Computational exploration of the self-aggregation mechanisms of phenol-soluble modulins β1 and β2 in Staphylococcus aureus biofilms.

ABSTRACT: The formation of functional bacterial amyloids by phenol-soluble modulins (PSMs) in Staphylococcus aureus is a critical component of biofilm-associated infections, providing robust protective barriers against antimicrobial agents and immune defenses. Clarifying the molecular mechanisms of PSM self-assembly within the biofilm matrix is essential for developing strategies to disrupt biofilm integrity and combat biofilm-related infections. In this study, we analyzed the self-assembly dynamics of PSM-β1 and PSM-β2 by examining their folding and dimerization through long-timescale atomistic discrete molecular dynamics simulations. Our findings revealed that both peptides primarily adopt helical structures as monomers but shift to β-sheets upon dimerization. Monomeric state, PSM-β1 exhibited fre

SUBMITTER: Xu H 

PROVIDER: S-EPMC12450408 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature