CN110204597A - A kind of antibacterial peptide and its application - Google Patents
A kind of antibacterial peptide and its application Download PDFInfo
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- CN110204597A CN110204597A CN201910457698.2A CN201910457698A CN110204597A CN 110204597 A CN110204597 A CN 110204597A CN 201910457698 A CN201910457698 A CN 201910457698A CN 110204597 A CN110204597 A CN 110204597A
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- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
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- 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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- A—HUMAN NECESSITIES
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Abstract
This application discloses a kind of antibacterial peptides of field of biotechnology, it is basic improvement and design with antibacterial peptide VL15, three kinds of obtained antibacterial peptides FL15-1, FL15-2, FL15-3, as shown in SEQ ID NO.1, SEQ ID NO.2, SEQ ID NO.3, the antibacterial peptide of the application has the application in preparation treatment gram-positive bacteria, Gram-negative bacteria, drug-fast bacteria and the extensive pedigree antibiotic of fungal infection.
Description
Technical field
The present invention and field of biotechnology, and in particular to a kind of antibacterial peptide and its application.
Background technique
Antibacterial peptide (Antimicrobial peptides, AMPs) is that organism is defendd to generate when extraneous pathogen invasion
It is encoded by gene, the small molecule active peptides of Ribosome biogenesis are the important compositions of innate defence system in organism
Ingredient.AMPs generally has antibacterium, fungi, virus or protozoon isoreactivity as a kind of bioactive small molecule.In addition,
AMPs is also used as drug carrier system, antitumor agent, immunomodulator and signaling molecule etc..
Antibiotic has saved the life of countless people, but in recent years as a kind of important clinical application since by application
Come, since the problems such as drug abuse medicament residue and bacterial drug resistance gets worse, more and more countries are sought for antibiosis
Plain substitute, and antibacterial peptide has become because of its unique bioactivity and different from the special mechanism of action of conventional antibiotic
For most potential one of Substitutes For Antibiotic, while answering in novel foodstuff, drug, skin care item and cosmetics preservative
With also more and more extensive, there is good development prospect.
The correlative study of antibacterial peptide can trace back to 1975 earliest, and Sweden scientist G.Bomam etc. was cherishing guppy at that time
Escherichia coli are injected in genius pupa, have found a kind of basic polypeptide class with antibacterial activity in its blood lymphocytes later
Substance, i.e. antibacterial peptide Ceropins.By research in more than 40 years, had found from animal, plant, bacterium and virus at present super
Cross 3000 kinds of antibacterial peptides.
Although natural antibacterial peptide has the advantages that universal, there is also certain clearly disadvantageous.Quite a few is natural
Antibacterial peptide bacteriostatic activity it is lower, stability is poor, toxicity is higher, or cause eukaryocyte that haemolysis etc. occurs.In addition, part
Antibacterial peptide is poor to the inhibitory effect of drug-fast bacteria, is not able to satisfy the requirement of practical application；And by being transformed to natural antibacterial peptide
Or completely newly synthesize obtained artificial antimicrobial peptide can largely improve certain of the above even all disadvantages, to adapt to difference
Application demand.Also up to thousands of kinds of artificial antimicrobial peptide at present, such as artificial synthesized antibacterial peptide VL15, amino acid sequence be
VLNRLFDKIRQVIRK, (the SEQ ID NO.4) antibacterial peptide are straight-chain polypeptide, contain 15 amino acid residues, molecular size range
It for 1898.35Da, isoelectric point 11.72, but is analyzed by the anti-microbial property to the antibacterial peptide, finds the suppression of the antibacterial peptide
Bacterium effect is poor, and inventor is transformed the antibacterial peptide, to obtain the better antibacterial peptide of bacteriostasis property.
Summary of the invention
The present invention to be provided is three kinds more excellent based on bacteriostasis property after antibacterial peptide VL15 transformation, effective to drug-fast bacteria
Antibacterial peptide.
A kind of antibacterial peptide is named as antibacterial peptide FL15-1, antibacterial peptide FL15-1 amino acid sequence to be distinguished herein
As shown in SEQ ID NO.1, specially Phe-Leu-Lys-Arg-Ile-Phe-asparagus fern acyl
Amine-Lys-Ile-Arg-Gln-Leu-Ile-arginine-lysine, more specifically:
Phe-Leu-Lys-Arg-Leu-Phe-Asp-Lys-Ile-Arg-Gln-Leu-Ile-Arg- Lys, molecular weight are
1974.49Da isoelectric point 11.73；
A kind of antibacterial peptide is named as antibacterial peptide FL15-2, the amino acid sequence of antibacterial peptide FL15-2 such as SEQ ID herein
Shown in NO.2, specially Phe-Leu-Lys-Arg-Ile-Phe-arginine-lysine-is different
Leucine-arginine-glutamine-leucine-isoleucine-arginine-lysine, more specifically:
Phe-Leu-Lys-Arg-Leu-Phe-Arg-Lys-Ile-Arg-Gln-Leu-Ile-Arg- Lys, molecular weight are
2015.59Da isoelectric point 12.48；
A kind of antibacterial peptide is named as antibacterial peptide FL15-3, the amino acid sequence of antibacterial peptide FL15-3 such as SEQ ID herein
Shown in NO.3, specially Phe-Leu-Lys-Arg-Ile-Phe-arginine-lysine-is different
Leucine-arginine-lysine-Leu-Ile-arginine-lysine, more specifically:
Phe-Leu-Lys-Arg-Leu-Phe-Arg-Lys-Ile-Arg-Lys-Leu-Ile-Arg- Lys, molecular weight are
2015.63Da isoelectric point 11.10.
The present invention also provides another antibacterial peptide, the amino acid sequence and SEQ ID NO.1, SEQ ID NO.2 or SEQ
ID NO.3 has the polypeptide of 67% or more homology.The polypeptide includes by replacing, extending or truncating SEQ ID NO.1, SEQ
The obtained similar sequences of 1-5 amino acid in ID NO.2 or SEQ ID NO.3, and the acquisition by the similar sequences
Compound.
The preparation method of above-mentioned antibacterial peptide is solid phase polypeptide synthesis comprising the steps of:
1) resin swelling: the 2-Chlorotrityl Chloride Resin tree that 0.6g degree of substitution is 0.4mmol/g is weighed
Resin is put into reaction tube by rouge, is added DCM (15ml/g), and 30min is vibrated.
2) it connects first amino acid: solvent is leached out by husky core, the Fmoc-L-Leu-OH ammonia of 3 times of molar excess is added
Base acid, adds the DIEA of 10 times of molar excess, is eventually adding a small amount of DMF dissolution, vibrates 1h.With DMF and DCM alternately cleaning 6
Time.
3) it is deprotected: adding 15ml Piperidine/DMF solution (15ml/g), solvent, then plus 15ml Piperidine/DMF solution are taken out after 5min
(15ml/g) vibrates 15min.
4) it detects: taking out piperidine solution, take more than ten grainy resins, washed three times with ethyl alcohol, ninhydrin, KCN, phenol solution is added
Each drop, 105 DEG C of -110 DEG C of heating 5min, deepening blue is positive reaction.
5) wash: twice, twice, DMF (10ml/g) is twice for methanol (10ml/g) by DMF (10ml/g).
6) be condensed: protected amino acid Fmoc-L-Leu-OH three times are excessive, and HBTU three times are excessive, molten with DMF few as far as possible
Reaction tube is added in solution, is added immediately ten times of excess of NMM, reacts 30min.
7) wash: once, twice, DMF (10ml/g) is twice for methanol (10ml/g) by DMF (10ml/g).
8) operation of two to six steps, the amino acid being sequentially connected in sequence from right to left are repeated.
9) the last one amino acid connection after, deprotection, wash resin in following manner: DMF (10ml/g) twice, methanol
(10ml/g) twice, twice, DCM (10ml/g) twice, drains 10min to DMF (10ml/g).
10) polypeptide is cut from resin: preparing cutting liquid TFA 94.5%, water 2.5%, EDT 2.5%, TIS 1% will
Resin is fitted into flask or centrifuge tube, and cutting liquid and resin ratio are according to 10ml/g, isothermal vibration, time: 120min.
11) drying washing: lysate being dried up as far as possible with nitrogen, is separated out with ether layer, then washes six times with ether, then
Room temperature volatilizes to get crude product peptide sequence.
12) HPLC purified polypeptide is used:
(1) it takes crude product peptide 200mg to be put into vessel, is dissolved with the acetonitrile solution of 2-5ml 50%, ultrasonic 2min.
(2) with 0.45 μm of membrane filtration lysate.
(3) it analyzes: taking the filtered solution analysis level HPLC analysis crude product of 3 μ l in order to subsequent preparation.Mobile phase is
HPLC start gradient is first balanced 5min then sample introduction, start gradient water by acetonitrile solution, time 30min, gradient elution
95%, acetonitrile 5% terminates ratio water 5%, acetonitrile 95%.
(4) it prepares: with filtered lysate sample introduction.It prepares HPLC and balances 10min, start gradient water 95%, acetonitrile
5%, terminate ladder: degree water 25%, acetonitrile 75%, gradient timetable 40min.Collect the sample come out from detector.
(5) identify: the sample that will be collected, sampling carry out the identification of purity and MS.
13) solution after purification is lyophilized, obtains finished product.
14) by the polypeptide of white powder, sealed package, -20 degree preservations.
The present invention provides a kind of application, i.e., above-mentioned antibacterial peptide preparation treatment gram-positive bacteria, Gram-negative bacteria,
Application in drug-fast bacteria and the extensive pedigree antibiotic of fungal infection.
The present invention also provides a kind of application, i.e., above-mentioned antibacterial peptide is preparing the application in antibacterial agent.
Specific embodiment
It is further described below by specific embodiment:
Embodiment 1:
1) antibacterial peptide FL15-1 product of the present invention is the amino acid sequence in SEQ ID NO.1, sequence are as follows: Phe-Leu-
Lys-Arg-Leu-Phe-Asp-Lys-Ile-Arg-Gln-Leu-Ile-Arg-Lys。
2) antibacterial peptide FL15-2 product of the present invention is the amino acid sequence in SEQ ID NO.2, sequence are as follows: Phe-Leu-
Lys-Arg-Leu-Phe-Arg-Lys-Ile-Arg-Gln-Leu-Ile-Arg-Lys。
3) antibacterial peptide FL15-3 product of the present invention is the amino acid sequence in SEQ ID NO.3, sequence are as follows: Phe-Leu-
Lys-Arg-Leu-Phe-Arg-Lys-Ile-Arg-Lys-Leu-Ile-Arg-Lys。
Sequence signature: length 15, type are amino acid sequence, and chain is straight chain, artificial synthesized.
The present embodiment antibacterial peptide FL15-1, FL15-2, FL15-3 product is using automatic Peptide synthesizer according to conventional more
Peptide synthesis in solid state, finally obtained antibacterial peptide FL15-1, FL15-2, FL15-3 through efficient liquid phase chromatographic analysis, purity >=
98%.
The measurement of antibacterial peptide VL15, FL15-1, FL15-2, FL15-3 minimal inhibitory concentration (MIC):
Respectively by Escherichia coli (ATCC8739), pseudomonas aeruginosa (CMCC10104), staphylococcus aureus
(ATCC6538), Candida albicans (ATCC10231) cultivates logarithmic phase, is diluted to 5 × 10 with 2 × liquid MHB culture medium5CFU/
ml.The 50 μ l of antibacterial peptide mother liquor for being diluted to gradient is sequentially added in 96 orifice plates, and 50 μ of bacterium solution diluted is added into each hole
L, after mixing in 37 DEG C stationary culture 16 hours, after concussion measure 600nm at absorbance value, with 100 μ g/ml ampicillins
Do positive control.Result judgement: take the hole that can't detect bacterial growth as minimal inhibitory concentration.As a result it is as shown in the table.
Table 1: the MIC value (μM) of antibacterial peptide VL15, FL15-1, FL15-2, FL15-3 to each bacterium
As can be seen from the above table, compared with VL15, improved antibacterial peptide FL15-1, FL15-2, FL15-3 are to gram
Negative and positive bacteria fungistatic effect is all significantly improved, wherein the inhibitory effect to staphylococcus aureus is best, has
Preferable research and development value.
The hemolytic activity of product of the present invention antibacterial peptide VL15, FL15-1, FL15-2, FL15-3 detect:
1) fresh rat blood is acquired, to stratification, upper serum is removed, physiological saline is added, gently with suction pipe
The red blood cell of tube bottom is dispelled, 1000rpm is centrifuged 5min, upper layer physiological saline is carefully drawn with suction pipe and is discarded, until supernatant
Without red.
2) red blood cell 2 for taking bottom to be compacted drips, and red blood cell is resuspended in the isotonic PBS that 2.0ml is added, and it is blood red thin to be configured to 4%
Born of the same parents' suspension.
3) experimental group: being added 50 μ l various concentrations, then the antibacterial peptide dissolved with isotonic PBS is added 50 μ l and configures
4% red blood cell suspension.
4) positive control: the tritonX-100 of 50 μ l 0.2% is added in each hole, and 50 μ l configured 4% are blood red thin
Born of the same parents' suspension.Negative control: the isotonic PBS of 50 μ l, configured 4% red blood cell suspension of 50 μ l is added in each hole.
5) after 37 DEG C of incubation 1h, after 1 000 × g is centrifuged 96 orifice plate 5min, 50 μ l supernatants are drawn into 96 orifice plates from each hole,
415nm wavelength measures A value, calculates percent hemolysis=[(ASample-AIt is negative)/(AIt is positive-AIt is negative)]×100。
The result shows that: under 78.05 μM of concentration, antibacterial peptide VL15 is suitable with negative control to the hemolysis rate of red blood cell；
Under 63.81 μM of concentration, antibacterial peptide FL15-1 is suitable with negative control to the hemolysis rate of red blood cell；In 62.02 μM of concentration
Under, antibacterial peptide FL15-2 is suitable with negative control to the hemolysis rate of red blood cell；Under 496.12 μM of concentration, antibacterial peptide FL15-3
It is suitable with negative control to the hemolysis rate of red blood cell, illustrate antibacterial peptide VL15, FL15-1, FL15-2, FL15-3 of the present invention to red
The osmotic fragility of cell can neglect column and disregard.
Product of the present invention antibacterial peptide VL15, FL15-1, FL15-2, FL15-3 is to the bacteriostatic activity for being clinically separated antibody-resistant bacterium
Measurement:
Using front MIC value measuring method, VL15, FL15-1, FL15-2, FL15-3 are measured respectively to four plants of separate sources
Methicillin-resistant staphylococcus aureus bacteriostatic activity, the results are shown in Table 2.
Table 2: antibacterial peptide VL15, FL15-1, FL15-2, FL15-3 to the antibacterial effect of methicillin-resistant staphylococcus aureus
Fruit
As can be seen from the above table, compared with VL15, improved antibacterial peptide FL15-1, FL15-2, FL15-3 are to different diseases
The methicillin-resistant staphylococcus aureus bacterial strain in people source has apparent fungistatic effect, has splendid Substitutes For Antibiotic
Drug development research value.
Using front MIC value measuring method, VL15, FL15-1, FL15-2, FL15-3 are measured respectively and is caused a disease to aquaculture
Bacterium vibrio parahaemolytious and bacteriostatic activity of the vibrio harveyi bacterial strain when salinity is respectively 0.5% and 1%, the results are shown in Table 3.
The fungistatic effect of table 3 antibacterial peptide VL15, FL15-1, FL15-2, FL15-3 to vibrio parahaemolytious and vibrio harveyi
As can be seen from the above table, compared with VL15, improved antibacterial peptide FL15-1, FL15-2, FL15-3 support aquatic products
Growing pathogenic bacteria vibrio parahaemolytious and vibrio harveyi bacterial strain has apparent fungistatic effect, and fungistatic effect is not substantially by salinity shadow
It rings, is worth with splendid Substitutes For Antibiotic drug development research.
In conclusion antibacterial peptide product of the present invention does not generate hemolytic, has a broad antifungal spectrum, to gram-positive bacteria, gram
Negative bacterium, drug-fast bacteria and fungi all have compared with antibacterial action.So product of the present invention antibacterial peptide FL15-1, FL15-2,
FL15-3 can be obtained in preparing anti-infective gram-positive bacteria, Gram-negative bacteria, drug-fast bacteria and fungal disease drug compared with
Good application.
The foregoing is only a preferred embodiment of the present invention, is not intended to restrict the invention, although referring to aforementioned reality
Applying example, invention is explained in detail, for those skilled in the art, still can be to aforementioned each implementation
Technical solution documented by example is modified or equivalent replacement of some of the technical features.It is all in essence of the invention
Within mind and principle, any modification, equivalent substitution, improvement and etc. done be should all be included in the protection scope of the present invention.
Sequence table
<110>Zun Yi medical university, school district, Zhuhai
<120>a kind of antibacterial peptide and its application
<160> 4
<170> PatentIn version 3.3
<210> 1
<211> 15
<212> PRT
<213>artificial sequence
<400> 1
Phe Leu Lys Arg Leu Phe Asp Lys Ile Arg Gln Leu Ile Arg Lys
1 5 10 15
<210> 2
<211> 15
<212> PRT
<213>artificial sequence
<400> 2
Phe Leu Lys Arg Leu Phe Arg Lys Ile Arg Gln Leu Ile Arg Lys
1 5 10 15
<210> 3
<211> 15
<212> PRT
<213>artificial sequence
<400> 3
Phe Leu Lys Arg Leu Phe Arg Lys Ile Arg Lys Leu Ile Arg Lys
1 5 10 15
<210> 4
<211> 15
<212> PRT
<213>artificial sequence
<400> 4
Val Leu Asn Arg Leu Phe Asp Lys Ile Arg Gln Val Ile Arg Lys
1 5 10 15
Claims (8)
1. a kind of antibacterial peptide, it is characterised in that: the amino acid sequence of the antibacterial peptide is as shown in SEQ ID NO.1, specially benzene
Ala-Leu-Lys-Arg-Ile-Phe-Asn-Lys-isoleucine-arginine-
Glutamine-leucine-isoleucine-arginine-lysine.
2. a kind of antibacterial peptide, it is characterised in that: the amino acid sequence of the antibacterial peptide is as shown in SEQ ID NO.2, specially benzene
Ala-Leu-Lys-Arg-Ile-Phe-arginine-lysine-isoleucine-arginine-paddy
Glutamine-Leu-Ile-arginine-lysine.
3. a kind of antibacterial peptide, it is characterised in that: the amino acid sequence of the antibacterial peptide is as shown in SEQ ID NO.3, specially benzene
Ala-Leu-Lys-Arg-Ile-Phe-arginine-lysine-isoleucine-arginine-relies
Propylhomoserin-Leu-Ile-arginine-lysine.
4. a kind of antibacterial peptide, which is characterized in that the amino acid sequence and SEQ ID NO.1, SEQ ID NO.2 or SEQ ID
NO.3 has the polypeptide of 67% or more homology.
5. a kind of antibacterial peptide as described in claims 1 to 3 is any preparation treatment gram-positive bacteria, Gram-negative bacteria,
Application in drug-fast bacteria and the extensive pedigree antibiotic of fungal infection.
6. a kind of antibacterial peptide as claimed in claim 4 preparation treatment gram-positive bacteria, Gram-negative bacteria, drug-fast bacteria and
Application in the extensive pedigree antibiotic of fungal infection.
7. a kind of antibacterial peptide as described in claims 1 to 3 is any is preparing the application in antibacterial agent.
8. a kind of antibacterial peptide as claimed in claim 4 is preparing the application in antibacterial agent.
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| CN110317248A (en) * | 2019-06-05 | 2019-10-11 | 遵义医科大学珠海校区 | A kind of artificial synthetic antimicrobial peptide and its design method and application |
| CN111729070A (en) * | 2020-06-02 | 2020-10-02 | 遵义医科大学珠海校区 | Application of polypeptide FL15 in preparation of antitumor drugs |
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| US20080125359A1 (en) * | 2006-10-26 | 2008-05-29 | Wang Guangshun | Antimicrobial peptides and methods of identifying the same |
| CN102405053A (en) * | 2009-01-06 | 2012-04-04 | C3剑股份有限公司 | Targeted antimicrobial moieties |
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| US20080125359A1 (en) * | 2006-10-26 | 2008-05-29 | Wang Guangshun | Antimicrobial peptides and methods of identifying the same |
| CN102405053A (en) * | 2009-01-06 | 2012-04-04 | C3剑股份有限公司 | Targeted antimicrobial moieties |
| CN106008677A (en) * | 2016-08-04 | 2016-10-12 | 遵义医学院 | Antibacterial peptide SE37 and application thereof |
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| CN110317248A (en) * | 2019-06-05 | 2019-10-11 | 遵义医科大学珠海校区 | A kind of artificial synthetic antimicrobial peptide and its design method and application |
| CN111729070A (en) * | 2020-06-02 | 2020-10-02 | 遵义医科大学珠海校区 | Application of polypeptide FL15 in preparation of antitumor drugs |
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