Optimization of Antibacterial Activity in Tibetan Swine α-Helix Peptide TP by Site-Directed Mutagenesis.

ABSTRACT: Antimicrobial peptides (AMPs) have attracted extensive attention because of their broad-spectrum antibacterial activity and low level of induced bacterial resistance. However, the development of some natural AMPs does not consider the perfect balance of structural characteristics, resulting in some empirical and controversial practices still existing. To further explore and complete the relationship between parameters and function of α-helix peptide, in this study, the natural antimicrobial peptide TP secreted from Bacillus strain of Tibetan pigs was selected as a template to investigate the effect of systematic mutations in the hydrogen bond formation site of the α-helical antimicrobial peptide on the activity and cell selectivity of the antimicrobial peptide. The target peptide TP(i+4) 1

SUBMITTER: Li G 

PROVIDER: S-EPMC9289672 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature