CN106749586A - One kind transformation ring type polypeptide PV and its application and antibiotic preparation - Google Patents
One kind transformation ring type polypeptide PV and its application and antibiotic preparation Download PDFInfo
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- CN106749586A CN106749586A CN201611035182.1A CN201611035182A CN106749586A CN 106749586 A CN106749586 A CN 106749586A CN 201611035182 A CN201611035182 A CN 201611035182A CN 106749586 A CN106749586 A CN 106749586A
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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
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- A—HUMAN NECESSITIES
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- A61K38/00—Medicinal preparations containing peptides
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Abstract
The present invention relates to the synthesis polypeptide PV and its antibacterial applications of a kind of ring-type.The synthesis polypeptide PV of ring-type involved in the present invention is respectively with the amino acid sequence and architectural feature shown in SEQ ID No.1 in sequence list；The synthesis polypeptide PV of ring-type is derived from LBDv active peptides shown in SEQ ID No.2 in sequence list；Biological function Validation in vitro is carried out through the synthesis polypeptide PV to ring-type of the present invention, it was demonstrated that its growth or propagation to gram-positive bacteria and Gram-negative bacteria is respectively provided with very strong inhibitory action.
Description
Technical field
The present invention relates to the synthesis polypeptide PV and its antibacterial applications of a kind of ring-type, specifically a kind of synthesis derived from
The structure of modification ring type polypeptide and its antibacterial applications of LBDv active peptides.
Background technology
The cultivation of prawn occupies critical role in the culture fishery of China, in the last few years, during prawn culturing
Disease problem has seriously hindered the sound development of its breeding production, and the abuse of antibiotic makes sea-farming with the deterioration of environment
The disease of animal is difficult to fundamentally be controlled.
Antibacterial peptide (albumen) is considered as the important effect point of the exogenous pathogens such as the defense against bacterial such as fish, shrimp, shellfish, virus infection
Son, plays a significant role during the congenital immunity of animal.The antibacterial peptide species for being found from crustacean at present is various, resists
Lipopolysaccharide factor (anti-lipopolysaccharide factor, ALF) is exactly the important antibacterial peptide of one of which.1982
Year, Tanaka etc. is first from Tachypleus tridentatus (Tachypleus tridentatus) and North America horseshoe crab (Limulus polyphemus)
Isolated ALF in haemocyte, and find the activation of its Coagulation test that can suppress LPS mediations.1985, Morita etc. had found
ALF also has very strong anti-Gram-negative bacteria activity.Afterwards, people in succession Penaeus monodon (Penaeus monodon), in
The bright prawn of state (Fenneropenaeus chinensis), Marsupenaeus japonicus (Marsupenaeus japonicus), vannamei boone
In various crustaceans such as prawn (Litopenaeus vannamei), pink shrimp (Farfantepenaeus duorarum)
It was found that the presence of ALF encoding genes, and confirm that the recombinant protein of ALF genes has extensive anti-Gram-negative bacteria and gram
The activity of positive bacteria growing.In addition, research it has also been found that shrimp white spot syndrome virus (WSSV) in advance with recombination expression ALF eggs
Bai Yiqi is injected into shrimp body again after being incubated, and can substantially suppress the duplication of the WSSV in injection shrimp body.
The mechanism of action from conventional antibiotic is different, and ALF can directly neutralize the lipopolysaccharides of bacteria cell wall, dissolution of bacteria,
Therefore it is difficult to cause the drug resistance of bacterium.The ALF antiviral mechanism of action it is not immediately clear.With the application of antibiotic, perhaps
Many pathogens progressively produce drug resistance to existing antibiotic, and the discovery of new antibiotic is extremely difficult, therefore, ALF's grinds
Study carefully for exploitation novel antibacterial medicine provides important foundation.
Research discovery, forms disulfide bond, the two half Guang ammonia between two Conserved cysteines in ALF amino acid sequences
Amino acid between acid collectively constitutes one section of anionic polypeptides, and with the ability combined with LPS, this section of conservative structure is named
It is LPS binding structural domains, it is considered to be the functional domain of ALF degraded gram-negative bacteria cell wall lipopolysaccharides., Sachin in 2011
Sharma etc. have studied 24 amino of tool synthesized according to the LPS binding structural domains of mud crab (Scylla serrata) ALF
The polypeptide of sour residue is acted on during antibacterial immunity, it is found that synthesis polypeptide SsALF24 has and combined the active of LPS and to big
Enterobacteria all have obvious inhibitory action, its MIC be 16.16~32.32uM (Sharma S, Yedery RD,
Patgaonkar MS, Selvaakumar C, Reddy KV.Antibacterial activity of a synthetic
Peptide that mimics the LPS binding domain of Indian mud crab, Scylla serrata
anti-lipopolysaccharide factor(SsALF)also involved in the modulation of
vaginal immune functions through NF-kB signaling.Microbial pathogenesis 2011；
50∶179-191.)。
Early-stage Study finds that the LPS binding structural domains of ALF have different antibiosis and antiviral functions in Crustin,
The LBDv peptide molecules for obtaining are transformed by the LPS binding structural domains of Crustin ALF and shows significant anti-bacteria and anti-virus
Effect (Yang H, Li SH, Li FH, Xiang JH.Structure and bioactivity of a modified
peptide derived from the LPS-binding domain of an anti-lipopolysaccharide
Factor (alf) of shrimp.Mar.Drugs 2016,14,96；doi：10.3390/md14050096.).Based on what is delivered
The amino acid sequence of active peptides LBDv, the present invention carries out the further transformations, profit such as amino acid substitution, sequence shortening to its sequence
Improved circular polypeptides PV is obtained with the method for chemical synthesis, they show significant antibacterial biological activity, have
Important application prospect.
The content of the invention
The present invention is intended to provide a kind of ring-type synthesis polypeptide PV by structure of modification, there is obvious antibacterial to live for they
Property.
Technical scheme is as follows：
The synthesis polypeptide PV of ring-type is obtained using the method for chemical synthesis, with the amino acid shown in SEQ ID No.1
Sequence, its sequence signature is：
SEQ ID No.1：Ac-c(CKPKFKRWKLKFKKWC)-NH2
The synthesis polypeptide PV sequences of described ring-type have disulfide bond pattern.Its architectural feature is：Synthesis polypeptide PV's
There is disulfide bond pattern between first cysteine (C) of first cysteine (C) of aminoterminal and c-terminus；The amino of polypeptide
The amino of C is held to be acetylation (Ac-), the carboxyl of c-terminus C is amidated (- NH2)。
Described structure of modification of the ring-type synthesis polypeptide PV derived from active peptides LBDv.LBDv is characterised by：Have
Amino acid sequence in sequence list shown in SEQ ID No.2.
The synthesis polypeptide PV of described ring-type has obvious antibacterial activity.Specially：It is blue to gram-positive bacteria and leather
The growth of family name's negative bacterium or propagation are respectively provided with very strong inhibitory action.
The synthesis polypeptide PV of the ring-type, as the active ingredient of antibacterial, can be used to prepare the medicine or preparation of antibacterial
In.
The present invention has the following advantages
1st, present invention determine that a kind of antibacterial polypeptide PV and its architectural feature derived from active peptides LBDv structure of modification.
2nd, the protective agents of effective bacterium class disease can be developed by the present invention.
Brief description of the drawings
The space structure figure of Fig. 1 synthesis polypeptides PV；
The HPLC purity detecting figures of Fig. 2 synthesis polypeptides PV；
The MS Mass Spectrometric Identification figures of Fig. 3 synthesis polypeptides PV.
Specific embodiment
The present invention is described in further detail with reference to embodiment.
A kind of prawn ring type polypeptide PV with obvious antibacterial activity of chemical synthesis, their sequence and derived sequences letter
Breath is as follows：
(1) information of SEQ ID No.1
(a) sequence signature
* length：16 amino acid
* type：Amino acid
* chain：It is single-stranded
* topological structure：Annular, disulfide bond is formed between two cysteines
* space structure：It is connected by disulfide bond between two cysteines, forms cyclic structure, with empty shown in Fig. 1
Between structure：Polypeptide sequence forms two connected β-pleated sheet structures.
(b) molecule type：Albumen
Sequence description：
SEQ ID No.1
Ac-c(CKPKFKRWKLKFKKWC)-NH2
Amino acid in its bracket is the amino acid of cyclization, and the small letter c in the outer left side of bracket represents the amino acid in bracket
To form cyclic structure amino acid；Ac- represents that the amino of amino acid C is acetylation；-NH2Represent the carboxyl of amino acid C by acid amides
Change.
(2) information of SEQ ID No.2
(a) sequence signature
* length：24 amino acid
* type：Amino acid
* chain：It is single-stranded
* topological structure：Annular, disulfide bond is formed between two cysteines
(b) molecule type：Albumen
Sequence description：SEQ ID No.2
Ac-Yc(CKFRVKPKFKRWRLRFKGRMWC)P-NH2
The synthesis of the antibacterial polypeptide PV, cyclisation, purifying, identification and Analysis on Biological Activity：
By artificial chemistry route of synthesis, crude product polypeptide is obtained using solid phase synthesis process, through solid phase cyclization, Mass Spectrometric Identification
The synthesis polypeptide PV containing disulfide bond is obtained with liquid chromatography purification.Specially：
1) Peptide systhesis
Using 9-fluorenylmethyloxycarbonyl (Fmoc) synthesis strategy, from C-terminal to N-terminal direction composition.Use 10mg Rink-Amide-
Resin resins (AAPPTec, article No. RRZ001) carry out ammonia by carrier active group in itself and 5mg as carrier by Fmoc
First amino acid (Fmoc-Pro-NH of base protection2) carboxyl be connected (method detailed bibliography：Panagiotis
Stathopoulos, Serafim Papas, Vassilios Tsikaris.C-terminal N-alkylated peptide
amides resulting from the linker decomposition of the Rink amide resin.A new
cleavage mixture prevents their formation.Journal of Peptide Science 2006；12：
227-232.)。
Adjoined with N- methyl and cough up Anhui intoxicated (NMP) flushing resin removing redundant protection amino acid, to reactor (synthesis in solid state device)
Middle addition 20% piperidines/nmp solution (volume fraction) removing Fmoc groups, react 20min, empty reactor, are shaken with 5mL NMP
Flushing resin is swung, is repeated 3 times, the Fmoc protections of first amino acid residue of removing；The active amine groups for exposing with it is next
The carboxyl of the individual amino acid (5mg) that amido protecting is carried out by Fmoc is connected, and forms first peptide bond (Cys-Trp).This section with
Upper step cycle carries out that (difference is：Simply every time need to be using the corresponding amino acid that amido protecting is carried out by Fmoc) it is straight
To polypeptide sequence Ac-CKPKFKRWKLKFKKWC-NH2Synthesis is finished, and obtains about 20mg linear polypeptides.
2) polypeptide cyclisation
After 20mg linear polypeptides have been coupled last amino acid, the I of 0.1mol/L is configured2Solution (I2It is dissolved in volume ratio 1:
1 methyl alcohol: in DMF mixed solutions), in addition 10mL to synthesis in solid state device, nitrogen brushes reaction, about 6 hours.
3) peptide purification and identification
Peptide reagent trifluoroacetic acid: thioanisole: phenol: dithioglycol is cut with 50mL: distilled water (volume ratio 82.5: 5: 5:
2.5: the polypeptide after 5) 20mg is cyclized is cleaved from vector resin, after 2 hours, adding the ether 100ml of 4 DEG C of precoolings makes
Polypeptide is precipitated, and sediment is collected by centrifugation, and is washed with ether 3 times, and vacuum is drained, and the polypeptide crude product for obtaining is through reverse phase liquid chromatography
Purifying, HPLC purity detectings (Fig. 2) and Mass Spectrometric Identification (Fig. 3) are carried out after polypeptide after purification is lyophilized.Detect that HPLC chromatogram post is
250*4.6mm, Kromasil-C18-5 μm；Mobile phase A：0.1%TFA/ acetonitriles, Mobile phase B：0.1%TFA/H2O；Linearly wash
De- 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 MS is examined
Survey result to show, the purity of synthesis polypeptide PV is 96.05%, and molecular weight is 2193.82, with predicted molecular weight (2193.82)
Cause.
4) bacteriostatic test
It is 640 μm of solution of ol/L that synthesis polypeptide PV is dissolved to concentration with the PBS of 50mmol/LpH7.4 respectively, while with
The PBS of 50mmol/L pH7.4 is negative control.Detect synthesis polypeptide PV to gram using minimum inhibitory concentration (MIC) method
Negative bacterium includes Vibrio harveyi (Vibrio harveyi), Escherichia coli (Escherichia coli), Mermaid luminous bar
Bacterium (Photobacterium damselae subsp.piscicida) and gram-positive bacteria include MRSE
The bacteriostatic activity of bacteriums such as (Staphylococcus epidermidis).I.e.：By Escherichia coli to be measured, MRSE point
Not at 37 DEG C, cultivated to 1 × 10 in LB culture mediums under 200r/min condition of culture8Cells/mL, Vibrio harveyi, mermaid
Luminous bacillus at 30 DEG C, are cultivated to 1 × 10 under 200r/min condition of culture in TSB culture mediums respectively8cells/mL；Culture
Bacterium is added separately in 48 well culture plates, with fresh LB or TSB culture mediums by bacterium solution to be measured be diluted to final concentration 1 ×
106cells/mL；It is 200 μ l, polypeptide H ends to the polypeptide PV solution of gradient dilution to final volume is separately added into 48 well culture plates
Concentration is followed successively by 64 μm of ol/L, 32 μm of ol/L, 16 μm of ol/L, 8 μm of ol/L, 4 μm of ol/L, 2 μm of ol/L and 1 μm of ol/L；Made with PBS
Be negative control, 58 μm of ampicillins of ol/L of final concentration (Escherichia coli, MRSE) or 88 μm of cards of ol/L that
Mycin (Vibrio harveyi, Mermaid luminous bacillus) is respectively as positive control；After 3h being cultivated under the conditions of 37 DEG C or 28 DEG C, point
The fresh LB or TSB culture mediums of 300 μ l not being added, continuing to cultivate 18h, the OD600 light absorption values of bacterium in determining per hole calculate bacterium
Concentration.
Result shows that the 1-2 μm of synthesis polypeptide PV of ol/L can effectively suppress Vibrio harveyi and Mermaid luminous bacillus
Growth, the 2-4 μm of synthesis polypeptide PV of ol/L can effectively suppress the growth of Escherichia coli and MRSE.Result explanation
Synthesis polypeptide PV has the activity of significant resisting gram-positive bacteria and negative bacterium.
The discovery of synthesis polypeptide PV and Biological Activity Identification, have important application preceding in the exploitation of novel antibacterial medicine
Scape.
SEQUENCE LISTING
<110>The Institute of Oceanology of the Chinese Academy of Sciences
<120>One kind transformation ring type polypeptide PV and its application and antibiotic preparation
<130>
<160> 2
<170> PatentIn version 3.5
<210> 1
<211> 16
<212> PRT
<213>It is artificial synthesized
<220>
<221> PRT
<222> (1)..(16)
<223>The amino of 1 and 16 amino acids C is acetylation, carboxyl is amidated
<400> 1
Cys Lys Pro Lys Phe Lys Arg Trp Lys Leu Lys Phe Lys Lys Trp Cys
1 5 10 15
<210> 2
<211> 24
<212> PRT
<213>It is artificial synthesized
<220>
<221> PRT
<222> (1)..(24)
<223>The amino of 2 and 23 amino acids C is acetylation, carboxyl is amidated
<400> 2
Tyr Cys Lys Phe Arg Val Lys Pro Lys Phe Lys Arg Trp Arg Leu Arg
1 5 10 15
Phe Lys Gly Arg Met Trp Cys Pro
20
Claims (7)
1. the synthesis polypeptide PV of a kind of ring-type, it is characterised in that：The synthesis polypeptide PV sequences of described ring-type have disulfide bond knot
Structure, first amino acid residue of aminoterminal (cysteine, C) and c-terminus first amino acid residue (half Guang ammonia of polypeptide PV
Acid, C) between have disulfide bond pattern；
Sequence is the amino acid sequence shown in SEQ ID No.1.
2. according to the synthesis polypeptide PV of the ring-type described in claim 1, it is characterised in that：SEQ ID No.1 are Ac-c
(CKPKFKRWKLKFKKWC)-NH2。
3. according to the synthesis polypeptide PV of the ring-type described in claim 1, it is characterised in that：The synthesis polypeptide PV of described ring-type spreads out
It is conigenous the structure of modification of LBDv active peptides sequences, LBDv has the amino acid sequence shown in SEQ ID No.2 in sequence list.
4. a kind of antibiotic preparation or antibacterials, it is characterised in that：Synthesis polypeptide PV comprising the ring-type described in claim 1.
5. according to the antibiotic preparation or antibacterials described in claim 4, it is characterised in that：It is for Escherichia coli, Ha Wei
A kind of bacterium or more than two kinds bacterium in being selected in the group that the bacteriums such as family name vibrios, Mermaid luminous bacillus, MRSE are constituted
Antiseptic.
6. the application of the synthesis polypeptide PV of the ring-type described in a kind of claim 1, it is characterised in that：The synthesis polypeptide of the ring-type
PV can be used as the active ingredient of antibacterial, and it can be used for antibiotic preparation or antibacterials.
