CN103539846B - A kind of synthetic polypeptide F of ring-type and anti-bacteria and anti-virus application thereof - Google Patents

A kind of synthetic polypeptide F of ring-type and anti-bacteria and anti-virus application thereof Download PDF

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CN103539846B
CN103539846B CN201310534865.1A CN201310534865A CN103539846B CN 103539846 B CN103539846 B CN 103539846B CN 201310534865 A CN201310534865 A CN 201310534865A CN 103539846 B CN103539846 B CN 103539846B
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synthetic polypeptide
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ring
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bacteria
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CN103539846A (en
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李诗豪
李富花
郭书悦
相建海
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Institute of Oceanology of CAS
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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
    • C07K14/43504—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates
    • C07K14/43509—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates from crustaceans
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans

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Abstract

The present invention relates to a kind of synthetic polypeptide F and anti-bacteria and anti-virus application thereof of ring-type. Does the synthetic polypeptide F of ring-type involved in the present invention have SEQ in sequence list? ID? amino acid sequence shown in No.1 and architectural feature; Is the synthetic polypeptide F of this ring-type derived from SEQ in sequence list? ID? the LPS binding structural domain of the ALFFc of Fenneropenaeus chinensis Anti-LPS factor shown in No.2; Through the synthetic polypeptide F of the ring-type the present invention relates to is carried out to biological function Validation in vitro, confirm that its growth or propagation to gram-positive bacteria, Gram-negative bacteria or virus all has very strong inhibitory action.

Description

A kind of synthetic polypeptide F of ring-type and anti-bacteria and anti-virus application thereof
Technical field
The present invention relates to a kind of synthetic polypeptide F of ring-type and anti-bacteria and anti-virus application thereof, specifically a kind of synthetic derived fromThe ring type polypeptide of lipopolysaccharides (LPS) binding structural domain of Fenneropenaeus chinensis Anti-LPS factor ALFFc and anti-bacteria and anti-virus application thereof.
Background technology
The cultivation of prawn occupies critical role in the culture fishery of China, and in the last few years, the disease in prawn culturing process was askedTopic has seriously hindered the sound development of its breeding production, and the deterioration of antibiotic abuse and environment makes the disease of marine cultured animalEvil is difficult to fundamentally controlled.
Antibacterial peptide (albumen) is considered to the important effect molecule of the external source such as defense against bacterial, the virus pathogen infections such as fish, shrimp, shellfish,In the congenital immunity process of animal, play a significant role. The antibacterial peptide of finding from crustacean is at present of a great variety, and lipotropism is manyThe sugar factor (anti-lipopolysaccharidefactor, ALF) is exactly a kind of important antibacterial peptide wherein. Nineteen eighty-two,Tanaka etc. are first from the blood of Tachypleus tridentatus (Tachypleustridentatus) and North America king crab (Limuluspolyphemus)In cell, separate and obtain ALF, and find that it can suppress the activation of the blood coagulation reaction of LPS mediation. 1985, the discoveries such as MoritaALF also has very strong anti-Gram-negative bacteria activity. Afterwards, people in succession Penaeus monodon (Penaeusmonodon),Crustin (Fenneropenaeuschinensis), Marsupenaeus japonicus (Marsupenaeusjaponicus), all receivingThe multiple crustaceans such as shore prawn (Litopenaeusvannamei), pink shrimp (Farfantepenaeusduorarum)The existence of middle discovery ALF gene, and confirm that the recombinant protein of ALF has anti-Gram-negative bacteria and gram-positive bacteria widelyThe activity of growth. In addition, research also find shrimp white spot syndrome virus (WSSV) in advance with recombinant expressed ALF albumen oneRise after hatching and be injected into again in shrimp body, can suppress copying of WSSV in shrimp body.
Different from the antibiotic mechanism of action of tradition, ALF directly in and the lipopolysaccharides of bacteria cell wall, dissolution of bacteria, therefore notEasy diseaseful drug resistance. ALF is still unclear at present to the viral mechanism of action. Along with antibiotic application, many cause of diseasesBacterium progressively produces drug resistance to existing antibiotic, and the discovery of new antibiotic is extremely difficult, and therefore, the research of ALF is for openingSend out novel antibacterial medicine and opened up wide prospect.
Research find, between two conservative cysteines in ALF amino acid sequence, form disulfide bond, and and between amino acidOne section of anion polypeptide of the common formation of sequence, has the ability of being combined with LPS, and this section of conservative structure called after LPS is in conjunction with knotStructure territory, is considered to the functional domain of ALF degraded gram-negative bacteria cell wall lipopolysaccharides. 2011, SachinSharma etc.Tool 24 amino acid residues synthetic according to the LPS binding structural domain of mud crab (Scyllaserrata) ALF are studiedPolypeptide acts in antibacterial immunity process, finds that synthetic polypeptide SsALF24 has in conjunction with the active of LPS and to Escherichia coli allHave obvious inhibitory action, its MIC is 16.16～32.32uM(SharmaS, YederyRD, PatgaonkarMS,SelvaakumarC,ReddyKV.AntibacterialactivityofasyntheticpeptidethatmimicstheLPSbindingdomainofIndianmudcrab,Scyllaserrataanti-lipopolysaccharidefactor(SsALF)alsoinvolvedinthemodulationofvaginalimmunefunctionsthroughNF-kBsignaling.Microbialpathogenesis2011;50:179-191.）。
Interestingly, the kind of different types of ALF bacterium that polypeptide is resisted and antibacterial activity thereof have significantly poorDifferent, point out us to there is high resistance or special resistance by changing indivedual amino acid whose kinds acquisitions in LPS binding structural domainPeptide molecule. Based on this imagination, our Crustin ALFFc(LiuFS based on having found, LiuYC, LiFH, DongB,XiangJH.MolecularcloningandexpressionprofileofputativeantilipopolysaccharidefactorinChineseshrimp(Fenneropenaeuschinensis).MarineBiotechnology2005; 7:600-608.) the change of the partial amino-acid residue that carries out of LPS binding structural domain, utilizeThe method of chemical synthesis has obtained annular polypeptide F, and this ring type polypeptide has obvious anti-bacteria and anti-virus BA, has heavilyThe application prospect of wanting.
Summary of the invention
The present invention aims to provide a kind of ring-type of the next LPS binding structural domain derived from Fenneropenaeus chinensis Anti-LPS factor ALFFcSynthetic polypeptide F, there is significantly antibacterial and antiviral activity.
Technical scheme of the present invention is as follows:
Utilize the method for chemical synthesis to obtain the synthetic polypeptide F of ring-type, there is the amino acid sequence shown in SEQIDNo.1,Its sequence signature is:
SEQIDNo.1：Ac-Sc(CKYSQKPSFKRWQLYFKGRMWC)P-NH2
