Binding of Antimicrobial Peptide Indolicidin to DMPC Bilayer Using Replica-Exchange Molecular Dynamics.

ABSTRACT: Cationic antimicrobial peptides (AMPs) are toxic to microbes, such as bacteria and fungi, and have been increasingly studied as an alternative to traditional antibiotics, in part because AMPs are bactericidal with a minimum risk of developing bacterial resistance. Indolicidin (IL) is an AMP derived from bovine neutrophils that is unique due to its high prevalence of tryptophan and proline amino acids and its disordered structure. In addition to its antimicrobial activity, IL has exhibited toxicity toward mammalian cells, resulting in hemolysis. Although the precise physicochemical mechanism of IL cytotoxicity is unknown, its interactions with lipid bilayers are the primary focus of investigation. We conducted all-atom replica-exchange molecular dynamics simulations with solute tempering (R

SUBMITTER: Fitz AR 

PROVIDER: S-EPMC12421676 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature