Litopenaeus vannamei haemocyanin antibacterial peptide and applications thereof

A technology of hemocyanin and antimicrobial peptides, which can be applied in the direction of antibacterial drugs, peptide/protein components, peptides, etc., can solve the problems of low efficiency of shrimp farming industry, insufficient development momentum, and unoptimistic prospects for sustainable development.

Inactive Publication Date: 2017-12-22
SHANTOU UNIV
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, compared with the international shrimp farming industry, the relative efficiency of the shrimp farming industry in our country and our province is relatively low, the development stamina is insufficient, and the prospect of sustainable development is not optimistic

Method used

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  • Litopenaeus vannamei haemocyanin antibacterial peptide and applications thereof
  • Litopenaeus vannamei haemocyanin antibacterial peptide and applications thereof
  • Litopenaeus vannamei haemocyanin antibacterial peptide and applications thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0020] Example 1 Prediction of Litopenaeus vannamei Hemocyanin Antimicrobial Peptide

[0021] Firstly, three online prediction software, AntiBP Server, CAMP, and APD2, were used to predict the large and small subunit antimicrobial peptides of Litopenaeus vannamei hemocyanin, as shown in Table 1 and Table 2. A total of 34 antibacterial peptides with possible antibacterial activity were predicted Small molecular fragments, among which 11 polypeptide sequences (indicated in bold) may form an α-helical structure and can interact with pathogenic bacteria membranes to exert antibacterial effects. The predicted molecular weight of these polypeptides ranges from 1.5 to 1.9 kDa. In addition, the prediction results showed that there were active fragments in the α-helical domain at the N-terminus of hemocyanin, the Ig-like domain at the C-terminus, and the conserved copper ion-binding domain in the middle, of which the copper-ion-binding domain and the Ig-like domain accounted for the mai...

Embodiment 2

[0030] Example 2 Analysis of Litopenaeus vannamei Hemocyanin Antimicrobial Peptide Secondary Structure Content by Circular Dichroism

[0031] The 11 peptides described in Implementation 1 (the bolded peptides in Table 1 and Table 2) that may form an α-helical structure and can interact with pathogenic bacteria membranes to exert antibacterial effects were scanned by circular dichroism chromatography, and analyzed its structural content.

[0032] 2.1 Experimental equipment

[0033] 2.1.1 Experimental materials

[0034] The polypeptide used in the experiment was synthesized by Beijing Zhongke Yaguang Biotechnology Co., Ltd. The N-terminal acetylation and C-terminal amidation of the polypeptide were modified, and the purity was >95%. A total of 11 antimicrobial peptides, numbered S7, S8, S9, S10, B1, B2, B3, B9, B11, B13, B14.

[0035] 2.1.2 Experimental Instruments

[0036] Ultraviolet spectrophotometer (UV5200) manufacturer: Shanghai Yuanxi Instrument Co., Ltd.

[0037] Ci...

Embodiment 3

[0075] Embodiment 3 adopts plate count method to verify the bacteriostatic activity of antimicrobial peptide B2

[0076] 3.1 Experimental materials

[0077] 3.1.1 Experimental materials

[0078] The polypeptide used in the experiment was synthesized by Beijing Zhongke Yaguang Biotechnology Co., Ltd. The N-terminal acetylation and C-terminal amidation of the polypeptide were modified, and the purity was >95%.

[0079] The pathogenic bacteria in the experimental aquatic products were Vibrio, Alginolyticus, Escherichia coli, Aeromonas hydrophila, Vibrio parahaemolyticus, Streptococcus B and Staphylococcus aureus, all of which were preserved in our laboratory. strains.

[0080] 3.1.2 Main reagents

[0081] Bovine tryptone, beef extract, agar powder, sodium chloride, and sodium hydroxide were purchased from Guangzhou Weijia Technology Co., Ltd.

[0082] 3.1.3 Solution preparation

[0083] 3.1.3.1 Artificially synthesized peptide solution

[0084] 1.0 mg / mL peptide solution: t...

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Abstract

The present invention discloses a litopenaeus vannamei haemocyanin antibacterial peptide, which has the amino acid sequence represented by SEQ ID NO:1 in the sequence table, and has the molecular weight of 1837 Da. The invention further discloses applications of the litopenaeus vannamei haemocyanin antibacterial peptide, particularly applications of the litopenaeus vannamei haemocyanin antibacterial peptide in preparation of drugs for treatment or prevention of bacteria. According to the present invention, the foundation is established for the subsequent further study on the immunologic defence mechanism of litopenaeus vannamei and the development of antibacterial drugs.

Description

technical field [0001] The invention relates to the technical field of aquaculture, in particular to a hemocyanin antibacterial peptide of Litopenaeus vannamei and its application. Background technique [0002] In recent years, with the development of the economy, people's demand for aquatic products is increasing day by day. Under the condition that the catch cannot meet the market demand, the aquaculture industry has developed rapidly. Shrimp is one of the fastest-growing products in aquaculture, and my country is the country with the highest annual output of aquaculture shrimp. However, compared with the international shrimp farming industry, the relative efficiency of the shrimp farming industry in our country and our province is relatively low, the development stamina is insufficient, and the prospect of sustainable development is not optimistic. The reason is mainly related to the frequent occurrence of prawn farming diseases in my country and the repeated trade barri...

Claims

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Application Information

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IPC IPC(8): C07K14/795A61K38/10A61P31/04
CPCA61K38/00C07K14/795Y02A50/30
Inventor 章跃陵黄河杨燊刘尚杰伦镜盛
Owner SHANTOU UNIV
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