The synthetic polypeptide F sequence of described ring-type has disulfide bond structure. Its architectural feature is: synthetic polypeptide F sequence aminoHold between second cysteine (C) and second cysteine of c-terminus (C) and there is disulfide bond structure; The aminoterminal of polypeptideThe amino of S is acetylation (Ac-), and the carboxyl of c-terminus P is amidated (NH2)。
The synthetic polypeptide F of described ring-type, is characterized in that: the synthetic polypeptide F of described ring-type is anti-derived from CrustinThe LPS binding structural domain of lipopolysaccharide factor ALFFc.
The LPS binding structural domain of described Fenneropenaeus chinensis Anti-LPS factor ALFFc, is characterized by: have in sequence listAmino acid sequence shown in SEQIDNo.2, concrete sequence is: ECKFTVKPYIKRFQLYYKGRMWCP.
The synthetic polypeptide F of described ring-type has obvious antimicrobial antiviral activity. Be specially: to gram-positive bacteria, leather orchidThe growth of family name's negative bacterium and virus or propagation all have very strong inhibitory action.
The synthetic polypeptide F of described ring-type can be used as antibacterial and/or antiviral active ingredient, can be used for preparing antibacterial and/or disease-resistantIn the medicine or preparation of poison.
The present invention has the following advantages:
1, the present invention has determined a kind of anti-bacteria and anti-virus polypeptide F and knot thereof derived from Fenneropenaeus chinensis Anti-LPS factor ALFFcStructure feature.
2, can develop the control medicine of effective prawn bacterium class and virus type disease by the present invention.
Brief description of the drawings
The skeleton structure diagram of the synthetic polypeptide F of Fig. 1;
The space structure figure of the synthetic polypeptide F of Fig. 2;
The HPLC purity detecting figure of the synthetic polypeptide F of Fig. 3;
The MS Mass Spectrometric Identification figure of the synthetic polypeptide F of Fig. 4.
Detailed description of the invention
Below in conjunction with embodiment, the present invention is described in further detail.
Chemical synthesis there is an obviously prawn ring type polypeptide F for antibacterial and antiviral activity, its sequence and source sequence informationAs follows:
(1) information of SEQIDNo.1
(a) sequence signature
* length: 24 amino acid
* type: amino acid
* chain: strand
* topological structure: annular, forms disulfide bond between two cysteines
* space structure: have 1) skeleton structure shown in Fig. 1: between two cysteines, be connected by disulfide bond, form ringShape structure, wherein disulfide bond represents with intensification black, C skeleton and other atom represent by grey; With 2) knot of space shown in Fig. 2Structure: peptide sequence forms two connected β-pleated sheet structures.
(b) molecule type: albumen
Sequence description: SEQIDNo.1
Ac-Sc(CKYSQKPSFKRWQLYFKGRMWC)P-NH2
Amino acid in its bracket is into the amino acid of ring, and the small letter c in the outer left side of bracket represents that the amino acid in bracket is formationCirculus amino acid; Ac-represents that the amino of amino acid S is acetylation;-NH2The carboxyl that represents amino acid P is acetylation.
(2) information of SEQIDNo.2
(a) sequence signature
* length: 24 amino acid
* type: amino acid
* chain: strand
* topological structure: linearity
(b) molecule type: albumen
Sequence description: SEQIDNo.2
ECKFTVKPYIKRFQLYYKGRMWCP
Synthetic, cyclisation, purifying, qualification and the Analysis on Biological Activity of described anti-bacteria and anti-virus polypeptide F:
By artificial chemistry route of synthesis, utilize solid phase synthesis process to obtain crude product polypeptide, through solid phase cyclization, Mass Spectrometric Identification and liquidPhase chromatogram purification obtains the synthetic polypeptide F that contains disulfide bond. Be specially:
1) polypeptide is synthetic
Adopt 9-fluorenylmethyloxycarbonyl (Fmoc) synthesis strategy, synthetic to N extreme direction from C end. Use 10mgRink-Amide-ResinResin (AAPPTec, article No. RRZ001), as carrier, relies on active group and the 5mg of carrier itself to be carried out ammonia by FmocFirst amino acid (Fmoc-Pro-NH of base protection2) carboxyl be connected (method detailed bibliography: PanagiotisStathopoulos,SerafimPapas,VassiliosTsikaris.C-terminalN-alkylatedpeptideamidesresultingfromthelinkerdecompositionoftheRinkamideresin.Anewcleavagemixturepreventstheirformation.JournalofPeptideScience2006;12:227-232.）。
With N-methyl adjoin cough up Anhui intoxicated (NMP) rinse resin remove redundant protection amino acid, in reactor (solid phase synthesizer), addEnter 20% piperidines/nmp solution (volume fraction) and remove Fmoc group, reaction 20min, emptying reactor, shakes with 5mLNMPSwing flushing resin, repeat 3 times, remove the Fmoc protection of first amino acid residue; The active amino group exposing with underA carboxyl that is carried out the amino acid (5mg) of amido protecting by Fmoc is connected, and forms first peptide bond (Pro-Cys). This sectionAbove step cycle carry out (difference is: just at every turn need to adopt the corresponding amino acid that is carried out amido protecting by Fmoc)Until peptide sequence Ac-SCKYSQKPSFKRWQLYFKGRMWCP-NH2Synthetic complete, obtain about 20mg linear polypeptide.
2) polypeptide cyclisation
After complete last amino acid of 20mg linear polypeptide coupling, the I of configuration 0.1mol/L2Solution (I2Be dissolved in volume ratio 1:1Methyl alcohol: in DMF mixed solution), add 10mL to solid phase synthesizer, nitrogen brushes reaction, approximately 6 hours.
3) peptide purification and qualification
Cut peptide reagent trifluoroacetic acid with 50mL: thioanisole: phenol: dithioglycol: distilled water (volume ratio 82.5:5:5:2.5:5)The cracking from vector resin of polypeptide after 20mg cyclisation is got off, after 2 hours, add the ether 100ml of 4 DEG C of precoolings to make manyPeptide precipitation, centrifugal collecting precipitate, and with ether washing 3 times, vacuum is drained, the polypeptide crude product obtaining is through reverse phase liquid chromatographyPurifying, carries out HPLC purity detecting (Fig. 3) and Mass Spectrometric Identification (Fig. 4) after the polypeptide freeze-drying after purifying. Detect HPLC chromatogramPost is 250*4.6mm, Kromasil-C18-5 μ m; Mobile phase A: 0.1%TFA/ acetonitrile, Mobile phase B: 0.1%TFA/H2O；Linear elution gradient: 15%A-100%A; Flow velocity is 1ml/min, and detection wavelength is 220nm; Single injected sampling amount is 10 μ l.HPLC and the demonstration of MS testing result, the purity of synthetic polypeptide F is 95.37%, molecular weight is 3098.25, with predicted molecular weight(3094.70) basically identical.
4) bacteriostatic test
Synthetic polypeptide F is dissolved to the PBS of 50mmol/LpH7.4 the solution that concentration is 640 μ mol/L, the while withThe negative contrast of PBS of 50mmol/LpH7.4. Adopt minimum inhibitory concentration (MIC) method to detect synthetic polypeptide to gramNegative bacterium comprises Escherichia coli (Escherichiacoli), Vibrio anguillarum (Vibrioanguillarum) and gram-positive bacteriaComprise pressing down of micrococcus luteus (Micrococcusluteus), micrococcus lysodeikticus (Micrococcuslysodeikticus)Bacterium activity. That is: by Escherichia coli to be measured, micrococcus luteus and micrococcus lysodeikticus respectively at 37 DEG C, under 200r/min condition of cultureIn LB culture medium, be cultured to 1 × 108Cells/mL, Vibrio anguillarum cultivation temperature is 28 DEG C, other condition is the same constant; CultivateBacterium join respectively in 48 well culture plates, with fresh LB culture medium by bacterium liquid dilute to be measured to final concentration 1 × 106Cells/mL; Be 200 μ l to adding respectively polypeptide F solution to the final volume of gradient dilution in 48 well culture plates, polypeptide F eventuallyConcentration be followed successively by 64 μ mol/L, 32 μ mol/L, 16 μ mol/L, 8 μ mol/L, 4 μ mol/L, 2 μ mol/L and1 μ mol/L; With PBS as negative control, the ampicillin of final concentration 58 μ mol/L (Escherichia coli, gamboge microballoonBacterium, micrococcus lysodeikticus) or the kanamycins (Vibrio anguillarum) of 88 μ mol/L respectively as positive control; At 37 DEG C or 28 DEG CUnder condition, cultivate after 3h, add respectively the fresh LB culture medium of 300 μ l, continue to cultivate 18h, measure bacterium in every holeOD600 light absorption value, calculates bacterial concentration.
Result shows, to Gram-negative bacteria, the synthetic polypeptide F of 16-32 μ mol/L can effectively suppress the growth of Vibrio anguillarum,The synthetic polypeptide F of 32-64 μ mol/L can effectively suppress colibacillary growth; To gram-positive bacteria, 16-32 μ mol/LSynthetic polypeptide F can effectively suppress the growth of micrococcus luteus, the synthetic polypeptide F of 32-64 μ mol/L can effectively suppressThe growth of micrococcus lysodeikticus. Illustrate that synthetic polypeptide F has the activity of obvious resisting gram-positive bacteria and negative bacterium.
5) virus neutralization experiment
Press embodiment bacteriostatic test step PBS and dissolve synthetic polypeptide F, use the synthetic polypeptide of final concentration 50 μ mol/L in room temperatureLower and WSSV(whitespotsyndromevirus, white spot syndrome virus) hatch 2h; With haveing nothing to do of same concentrationsPolypeptide (the green fluorescent protein GFP peptide section of equal length) is hatched WSSV under the same conditions as negative control, after hatchingWSSV injects respectively Exopalaemon carinicauda (Exopalaemoncarinicauda), and the injection volume of every tail shrimp is 104Copy WSSV grainSon; Injection is got Exopalaemon carinicauda swimmeret after 24h, adopt the DNA of Tian Gen biochemical technology Co., Ltd extract kit (article No.:DP324) extract total DNA; Gradient dilution WSSV, as standard items, utilizes WSSV copy number to detect primer pair VP28rF(5 '-AAACCTCCGCATTCCTGTGA-3 ') and VP28rR(5 '-TCCGCATCTTCTTCCTTCAT-3 '), adopt realTime fluorescent quantitative PCR technique the increase respectively expression (detection side in detail of VP28 gene in standard items and prawn DNA sample to be measuredMethod bibliography: YumiaoSun, FuhuaLi, JianhaiXiang.AnalysisonthedynamicchangesoftheamountofWSSVinChineseshrimpFenneropenaeuschinensisduringinfection.Aquaculture2013; 376-379:124-132.), be then converted into the copy number of WSSV in prawn DNA sample to be measured.
Result shows, the WSSV copy number of synthetic polypeptide F processed group is 8.68 × 103/ ngDNA, and GFP negative control groupWSSV copy number is 1.50 × 105/ ngDNA, in processed group, the copy number of WSSV is starkly lower than control group, and synthetic polypeptide F is describedThere is obvious antiviral activity.
Discovery and the Biological Activity Identification of this polypeptide F have important application prospect in the exploitation of novel antiviral medicine.

