CN106749586B - Modified cyclic polypeptide PV and application and antibacterial preparation thereof - Google Patents
Modified cyclic polypeptide PV and application and antibacterial preparation thereof Download PDFInfo
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- CN106749586B CN106749586B CN201611035182.1A CN201611035182A CN106749586B CN 106749586 B CN106749586 B CN 106749586B CN 201611035182 A CN201611035182 A CN 201611035182A CN 106749586 B CN106749586 B CN 106749586B
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Abstract
The invention relates to a cyclic synthetic polypeptide PV and antibacterial application thereof. The circular synthetic polypeptide PV related by the invention has the amino acid sequence and the structural characteristics shown in SEQ ID No.1 in a sequence list respectively; the cyclic synthetic polypeptide PV is derived from an LBDv active polypeptide shown as SEQ ID No.2 in a sequence list; the biological function in vitro verification of the cyclic synthetic polypeptide PV provided by the invention proves that the cyclic synthetic polypeptide PV has a strong inhibiting effect on the growth or proliferation of gram-positive bacteria and gram-negative bacteria.
Description
Technical Field
The invention relates to a cyclic synthetic polypeptide PV and antibacterial application thereof, in particular to a synthetic structurally-modified cyclic polypeptide derived from LBDv active polypeptide and antibacterial application thereof.
Background
The culture of prawns plays an important role in the aquaculture industry of China, in recent years, the disease problem in the process of prawn culture seriously hinders the healthy development of the culture production of the prawns, and the abuse of antibiotics and the deterioration of the environment make the disease of mariculture animals difficult to be controlled fundamentally.
The antibacterial peptide (protein) is considered to be an important effector molecule for defending fish, shrimps, shellfish and the like from exogenous pathogenic infection such as bacteria, viruses and the like, and plays an important role in the innate immune process of animals. Currently, many kinds of antibacterial peptides are found in crustaceans, and an anti-lipopolysaccharide factor (ALF) is an important antibacterial peptide. In 1982, Tanaka et al isolated ALF from blood cells of Tachypleus tridentatus (Tachypleus tridentatus) and Tachypleus tridentatus (Limulus polyphemus) for the first time and found that it could inhibit the activation of LPS-mediated coagulation reaction. In 1985, Morita et al found that ALF also had strong activity against gram-negative bacteria. Then, it was successively found that the ALF-encoding gene existed in several crustaceans such as Penaeus monodon (Penaeus monodon), Penaeus chinensis (Fenneropenaeus chinensis), Penaeus japonicus (Marsupenaus japonica), Litopenaeus vannamei (Litopenaeus vannamei), and Penaeus persiciformis (Farfantepenaeus durarium), and it was confirmed that the recombinant protein of the ALF gene had a wide range of activities against the growth of gram-negative bacteria and gram-positive bacteria. In addition, the research also finds that the prawn White Spot Syndrome Virus (WSSV) can obviously inhibit the replication of the WSSV injected into the prawn bodies after being incubated with the recombinant expressed ALF protein in advance and then injected into the prawn bodies.
Unlike the action mechanism of traditional antibiotics, ALF can directly neutralize lipopolysaccharide on bacterial cell walls and dissolve bacteria, so that the bacterial drug resistance is not easy to cause. The mechanism of action of ALF antiviral is currently unknown. With the application of antibiotics, many pathogenic bacteria gradually generate drug resistance to the existing antibiotics, and the discovery of novel antibiotics is extremely difficult, so the research of ALF provides an important basis for developing novel antibacterial drugs.
The research finds that disulfide bonds are formed between two conserved cysteines in the ALF amino acid sequence, the amino acids between the two cysteines jointly form a section of anionic polypeptide, the anionic polypeptide has the capacity of being combined with LPS, and the conserved structure is named as LPS binding domain and is considered as a functional domain of ALF for degrading lipopolysaccharide on the cell wall of gram-negative bacteria. In 2011, SachinSharma et al studied the effect of a polypeptide with 24 amino acid residues synthesized from the LPS-binding domain of Scylla serrata (ALF) during the course of antibacterial immunization, found that the synthetic polypeptide SsALF24 has LPS-binding activity and significant inhibitory effect on Escherichia coli, with a minimum inhibitory concentration of 16.16-32.32uM (Sharma S, Yeast RD, Patganonkar MS, Selvaakumar C, Reddy KV. antibacterial activity of a synthetic peptide which binds the LPS binding domain of Indian mu rod, Scyla seratanti-lipolysis factor (SsALF) adsorbed protein modification of microorganism strain, 191.179: 50. Biotin strain F: 179).
Earlier researches found that the LPS binding domain of ALF in Penaeus chinensis has different antibacterial and antiviral effects, and LBDv polypeptide molecules obtained by modifying the LPS binding domain of the ALF of Penaeus chinensis show significant antibacterial and antiviral effects (Yang H, Li SH, Li FH, Xiaoing JH. structure and biological activity of modified and derived from the LPS-binding domain of an anti-i-lipopolysacchareid effector (ALF) of shrimp. Mar. drugs 2016,14, 96; and doi:10.3390/md 14050096.). Based on the published amino acid sequence of the active polypeptide LBDv, the invention carries out further modification such as amino acid substitution, sequence shortening and the like on the sequence, obtains the modified annular polypeptide PV by utilizing a chemical synthesis method, and the modified annular polypeptide PV shows remarkable antibacterial biological activity and has important application prospect.
Disclosure of Invention
The invention aims to provide a structurally modified cyclic synthetic polypeptide PV, which has obvious antibacterial activity.
The technical scheme of the invention is as follows:
the circular synthesized polypeptide PV is obtained by a chemical synthesis method, has an amino acid sequence shown in SEQ ID No.1, and has the sequence characteristics that:
SEQ ID No.1：Ac-c(CKPKFKRWKLKFKKWC)-NH2
the cyclic synthetic polypeptide PV sequence has a disulfide bond structure. The structure is characterized in that: a disulfide bond structure is formed between the first amino-terminal cysteine (C) and the first carboxyl-terminal cysteine (C) of the synthetic polypeptide PV; the amino group of the amino-terminal C of the polypeptide is acetylated (Ac-), and the carboxyl group of the carboxyl-terminal C is amidated (-NH)2)。
The cyclic synthetic polypeptide PV is derived from the structural modification of the active polypeptide LBDv. LBDv is characterized by: has an amino acid sequence shown as SEQ ID No.2 in a sequence list.
The cyclic synthetic polypeptide PV has obvious antibacterial activity. The method specifically comprises the following steps: has strong inhibiting effect on the growth or proliferation of gram-positive bacteria and gram-negative bacteria.
The cyclic synthetic polypeptide PV can be used as an antibacterial active ingredient and can be used for preparing antibacterial medicines or preparations.
The invention has the following advantages
1. The invention determines an antibacterial polypeptide PV derived from the structural modification of an active polypeptide LBDv and the structural characteristics thereof.
2. The invention can be used for developing effective prevention and treatment medicines for bacterial diseases.
Drawings
FIG. 1 is a spatial structure diagram of a synthetic polypeptide PV;
FIG. 2 HPLC purity assay chart of synthetic polypeptide PV;
FIG. 3 is a MS mass spectrum identification chart of the synthesized polypeptide PV.
Detailed Description
The present invention will be described in further detail with reference to examples.
Chemically synthesized prawn cyclic polypeptide PV with obvious antibacterial activity has the following sequence and source sequence information:
(1) information of SEQ ID No.1
(a) Sequence characterization
Length: 16 amino acid
Type: amino acids
Chain type: single strand
Topology structure: circular, disulfide bond formation between two cysteines
Spatial structure: two cysteines are linked by a disulfide bond to form a cyclic structure having the spatial structure shown in FIG. 1: the polypeptide sequence forms two linked beta sheet structures.
(b) Molecular type: protein
Description of the sequence:
SEQ ID No.1
Ac-c(CKPKFKRWKLKFKKWC)-NH2
wherein the amino acid in the parentheses is a cyclic amino acid, and the lower case c on the left side outside the parentheses indicates that the amino acid in the parentheses is an amino acid forming a cyclic structure; ac-represents that the amino group of amino acid C is acetylated; -NH2Indicates that the carboxyl group of the amino acid C is amidated.
(2) Information of SEQ ID No.2
(a) Sequence characterization
Length: 24 amino acid
Type: amino acids
Chain type: single strand
Topology structure: circular, disulfide bond formation between two cysteines
(b) Molecular type: protein
Description of the sequence: SEQ ID No.2
Ac-Yc(CKFRVKPKFKRWRLRFKGRMWC)P-NH2
The synthesis, cyclization, purification, identification and biological activity analysis of the antibacterial polypeptide PV are as follows:
the synthetic polypeptide PV containing disulfide bonds is obtained by a synthetic chemical synthesis way, a solid-phase synthesis method is utilized to obtain crude polypeptide, and solid-phase cyclization, mass spectrum identification and liquid chromatography purification are carried out. The method specifically comprises the following steps:
1) polypeptide synthesis
Adopting a 9-fluorenylmethyloxycarbonyl (Fmoc) synthesis strategy to synthesize from the C end to the N end. 10mg of Rink-Amide-Resin (AAPPtec, cat # RRZ001) was used as a carrier, depending on the active group of the carrier itself and 5mg of the first amino acid (Fmoc-Pro-NH) amino-protected by Fmoc2) To the carboxyl group (detailed process reference: panagiotisis Stathopoulos, Serafim Papas, Valisios Tsidars.C-terminal N-alkylated peptidamides reactivating from the linker composition of the Rink amine resin.A new clearage mixture compositions the formulation journal of Peptide Science 2006; 12:227-232.).
The resin was washed with N-methyl pyrrolidine Anhui urea (NMP) to remove excess protected amino acids, and 20% piperidine/NMP solution (vol/vol) was added to the reactor (solid phase synthesizer)Fraction) removing Fmoc group, reacting for 20min, emptying the reactor, oscillating and washing the resin by 5mL of NMP, repeating for 3 times, and removing Fmoc protection of the first amino acid residue; the exposed reactive amino group was attached to the carboxyl group of the next amino acid (5mg) amino-protected by Fmoc to form the first peptide bond (Cys-Trp). This sequence of steps is repeated (except that each time the corresponding amino acid protected by Fmoc is used) until the polypeptide sequence Ac-CKPKFKRWKLKFKKWC-NH is reached2After synthesis, about 20mg of linear polypeptide was obtained.
2) Polypeptide cyclisation
After 20mg of linear polypeptide is coupled with the last amino acid, 0.1mol/L of I is prepared2Solution (I)2Methanol dissolved in a volume ratio of 1: DMF mixed solution), 10mL was added to a solid phase synthesizer, and the reaction was blown with nitrogen for about 6 hours.
3) Polypeptide purification and characterization
Trifluoroacetic acid with 50mL of peptide-cleaving reagent: thioanisole: phenol: ethanedithiol: double distilled water (volume ratio 82.5:5:5:2.5:5) is used for cracking 20mg of cyclized polypeptide from a carrier resin, after 2 hours, 100ml of ether precooled at 4 ℃ is added to precipitate the polypeptide, the precipitate is collected by centrifugation and washed for 3 times by ether, vacuum pumping is carried out, the obtained crude polypeptide is purified by reverse liquid chromatography, and the purified polypeptide is freeze-dried and then subjected to HPLC purity detection (figure 2) and mass spectrum identification (figure 3). Detecting the HPLC chromatographic column to be 250 x 4.6mm, Kromasil-C18-5 μm; mobile phase A: 0.1% TFA/acetonitrile, mobile phase B: 0.1% TFA/H2O; linear elution gradient: 15% A-100% A; the flow rate is 1ml/min, and the detection wavelength is 220 nm; the amount of the sample to be added at one time was 10. mu.l. HPLC and MS detection results show that the purity of the synthesized polypeptide PV is 96.05%, the molecular weight is 2193.82, and the molecular weight is consistent with the predicted molecular weight (2193.82).
4) Bacteriostasis test
The synthesized polypeptide PV was dissolved in a concentration of 640. mu. mol/L with 50mmol/L PBS (pH7.4), and a negative control was made with 50mmol/L PBS (pH7.4). Detecting the gram-negative bacteria including Vibrio harveyi, Escherichia coli and mermaid by using Minimum Inhibitory Concentration (MIC) methodThe antibacterial activity of Bacillus subtilis and gram-positive bacteria including Staphylococcus epidermidis is obtained by culturing Escherichia coli and Staphylococcus epidermidis to be detected in LB culture medium at 37 deg.C and 200r/min to 1 × 108cells/mL, Vibrio harveyi and Photobacterium mermairei are respectively cultured in TSB culture medium at 30 ℃ and 200r/min to 1 × 108cells/mL, respectively adding the cultured bacteria into 48-hole culture plates, and diluting the bacterial liquid to be detected to the final concentration of 1 × 10 by using fresh LB or TSB culture medium6cells/mL; adding the polypeptide PV solution which is diluted in a gradient way into a 48-hole culture plate respectively until the final volume is 200 mu L, wherein the final concentration of the polypeptide PV is 64 mu mol/L, 32 mu mol/L, 16 mu mol/L, 8 mu mol/L, 4 mu mol/L, 2 mu mol/L and 1 mu mol/L in sequence; PBS was used as a negative control, and ampicillin (E.coli, Staphylococcus epidermidis) with a final concentration of 58. mu. mol/L or kanamycin (Vibrio harveyi, Photobacterium mermairei) with a final concentration of 88. mu. mol/L were used as positive controls, respectively; after culturing at 37 ℃ or 28 ℃ for 3 hours, 300. mu.l of fresh LB or TSB medium was added, respectively, and the culture was continued for 18 hours, and the OD600 absorbance of the bacteria in each well was measured to calculate the bacterial concentration.
The result shows that 1-2 mu mol/L of the synthetic polypeptide PV can effectively inhibit the growth of Vibrio harveyi and Photobacterium mermairei, and 2-4 mu mol/L of the synthetic polypeptide PV can effectively inhibit the growth of Escherichia coli and Staphylococcus epidermidis. The results indicate that the synthetic polypeptide PV has significant activity against gram-positive and gram-negative bacteria.
The discovery and the biological activity identification of the synthetic polypeptide PV have important application prospects in the development of novel antibacterial drugs.
SEQUENCE LISTING
<110> oceanographic institute of Chinese academy of sciences
<120> modified cyclic polypeptide PV, application thereof and antibacterial preparation
<130>
<160>2
<170>PatentIn version 3.5
<210>1
<211>16
<212>PRT
<213> Artificial Synthesis
<220>
<221>PRT
<222>(1)..(16)
<223> amino group of amino acid C at positions 1 and 16 is acetylated, carboxyl group 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> Artificial Synthesis
<220>
<221>PRT
<222>(1)..(24)
<223> amino group of amino acid C at positions 2 and 23 is acetylated, and carboxyl group 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 (5)
1. A circular synthetic polypeptide PV, the sequence of which is an amino acid sequence shown in SEQ ID No.1, specifically is: SEQ ID No.1 is Ac-c (CKPKFKRWKLKFKKWC) -NH2The sequence is characterized in that: the annular synthesized polypeptide PV sequence has a disulfide bond structure, and a disulfide bond structure is formed between amino-terminal cysteine residues and carboxyl-terminal cysteine residues of the polypeptide PV.
2. An antibacterial agent or an antibacterial drug, characterized in that: comprising the cyclic synthetic polypeptide PV of claim 1.
3. An antibacterial preparation or medicament according to claim 2, characterised in that: the cyclic synthetic polypeptide PV is prepared into an antibacterial agent or an antibacterial drug which comprises one or more than two of Escherichia coli, Vibrio harveyi, Photobacterium mermairei and staphylococcus epidermidis.
4. Use of the cyclic synthetic polypeptide PV of claim 1, wherein: the cyclic synthetic polypeptide PV is used as an antibacterial active ingredient and is used for preparing antibacterial preparations or antibacterial drugs.
5. Use according to claim 4, characterized in that: the annular synthetic polypeptide PV has an inhibitory effect on the growth or proliferation of one or more than two of Escherichia coli, Vibrio harveyi, Photobacterium mermairei and Staphylococcus epidermidis in vitro.
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| CN113831399B (en) * | 2021-06-02 | 2022-04-12 | 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 |
| CN113563444B (en) * | 2021-06-02 | 2022-02-01 | 北京师范大学珠海校区 | Polypeptide, application, and shrimp culture feed and drug containing polypeptide |
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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 (5)
| Title |
|---|
| 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;Sachin Sharma等;《Microbial Pathogenesis》;20111231;第50卷(第3-4期);第179-191页 * |
| Characterization and function analysis of an anti-lipopolysaccharide factor (ALF) from the Chinese shrimp Fenneropenaeus chinensis;Shihao Li等;《Developmental and Comparative Immunology》;20140528;第46卷(第2期);第351页第2.4小节，第2.6小节，第353页表2 * |
| Shihao Li等.Characterization and function analysis of an anti-lipopolysaccharide factor (ALF) from the Chinese shrimp Fenneropenaeus chinensis.《Developmental and Comparative Immunology》.2014,第46卷(第2期), * |
| Structure and Bioactivity of a Modified Peptide Derived from the LPS-Binding Domain of an Anti-Lipopolysaccharide Factor (ALF) of Shrimp;Hui Yang等;《marine drugs》;20160519;第14卷(第5期);第1页摘要，第2页表1，第7页表3 * |
| Transcriptome Analysis on Chinese Shrimp Fenneropenaeus chinensis during WSSV Acute Infection;Shihao Li等;《PLOS one》;20130331;第8卷(第3期);第1-15页 * |
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