Antimicrobial peptide with drug-resistance bacteria resistance activity and synthesis and application thereof

Abstract

The invention designs antimicrobial peptide with drug-resistance bacteria resistance activity and a novel structure. The antimicrobial peptide is obtained by modifying amino acid at N tail ends of natural antimicrobial peptide Anoplin and MPI respectively, then performing acetylization on the amino acid, and performing intermolecular connection on every two side chains of the peptide by replacing a -1H-1,2,3-triazole structure by one 1,4- under the 1,3-dipolar cycloaddition reaction of the click chemistry. The antimicrobial experiments and pyridinium iodide dyeing method experiments for staphylococcus aureus and escherichia coli of the conventional gram-positive bacterium and clinically separated drug-resistant staphylococcus aureus and drug-resistant escherichia coli show that the J-AM peptide and the J-AA peptide which are synthesized by the method are higher in antimicrobial activity, higher in drug-resistance bacteria resistance activity and higher in cytomembrane film penetration capacity and has an obvious drug-resistance advantage of avoiding a drug-resistance phenomenon caused by the general antibiotics; and therefore, the antimicrobial peptide has an extremely high application prospect in preparation of clinical treatment medicines.

Description

technical field [0001] The invention belongs to the technical field of biochemistry, and relates to a novel structure antibacterial peptide with anti-drug-resistant bacteria activity; the invention also relates to a synthesis method of the antibacterial peptide and an application in preparing antibacterial drugs. Background technique [0002] With the extensive use of antibiotics in people's lives, drug-resistant strains continue to emerge, making many highly effective antibiotics ineffective, so seeking new antibiotics is becoming more and more important to human development. Antimicrobial Peptides (AMPs) refer to a class of small molecule polypeptides that are often positively charged, have broad-spectrum antibacterial properties, and have 12 to 50 amino acids. With the rapid development of molecular biology, the study of antimicrobial peptides has increasingly become a hot topic in the field of biomedicine (Hancock RE. Peptide antibiotics[J]. Lancet, 1997,349(9049):418-42...

AI Technical Summary

Problems solved by technology

However, not all natural antimicrobial peptides have disadvantages, some natural antimicrobial peptides are not very active, and the antibacterial spectrum is relatively narrow, etc.

In addition, the mechanism of action of antimicrobial peptides is different from traditional antibiotics, and generally does not produce drug resistance, but there are always certain pathogenic microorganisms in nature, which are naturally resistant to drugs due to their very stable cell membrane structure or functional characteristics sex

Images