Revealing pH-dependent antimicrobial peptide, GL13K, characteristics: A constant pH molecular dynamics study.

ABSTRACT: Antimicrobial peptides (AMPs) are a promising potential solution to combat antimicrobial resistance (AMR) due to their positive charges, which induce selective interaction with negatively charged bacterial membranes. Certain AMPs exhibit a low hemolytic index and non-forming fibrils at physiological pH (7.4), enhancing their therapeutic potential. In this study, we employ constant pH molecular dynamics (CpHMD) simulations to investigate the pH-dependent behavior of a 13-residue-long positively charged AMP, GL13K, focusing on the deprotonation states of lysine residues in a single GL13K AMP and their impact on its structural dynamics. We show that the last lysine located near the C-terminus (LYS11) has a significant deprotonation ratio difference with other lysine residues at the reported a

SUBMITTER: Hamidabad MN 

PROVIDER: S-EPMC12621878 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature