Research progress in anti-enzymatic antimicrobial peptides.

Author: Changxuan SHAO ¹ ; Mengcheng WANG ¹ ; Yuanmengxue WANG ¹ ; Shiqi HE ¹ ; Yongjie ZHU ¹ ; Anshan SHAN ¹
Author Information

1. College of Animal Science and Technology, Northeast Agricultural University, Harbin 150030, Heilongjiang, China.
Publication Type:English Abstract
Keywords: antimicrobial peptide; arrangement of residues; chemical modification; cyclization; nanotechnology; protease stability; unnatural amino acids
MeSH: Antimicrobial Peptides/pharmacology*; Humans; Peptide Hydrolases/metabolism*; Protein Stability; Antimicrobial Cationic Peptides/chemistry*; Anti-Infective Agents/chemistry*
From: Chinese Journal of Biotechnology 2024;40(12):4396-4407
CountryChina
Language:Chinese
Abstract: Antimicrobial peptides (AMPs) are small molecular peptides widely existing in the innate immunity of organisms, serving as the first line of defense. Natural AMPs possess various biological activities and are difficult to develop drug resistance. However, they are easily broken down by digestive enzymes in the body. In recent years, increasing methods have been reported to enhance the stability of AMPs, including incorporation of unnatural amino acids, chemical modifications, strategic avoidance of enzyme cleavage sites, cyclization, and nano peptide design. This review summarizes the methods for improving the stability of AMPs against protease degradation, aiming to provide references for further research in this field.