α-Helical Structure of Antimicrobial Peptides Enhances Their Activity through Molecular Surface Signatures.

ABSTRACT: The increase in antibacterial resistance is one of the greatest challenges in modern medicine, driving an urgent need to develop new drugs to combat resistant pathogens. Peptides represent a promising class of molecules that can be efficiently designed to exhibit high antimicrobial efficacy. Recently, we have highlighted how prestructuring by a triazolyl-bridge significantly enhances the activity of an antimicrobial peptide. To learn more from these findings, the aim of this study is to relate the NMR-based structure of a triazolyl-bridged peptide to its antimicrobial activity against Gram-positive and Gram-negative bacteria in comparison to its linear analogues. As we show, the triazole modification indeed induces a well-defined α-helical structure, resulting in an improved positive elect

SUBMITTER: Quagliata M 

PROVIDER: S-EPMC12329715 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature