Simulations reveal that antimicrobial BP100 induces local membrane thinning, slows lipid dynamics and favors water penetration.

ABSTRACT: BP100, a short antimicrobial peptide, produces membrane perturbations that depend on lipid structure and charge, salts presence, and peptide/lipid molar ratios. As membrane perturbation mechanisms are not fully understood, the atomic scale nature of peptide/membrane interactions requires a close-up view analysis. Molecular Dynamics (MD) simulations are valuable tools for describing molecular interactions at the atomic level. Here, we use MD simulations to investigate alterations in membrane properties consequent to BP100 binding to zwitterionic and anionic model membranes. We focused on membrane property changes upon peptide binding, namely membrane thickness, order parameters, surface curvature, lipid lateral diffusion and membrane hydration. In agreement with experimental results, our si

SUBMITTER: Franco LR 

PROVIDER: S-EPMC8981376 | biostudies-literature | 2022 Feb

REPOSITORIES: biostudies-literature