of the bee peptide in insect is less, people are increasingly attempted in different expression
Bee peptide is expressed in system.However, antibacterial peptide exists in exogenous gene expression, gene expression amount is low, expression product is easy
Degrade, expression product activity is low, antibacterial peptide easily produces the problems such as poisoning to Host Strains.Therefore, expect that a kind of stability is good and anti-
The high antibacterial peptide of bacterium activity.
The content of the invention
The present invention provides a kind of antibacterial peptide and its preparation method and application, and the stability of the antibacterial peptide is good, and antibacterial activity is high.
The present invention provides a kind of antibacterial peptide, and its amino acid sequence is：Tyr‐Ile‐Pro‐Gln‐Pro‐Arg‐Pro‐Pro‐
His‐Pro‐Arg‐Leu(SEQ ID NO：1).
The present invention does not make strict limitation to the preparation method of the antibacterial peptide with above-mentioned amino acid sequence, can pass through chemistry
Synthesis is obtained, can also be by being fermented to the bacterial strain containing above-mentioned peptide expression carrier；Those skilled in the art
It can easily be built according to the amino acid sequence of above-mentioned antibacterial peptide and obtain above-mentioned peptide expression carrier, and then obtained containing upper
State the bacterial strain of peptide expression carrier and it is fermented.
The present invention also provides a kind of preparation method of antibacterial peptide, including：Sun is carried out to the zymotic fluid containing above-mentioned antibacterial peptide
Ion-exchange chromatography, hydrophobic chromatography and size exclusion chromatography, obtain the antibacterial peptide.
The present invention does not make strict limitation to the preparation method of above-mentioned zymotic fluid, as long as above-mentioned antibacterial can be obtained by fermentation
Peptide.In one embodiment, the preparation method of the zymotic fluid can include：To containing the peptide expression carrier
Bacillus subtilis is fermented, and obtains the zymotic fluid.
Specifically, can be by the recombinant bacillus disclosed in the Chinese invention patent to the A of publication number CN 105671069
Bacillus is transformed, so as to obtain the bacterial strain containing above-mentioned peptide expression carrier；Do not make strict limitation to reforming mode,
Can be using genetic engineering sides such as mutagenesis mode, the rite-directed mutagenesises such as physical mutagenesis mode, the mutagens such as ultraviolet mutagenesis
Formula etc..
In the present invention, the order to cation-exchange chromatography, hydrophobic chromatography and size exclusion chromatography does not make strict limitation,
Cation-exchange chromatography, hydrophobic chromatography and size exclusion chromatography are preferably carried out successively.
The present invention by three kinds of cation-exchange chromatography, hydrophobic chromatography and size exclusion chromatography by chromatographing the chromatography system constituted
System, remove in zymotic fluid has other things such as charge differences, hydrophobic difference, the foreign protein of difference in size respectively with purpose antibacterial peptide
Matter, so as to reach the effect of purifying；Antibacterial peptide after purified is by combining HPLC-MS, so as to be further purified
Antibacterial peptide sterling and its structural information.The above method is by using characteristic the characteristics of antibacterial peptide between different laminate methods
Difference, is not only scientifically and rationally isolated and purified to antibacterial peptide, also provides foundation for the detection of antibacterial peptide.
Wherein, cation-exchange chromatography is to be situated between using the exchangeable ion on ion-exchanger (i.e. exchange media) with surrounding
The various interionic affinity being separated in matter are different, i.e., using the charged group of ion-exchanger, phase in absorption zymotic fluid
The ion or ionic compound of counter charges, adsorbed material are then replaced and washed by other ions with same type electric charge
De-, because a variety of ions or ionic compound are different to the adhesion of ion-exchanger, thus the speed of elution is different
So as to form chromatography layer.Because ion exchange is reversible, it can reach balance, therefore ion exchange layer with the speed being exceedingly fast
Analysis have sensitivity it is high, repeated, selectivity good, the advantages of analyze speed is fast.
In the concrete scheme of the present invention, the exchange media of the cation-exchange chromatography is Capto S；The exchange media
The chromatography media on the high flow rate Agar substrate platform of novelty is built upon, it combines high mechanicalness, high dynamic carrying capacity and fast
The property of fast mass transfer, can fast purifying, meet flexible craft design and cost-benefit requirement to greatest extent.Compared to Bu Ju Portugals
Glycan modifies the medium of skeleton, and the combination carrying capacity of the exchange media is increased substantially.
The present invention does not make strict limitation to the specific separation condition of cation-exchange chromatography, can divide for the routine of this area
From condition.Specifically, equilibrium liquid can be the phosphate buffer solution that pH value is 5-6；Furthermore, it is possible to using 0.03-
0.12mol/L, pH value are eluted for 5-6 phosphate buffer solution as eluent.
In the present invention, hydrophobic chromatography is to be separated using the hydrophobic grouping of polypeptides/proteins with hydrophilic radical, many
The surface of peptide/protein generally has hydrophobic group, and it with hydrophobic carrier in high salt concentration with that can combine；Typically
For, ionic strength (salinity) is higher, stronger with reference to the hydrophobic bond formed.It is described to dredge in the concrete scheme of the present invention
The hydrophobic medium of water layer analysis is Phenyl-Sepharose, and it can preferably separate target antibacterial peptide.
The present invention does not make strict limitation to the specific separation condition of hydrophobic chromatography, can be the conventional lightning strip of this area
Part.Specifically, equilibrium liquid can be pH value 5-6, concentration 0.2mol/L phosphate buffer solution；Furthermore, it is possible to using 0.02-
0.05mol/L, pH value carry out gradient elution for 5-6 phosphate buffer solution as eluent.
Preferably, using reduce salinity by the way of eluted, for example successively using 0.05mol/L, 0.04mol/L,
0.03mol/L, 0.02mol/L, 0.01mol/L pH value carry out gradient elution for 5-6 phosphate buffer solution.In elution
When, the salinity of eluent is gradually reduced, the different material of hydrophobicity can be made one by one successively to be eluted out, so that
The materials such as purpose antibacterial peptide and other hydrophilic proteins are separated.Particularly, hydrophobic chromatography, energy are carried out after cation-exchange chromatography
Enough make two kinds of chromatographies complementary, therefore, be conducive in separation cation-exchange chromatography it is difficult to or indissociable material.
In the present invention, size exclusion chromatography is separated based on bulk of molecule difference, and it is a kind of non-adsorbed shape
The chromatography method of formula, therefore the composition of buffer solution will not directly affect separating resulting, purpose antibacterial peptide can be in extensive pH value
And the separation of material is carried out under ionic strength.Size exclusion chromatography provides the selection of flexibly suitable chromatography condition, meet into
The demand of one step purifying.
In the concrete scheme of the present invention, the filler of the size exclusion chromatography is sephadex g-100.The present invention is right
The specific separation condition of size exclusion chromatography does not make strict limitation, can be the conventional separation condition of this area.Specifically, can be with
It is 5-6 phosphate buffer solution as equilibrium liquid and eluent to use 0.02-0.08mol/L, pH value.
The present invention also provides a kind of antibiotic method, is carried out using above-mentioned antibacterial peptide.Above-mentioned antibacterial peptide is to a variety of gram-negatives
Property bacterium, particularly enterobacteriaceae, with the effect of killing of very strong wound, not only antibacterial activity is strong, and this external stability is good, is conducive to reality
Popularization and application.
Brief description of the drawings
Fig. 1 is the HPLC chromatogram of antibacterial peptide prepared by the embodiment of the present invention 1；
Fig. 2 is the mass spectrogram of antibacterial peptide prepared by the embodiment of the present invention 1.
Embodiment
To make the object, technical solutions and advantages of the present invention clearer, accompanying drawing and implementation below in conjunction with the present invention
Example, the technical scheme in the embodiment of the present invention is clearly and completely described, it is clear that described embodiment is the present invention
A part of embodiment, rather than whole embodiments.Based on the embodiment in the present invention, those of ordinary skill in the art are not having
The every other embodiment obtained under the premise of creative work is made, the scope of protection of the invention is belonged to.
The raw material that each embodiment is used：
Recombined bacillus subtilis bacterial strain：According to the side disclosed in the A of publication number CN 105671069 Chinese invention patent
Method is prepared；
Exchange media：Capto S, purchased from General Electric's Medical Group (GE Healthcare)；
Hydrophobic medium：Phenyl-Sepharose, purchased from Beijing Suo Laibao Science and Technology Ltd (Solarbio)；
Size exclusion chromatography filler：Sephadex g-100, purchased from Shanghai Yu Bo bio tech ltd
(Pharmacia)；
Antibacterial peptide (SEQ ID NO：1)：Obtained using the synthesis of ABI 433A full-automatic polypeptide synthetic instruments.
Embodiment 1
First, strain improvement
Ultraviolet mutagenesis, the larger bacterial strain of screening inhibition zone are carried out to restructuring bacillus subtilis strain using conventional method
(hereinafter referred to as mutant strain), it is standby.
A large amount of salmonellas are mixed with a small amount of above-mentioned mutant strain, increased and steady in mutant strain viable count
After fixed, by the pure culture of a small amount of bacterial suspension inoculation to salmonella, it is mixed repeatedly, mutant strain is in salmonella
Under the selection for attacking poison culture, the stronger bacillus subtilis new strains of antibacterial activity are produced.
Genetic stability experiment is carried out to above-mentioned bacillus subtilis new strains, the bacillus subtilis of genetic stability is obtained
Bacterium new strains (hereinafter referred to as transform bacterial strain).
2nd, ferment
By above-mentioned transformation inoculation into LB culture mediums, in 37 DEG C, 250r/min shaken cultivations 22 hours, 10000r/
Min centrifugations 10min collects fermented liquid supernatant, standby.
3rd, isolate and purify
Cation-exchange chromatography, hydrophobic chromatography and size exclusion chromatography are carried out successively to above-mentioned fermented liquid supernatant, specific step
Suddenly it is：
1st, cation-exchange chromatography
Cation-exchange chromatography is carried out to above-mentioned fermented liquid supernatant using Capto S as exchange media, wherein using pH5.8
Phosphate buffer solution balance after, with 2BV/h speed loading, then using 0.06mol/L, pH5.8 phosphate-buffered
Solution is eluted, and an eluent is collected per 5min and bacteriostatic test is carried out using double-deck agar perforation diffusion method, tool is collected
There is the eluent of inhibition zone.
2nd, hydrophobic chromatography
Hydrophobic chromatography is carried out to the eluent of above-mentioned collection using Phenyl-Sepharose as hydrophobic medium, wherein using
After 0.2mol/L, pH5.8 phosphate buffer solution balance, with 2BV/h speed loading, then successively using 0.05mol/L,
0.04mol/L, 0.03mol/L, 0.02mol/L, 0.01mol/L pH5.8 phosphate buffer solution carry out gradient elution, often
5min collects an eluent and carries out bacteriostatic test, collects the eluent with inhibition zone.
3rd, size exclusion chromatography
Size exclusion chromatography is carried out to the eluent of above-mentioned collection using sephadex g-100 as filler, wherein using
After pH5.8 phosphate buffer solution balance, with 2BV/h speed loading, then entered using pH5.8 phosphate buffer solution
Row elution, an eluent is collected per 5min and bacteriostatic test is carried out, the eluent with inhibition zone is collected, surpasses in the usual way
Filter concentration, dry, it is lyophilized after, the antibacterial peptide purified, sealing preserve.
4th, HPLC-MS analyses detection
Using the Infinity binary liquid chromatographic systems of Agilent 1260 (being purchased from Agilent companies) to above-mentioned preparation
Obtained antibacterial peptide carries out analysis detection, wherein：Chromatographic column is the StableBond of Agilent ZORBAX 300 (300SB)
C8HPLC chromatographic columns (are purchased from Agilent companies)；Mobile phase A：0.1% trifluoroacetic acid aqueous solution；Mobile phase B：80% second
The nitrile aqueous solution；Column temperature：25 DEG C, Detection wavelength：280nm；Maximum pressure：200bar；Time：65min；Flow velocity：0.700mL/
min；Applied sample amount：20ug, analysis gradient is shown in Table 1, and testing result is shown in Fig. 1.
The HPLC of table 1 analyzes gradient
| Time/min | 0 | 3.00 | 10.00 | 40.00 | 55.00 | 57.00 | 65.00 |
| A (%) | 95.0 | 95.0 | 91.0 | 83.0 | 70.0 | 95.0 | 95.0 |
| B (%) | 5.0 | 5.0 | 9.0 | 17.0 | 30.0 | 5.0 | 5.0 |
Mass Spectrometer Method condition：Sheath gas flow (arb)：15；Auxiliary gas flow amount (arb)：5；Thermal spraying voltage (kV)：
4.7；Capillary temperature (DEG C)：275；Capillary voltage (V)：49；Sleeve lens offset voltage (V)：120；Testing result is shown in figure
2。
As a result show：The amino acid sequence of the antibacterial peptide of above-mentioned preparation is：Tyr‐Ile‐Pro‐Gln‐Pro‐Arg‐Pro‐
Pro‐His‐Pro‐Arg‐Leu(SEQ ID NO：1).
Embodiment 2
The present embodiment is with chemical synthesis process synthetic antibacterial peptide, wherein being carried out using ABI 433A full-automatic polypeptide synthetic instruments
Synthesize, the amino acid sequence of antibacterial peptide is：Tyr‐Ile‐Pro‐Gln‐Pro‐Arg‐Pro‐Pro‐His‐Pro‐Arg‐Leu(SEQ
ID NO：1).
Reference examples 1
It is withered with the restructuring prepared according to the method disclosed in the A of publication number CN 105671069 Chinese invention patent
Careless Bacillus strain as control, the recombined bacillus subtilis bacterial strain is fermented with reference to the method for embodiment 1, separate it is pure
Change and HPLC-MS analyzes detection.
As a result show：The antibacterial peptide that above-mentioned recombined bacillus subtilis strain fermentation is produced is bee peptide.
The antibacterial tests of test example 1
Antibacterial is carried out to the antibacterial peptide of embodiment 1, embodiment 2 and reference examples 1 using standard agar hole diffusion method respectively
Experiment.
The antibacterial peptide of embodiment 1, embodiment 2 and reference examples 1 is configured to the antibacterial peptide solution of same concentrations respectively, with big
Enterobacteria K88, staphylococcus aureus, Salmonella, enterococcus faecalis and streptococcus fecalis are experimental strain, by each experimental strain
Tiling plate is after it solidifies after nutrient solution is mixed with 55 DEG C of LB solid mediums 25mL respectively, with sterilized card punch (directly
Footpath 5mm) punch, each antibacterial peptide solution is added dropwise respectively in hole, 12h are cultivated at 37 DEG C, each antibacterial circle diameter (mm) is determined, while with
Antibacterial circle diameter calculates disinfection vitality (X) and bactericidal titer (U/mL), and calculation formula is as follows：
Disinfection vitality (X)=(antibacterial circle diameter -2.3mm)/2
Bactericidal titer (U/mL)=2X × 1000
Inhibition zone size is observed, 2 are the results are shown in Table.
The antibacterial activity of each antibacterial peptide of table 2
As seen from the results in Table 1：The antibacterial activity of the antibacterial peptide of the present invention is significantly higher than bee peptide.
Test 2 stability tests
The antibacterial peptide of embodiment 1, embodiment 2 and reference examples 1 is continuously preserved 6 months under room temperature (28-32 DEG C) respectively,
Antibacterial tests (monthly) periodically are carried out according to the method for test example 1, the anti-bacterial result after preserving 6 months is shown in Table 3.
The stability of each antibacterial peptide of table 3
In table 3, "/" is represented and not detected.
Stability test result shows：Conventional bee peptide is preserved at room temperature does not have antibacterial activity substantially after 1 month,
And after the antibacterial peptide of the present invention is continuously preserved 6 months at room temperature, antibacterial activity only declines 10% or so, illustrate that the present invention's is anti-
Bacterium peptide has good stability.
Finally it should be noted that：Various embodiments above is merely illustrative of the technical solution of the present invention, rather than its limitations；To the greatest extent
The present invention is described in detail with reference to foregoing embodiments for pipe, it will be understood by those within the art that：Its according to
The technical scheme described in foregoing embodiments can so be modified, or which part or all technical characteristic are entered
Row equivalent substitution；And these modifications or replacement, the essence of appropriate technical solution is departed from various embodiments of the present invention technology
The scope of scheme.
<110>Gansu Olympic Bel's biotechnology Group Co., Ltd
<120>Antibacterial peptide and its preparation method and application
<160> 2
<170> PatentIn version 3.5
<210> 1
<211> 12
<212> PRT
<213>Artificial sequence
<400> 1
Tyr Ile Pro Gln Pro Arg Pro Pro His Pro Arg Leu
1 5 10
Claims (10)
1. a kind of antibacterial peptide, it is characterised in that amino acid sequence is：Tyr‐Ile‐Pro‐Gln‐Pro‐Arg‐Pro‐Pro‐His‐
Pro‐Arg‐Leu。
2. a kind of preparation method of antibacterial peptide, it is characterised in that including：To the zymotic fluid containing antibacterial peptide described in claim 1
Cation-exchange chromatography, hydrophobic chromatography and size exclusion chromatography are carried out, the antibacterial peptide is obtained.
3. preparation method according to claim 2, it is characterised in that the preparation method of the zymotic fluid includes：To containing
The bacillus subtilis of the peptide expression carrier is fermented, and obtains the zymotic fluid.
4. the preparation method according to Claims 2 or 3, it is characterised in that the exchange media of the cation-exchange chromatography
For Capto S.
5. preparation method according to claim 4, it is characterised in that when carrying out the cation-exchange chromatography, is used
0.03-0.12mol/L, pH value are eluted for 5-6 phosphate buffer solution as eluent.
6. the preparation method according to Claims 2 or 3, it is characterised in that the hydrophobic medium of the hydrophobic chromatography be phenyl-
Ago-Gel.
7. preparation method according to claim 6, it is characterised in that when carrying out the hydrophobic chromatography, using 0.02-
0.05mol/L, pH value carry out gradient elution for 5-6 phosphate buffer solution as eluent.
8. the preparation method according to Claims 2 or 3, it is characterised in that the filler of the size exclusion chromatography is poly- for Portugal
Sugared gel G-100.
9. preparation method according to claim 8, it is characterised in that when carrying out the hydrophobic chromatography, using 0.02-
0.08mol/L, pH value are used as equilibrium liquid and eluent for 5-6 phosphate buffer solution.
10. a kind of antibiotic method, it is characterised in that carried out using the antibacterial peptide described in claim 1.
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| CN201710309382.XA CN107141339A (en) | 2017-05-04 | 2017-05-04 | antibacterial peptide and its preparation method and application |
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Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN107987690A (en) * | 2017-11-16 | 2018-05-04 | 江山海维科技有限公司 | A kind of environmentally-friendly coating method of timber |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102851339A (en) * | 2012-03-21 | 2013-01-02 | 中农颖泰林州生物科园有限公司 | Production method of Sublancin antibacterial peptide |
| US20140309161A1 (en) * | 2011-06-20 | 2014-10-16 | Universitat Leipzig | Modified antibiotic peptides having variable systemic release |
| CN105671069A (en) * | 2014-11-18 | 2016-06-15 | 张掖奥谱生物科技有限公司 | Apidaecin expression vector as well as construction method and application thereof |
-
2017
- 2017-05-04 CN CN201710309382.XA patent/CN107141339A/en active Pending
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20140309161A1 (en) * | 2011-06-20 | 2014-10-16 | Universitat Leipzig | Modified antibiotic peptides having variable systemic release |
| CN102851339A (en) * | 2012-03-21 | 2013-01-02 | 中农颖泰林州生物科园有限公司 | Production method of Sublancin antibacterial peptide |
| CN105671069A (en) * | 2014-11-18 | 2016-06-15 | 张掖奥谱生物科技有限公司 | Apidaecin expression vector as well as construction method and application thereof |
Non-Patent Citations (1)
| Title |
|---|
| RANJNA C. DUTTA, ET AL.: "Functional mapping of apidaecin through secondary structure correlation", 《THE INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY》 * |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN107987690A (en) * | 2017-11-16 | 2018-05-04 | 江山海维科技有限公司 | A kind of environmentally-friendly coating method of timber |
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