Epinephelus malabaricus Piscidin transformation body antimicrobial peptide and application thereof

Abstract

The present invention provides an epinephelus malabaricus Piscidin transformation body antimicrobial peptide, an encoding gene thereof and a recombinant expression vector containing the encoding gene. The epinephelus malabaricus Piscidin transformation body antimicrobial peptide maintains bactericidal activity close to that of natural antibacterial peptide piscidin, meanwhile significantly reduces rabbit red blood cell hemolytic activity and cytotoxicity on human embryonic kidney cells, and has good application prospects.

Description

technical field [0001] The invention belongs to the field of biotechnology, and in particular relates to an antibacterial peptide and its application. Background technique [0002] The abuse and large doses of current chemicals and antibiotics can easily increase the number of drug-resistant strains. The imbalance of flora and cross-infection in hospitals have become a major problem in hospitals and seriously endanger human health. Environmental deterioration and the greenhouse effect have also accelerated the evolution of drug-resistant and vaccine-resistant pathogen strains (Peneau et al., 2007), and the discovery of antimicrobial peptides provides a new direction for solving these problems. Antimicrobial peptides are a class of small molecular polypeptides with broad-spectrum antimicrobial activity, widely exist in the biological world, and are important non-specific immune factors in the innate immune system. Antimicrobial peptides have the characteristics of small mole...

AI Technical Summary

Problems solved by technology

According to the contradictory relationship between the hydrophilicity and hydrophobicity of piscidin itself, antibacterial activity and hemolytic activity, it is necessary to deduce that the hydrophobicity of the polypeptide sequence should be appropriately reduced to enhance its hydrophilicity, and at the same time maintain its high-performance bactericidal activity. How should it be solved? How to reduce the change, there is no mature plan, no fixed principle, which undoubtedly increases the difficulty of transformation

[0010] Although it has been reported that K is a positively charged amino acid, which makes the peptide have a net positive charge, it can electrostatically attract the negatively charged lipopolysaccharide on the surface of the bacteria, so that the antimicrobial peptide is adsorbed on the surface of the bacteria; L is a hydrophobic Sexual residues make the peptide very hydrophobic, it can penetrate into the lipid bilayer to destroy the structure of the cell membrane, change the permeability of the cell, and then play a bactericidal effect (TeixeiraV, et al, 2012) However, should K replace In what position, is it better to replace as many as possible? There are also many uncertain factors.

[0011] In addition, although many people try to use D-type amino acids to improve the activity of polypeptides, there are still some problems: first, the cost of synthesis is too high; Subsequent experiments and future large-scale production and application will cause certain difficulties

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