Derived polypeptides formed by modifying structures of frog skin antibacterial peptides AR-23 and application of derived polypeptides

Abstract

The invention discloses a group of derived polypeptides formed by modifying the structures of frog skin antibacterial peptides AR-23 and an application of the derived polypeptides. The group of derived polypeptides are named as A1-A7, and have amino acid sequences, i.e., respectively SEQ ID No.1, SEQ ID No.2, SEQ ID No.3, SEQ ID No.4, SEQ ID No.5, SEQ ID No.6 and SEQ ID No.7. The experiment proves that compared with natural antibacterial peptides, according to the derived polypeptides formed by modifying the structures of frog skin antibacterial peptides AR-23, the selective toxicity of the derived polypeptides to bacteria is high while the toxicity of the derived polypeptides to human cells is obviously decreased, so that the influences of the derived polypeptides to somatic cells, red blood cells and the like are very low. The polypeptides A1-A7 have broad-spectrum killing effects on gram-positive bacteria or gram-negative bacteria, so that the polypeptides A1-A7 can be used for treating diseases caused by the infections of the gram-positive bacteria or the gram-negative bacteria resistant to antibiotics.

Description

technical field [0001] The invention relates to a modified derivative polypeptide of the frog skin antibacterial peptide AR-23 and its application in the field of biotechnology. Background technique [0002] Bacterial resistance to antibiotics has become a major problem threatening human health. Antibacterial peptide (Antibacterial Peptide) is a defensive peptide active substance produced by organisms against the invasion and pathogenicity of exogenous pathogens. It is an important part of the body's immune defense system. Antimicrobial peptides: an overview of a promising class of therapeutics. Central European Journal of Biology, 2007, 2(1): 1-33). [0003] Natural antimicrobial peptides are generally composed of 10-50 amino acids. The C-terminal is rich in hydrophilic amino acids, while the N-terminal contains more hydrophobic residues and has an amphipathic structure. Studies have shown that antimicrobial peptides can form holes on the surface of bacteria through modes...

AI Technical Summary

Problems solved by technology

The non-selective cytotoxicity of Melittin can induce serious side effects, which seriously affects its application prospect as an antibacterial drug

Studies have shown that among the 1-20 amino acids of melittin, amino acids such as Leu-6, Lys-7, Val-8, Leu-9, Leu-13, Leu-16, Ile-17, Trp-19 and Ile-20 are antibacterial Hemolytic and hemolytic effects are very important, and deletion of any amino acid will lead to a sharp decline in hemolytic activity and weaken the antibacterial activity (Blondelle SE, Houghten RA. Hemolytic and antimicrobial activities of the twenty-four individual omission analogues of melittin. Biochemistry. 1991May14 ;30(19):4671-8)

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