Claims (5)

1. a synthetic polypeptide F for ring-type, is characterized in that: its amino acid sequence is as shown in SEQ ID No .1;
The synthetic polypeptide F sequence of described ring-type has disulfide bond structure, between second cysteine of aminoterminal (C) of polypeptide F and second cysteine of c-terminus (C), has disulfide bond structure.
2. according to the synthetic polypeptide F of ring-type claimed in claim 1, its sequence signature is: the synthetic polypeptide F of described ring-type is derived from the LPS binding structural domain of Fenneropenaeus chinensis Anti-LPS factor ALFFc.
3. according to the synthetic polypeptide F of ring-type claimed in claim 2, it is characterized in that: the LPS binding structural domain of described Fenneropenaeus chinensis Anti-LPS factor ALFFc, its amino acid sequence is the amino acid sequence shown in SEQ ID No .2.
4. the synthetic polypeptide F of the arbitrary described ring-type of claim 1-3, for the preparation of the application in antiviral drug or preparation, is characterized in that:
Growth or the propagation of the synthetic polypeptide F of described ring-type to gram-positive bacteria, Gram-negative bacteria or virus is all inhibited, and it can be used in antibacterial and/or antiviral preparation.
According to the synthetic polypeptide F of ring-type described in claim 4 for the preparation of the application in antiviral drug or preparation, it is characterized in that:
The synthetic polypeptide F of described ring-type can be used as antibacterial and/or antiviral active component, in antibacterial and/or antiviral drug or preparation.
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CN106699860B (en) * 2016-11-22 2021-01-05 中国科学院海洋研究所 Three modified cyclic polypeptides, application thereof and antibacterial preparation
CN106749586B (en) * 2016-11-22 2020-08-11 中国科学院海洋研究所 Modified cyclic polypeptide PV and application and antibacterial preparation thereof

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