Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

Green mud crab antibacterial peptide Sphistin and application thereof

A technology of antimicrobial peptides and antibacterial peptides, which is applied in the antimicrobial peptide Sphistin and its application fields, can solve the problems of negative effects of drug resistance of pathogenic bacteria, application limitations, etc., achieve significant antibacterial effect, fast sterilization rate, The effect of broad application prospects

Active Publication Date: 2011-08-31
XIAMEN UNIV
View PDF1 Cites 26 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

In the exploration of disease control methods, traditional antibiotics cause drug resistance of pathogenic bacteria and negative effects on the environment, making them face serious challenges, and their application is increasingly restricted

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Green mud crab antibacterial peptide Sphistin and application thereof
  • Green mud crab antibacterial peptide Sphistin and application thereof
  • Green mud crab antibacterial peptide Sphistin and application thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0031] Example 1 Preparation of Sphistin, an antimicrobial peptide from Scylla pseudocaveae

[0032] Sphistin is derived from the partial N-terminal sequence of the histone H2A of the mud crab, consisting of 38 amino acids. The specific amino acid sequence is:

[0033] Met Ala Gly Gly Lys Ala Gly Lys Asp Ser Gly Lys Ala Lys Ala Lys

[0034] 1 5 10 15

[0035] Ala Val Ser Arg Ser Ala Arg Ala Gly Leu Gln Phe Pro Val Gly Arg

[0036] 20 25 30

[0037] Ile His Arg His Leu Lys

[0038] 35

[0039] The nucleotide sequence of Sphistin, an antimicrobial peptide from Scylla pseudocaveus, is:

[0040] atggctggtg gcaaggcagg caaggactcc ggcaaggcga aagccaaggc agtatcacgc 60

[0041] tcggccagggg ctggtctgca gtttcctgtc ggtcgtatcc atagacacct gaag 114

[0042] The molecular formula of the antibacterial polypeptide is C 170 h 293 N 61 o 46 S 1 , the molecular weight is 3959.61. The 38 amino acids of the antimicrobial peptide contain 10 positively charged amino acid residues and 1 nega...

Embodiment 2

[0044] Example 2 Determination of the minimum inhibitory concentration (MIC: minimum inhibition concentration) of the antimicrobial peptide Sphistin

[0045] (a) The preserved species of Escherichia coli, Escherichia coli MC1061, Staphylococcus epidermidis, Staphylococcus aureus, Corynebacterium glutamicum, Micrococcus lyticus, Bacillus subtilis, Bacillus cereus, Micrococcus luteus, Shiga Bacteria, Pseudomonas stutzeri, and Pseudomonas aeruginosa were streaked on the nutrient broth plate; The temperature was inverted for 12-16 hours; Candida albicans and Pichia pastoris were streaked on the YPG plate, and cultured at 28°C for 1-2 weeks. All the bacteria were inoculated on the corresponding slant, and the culture was continued for 12-16 hours, and the yeast was continued for 3-7 days; the freshly prepared bacterial slant culture was washed with 10mM sodium phosphate buffer (pH 7.4), and the dilution was adjusted to OD 600 =0.003; Vibrio was adjusted and diluted to OD with seaw...

Embodiment 3

[0062] Example 3 Determination of the minimum bactericidal concentration (MBC: minimum bactericidal concentration) of the antimicrobial peptide Sphistin

[0063] (a) The preserved species of Escherichia coli, Escherichia coli MC1061, Staphylococcus epidermidis, Staphylococcus aureus, Corynebacterium glutamicum, Micrococcus lyticus, Bacillus subtilis, Micrococcus luteus, Shigella, Shigella Pseudomonas, Aeromonas hydrophila, and Pseudomonas fluorescens were streaked on the nutrient broth plate, and cultured upside down at the corresponding temperature for 12-16 hours; Pichia pastoris was streaked on the YPG plate, and cultured at 28°C for one to two weeks. All the bacteria were inoculated on the corresponding slant, and the culture was continued for 12-16 hours, and the yeast was continued for 3-7 days; the freshly prepared bacterial slant culture was washed with 10mM sodium phosphate buffer (pH 7.4), and the dilution was adjusted to OD 600 =0.003; Yeast is adjusted to OD 600 ...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

PUM

PropertyMeasurementUnit
molecular weightaaaaaaaaaa
Login to View More

Abstract

The invention discloses a green mud crab antibacterial peptide Sphistin and application thereof, relates to the technical field of genetic engineering of crustaceans, and provides the green mud crab antibacterial peptide Sphistin and the application thereof. A molecular formula of the green mud crab antibacterial peptide Sphistin is C170H293N61O46S1 and molecular weight of the green mud crab antibacterial peptide Sphistin is 3,959.61 Dalton. The antibacterial peptide Sphistin consists of 38 amino acids, is derived from a part of sequences at end N of green mud crab histone 2A protein and is apolypeptide with an antibacterial function. By adopting the conventional solid-phase chemical synthesis method, the green mud crab antibacterial peptide Sphistin with purity of over 95 percent can beobtained. The green mud crab antibacterial peptide Sphistin has an obvious antibacterial effect on various gram negative bacteria and gram positive bacteria, has a broad antibacterial spectrum and high sterilization rate, shows extremely high medical value and is excellently applied to preparing antibacterial agents.

Description

technical field [0001] The invention relates to the technical field of crustacean genetic engineering, in particular to Sphistin, an antibacterial peptide of Scylla pseudocaveus, and its application. Background technique [0002] In recent years, with the rapid growth of the world's population and the improvement of people's consumption of aquatic products, the aquaculture industry has developed rapidly. However, high-density farming has caused frequent occurrence of aquatic animal diseases, and some diseases have even caused a devastating blow to the aquaculture industry. . In the exploration of disease control methods, traditional antibiotics cause drug resistance of pathogenic bacteria and negative effects on the environment, making them face serious challenges, and their application is increasingly limited. Antimicrobial peptides have the advantages of specifically killing pathogenic microorganisms, will not cause pathogenic bacteria to develop drug resistance, and will...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

Application Information

Patent Timeline
no application Login to View More
Patent Type & Authority Applications(China)
IPC IPC(8): C07K14/435C12N15/12C07K1/04A61K38/17A61P31/04A61P31/10A23K1/16A23K20/147
Inventor 王克坚范丹青蔡灵
Owner XIAMEN UNIV
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic, Popular Technical Reports.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com