7. according to the application described in claim 6, it is characterised in that：The synthesis polypeptide PV of the ring-type is to Escherichia coli, Kazakhstan
The growth of a kind of bacterium in the bacteriums such as Vickers vibrios, Mermaid luminous bacillus, MRSE or more than two kinds bacterium or propagation
It is respectively provided with inhibitory action.
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| CN201611035182.1A CN106749586B (en) | 2016-11-22 | 2016-11-22 | Modified cyclic polypeptide PV and application and antibacterial preparation thereof |
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| CN201611035182.1A CN106749586B (en) | 2016-11-22 | 2016-11-22 | Modified cyclic polypeptide PV and application and antibacterial preparation thereof |
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Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN113563444A (en) * | 2021-06-02 | 2021-10-29 | 北京师范大学珠海校区 | Polypeptide, application, and shrimp culture feed and drug containing polypeptide |
| CN113831399A (en) * | 2021-06-02 | 2021-12-24 | 北京师范大学珠海校区 | Application of short peptide LBD-Q in preparation of antiviral infection product, feed and medicine |
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| CN101024672A (en) * | 2007-02-12 | 2007-08-29 | 中国科学院昆明动物研究所 | Novel ring-shape small-peptide BA and its use |
| CN103539846A (en) * | 2013-11-01 | 2014-01-29 | 中国科学院海洋研究所 | Circular synthesized polypeptide F and antibacterial and antivirus application thereof |
| CN103539847B (en) * | 2013-11-01 | 2015-07-08 | 中国科学院海洋研究所 | Cyclic synthetic peptide B, and antibacterial and antiviral application thereof |
| CN103539848B (en) * | 2013-11-01 | 2015-07-08 | 中国科学院海洋研究所 | Annular synthetic polypeptide A and application thereof in term of bacteria and virus resistance |
| CN105566452A (en) * | 2016-01-22 | 2016-05-11 | 北京农学院 | Antibacterial peptide with annular structure and preparation method and application thereof |
-
2016
- 2016-11-22 CN CN201611035182.1A patent/CN106749586B/en active Active
Patent Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101024672A (en) * | 2007-02-12 | 2007-08-29 | 中国科学院昆明动物研究所 | Novel ring-shape small-peptide BA and its use |
| CN103539846A (en) * | 2013-11-01 | 2014-01-29 | 中国科学院海洋研究所 | Circular synthesized polypeptide F and antibacterial and antivirus application thereof |
| CN103539847B (en) * | 2013-11-01 | 2015-07-08 | 中国科学院海洋研究所 | Cyclic synthetic peptide B, and antibacterial and antiviral application thereof |
| CN103539848B (en) * | 2013-11-01 | 2015-07-08 | 中国科学院海洋研究所 | Annular synthetic polypeptide A and application thereof in term of bacteria and virus resistance |
| CN105566452A (en) * | 2016-01-22 | 2016-05-11 | 北京农学院 | Antibacterial peptide with annular structure and preparation method and application thereof |
Non-Patent Citations (4)
| Title |
|---|
| HUI YANG等: "Structure and Bioactivity of a Modified Peptide Derived from the LPS-Binding Domain of an Anti-Lipopolysaccharide Factor (ALF) of Shrimp", 《MARINE DRUGS》 * |
| SACHIN SHARMA等: "Antibacterial activity of a synthetic peptide that mimics the LPS binding domain of Indian mud crab, Scylla serrata Anti-lipopolysaccharide Factor (SsALF) also involved in the modulation of vaginal immune functions through NF-kB signaling", 《MICROBIAL PATHOGENESIS》 * |
| SHIHAO LI等: "Characterization and function analysis of an anti-lipopolysaccharide factor (ALF) from the Chinese shrimp Fenneropenaeus chinensis", 《DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY》 * |
| SHIHAO LI等: "Transcriptome Analysis on Chinese Shrimp Fenneropenaeus chinensis during WSSV Acute Infection", 《PLOS ONE》 * |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN113563444A (en) * | 2021-06-02 | 2021-10-29 | 北京师范大学珠海校区 | Polypeptide, application, and shrimp culture feed and drug containing polypeptide |
| CN113831399A (en) * | 2021-06-02 | 2021-12-24 | 北京师范大学珠海校区 | Application of short peptide LBD-Q in preparation of antiviral infection product, feed and medicine |
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| CN106749586B (en) | 2020-08-11 |
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