title: Bacteriocin AS-48 binding to model membranes and pore formation as revealed by coarse-grained simulations.
abstract: Bacteriocin AS-48 is a membrane-interacting peptide that acts as a broad-spectrum antimicrobial against Gram-positive and Gram-negative bacteria. Prior Nuclear Magnetic Resonance experiments and the high resolution crystal structure of AS-48 have suggested a mechanism for the molecular activity of AS-48 whereby the peptide undergoes transition from a water-soluble to a membrane-bound state upon membrane binding. To help interpret experimental results, we here simulate the molecular dynamics of this binding mechanism at the coarse-grained level. By simulating the self-assembly of the peptide, we predict induction by the bacteriocin of different pore types consistent with a "leaky slit" model.
authors.affiliation: BIOPHYM, Instituto de Estructura de la Materia CSIC, Serrano-113-bis., 28006 Madrid, Spain. Electronic address: victor.cruz@iem.cfmac.csic.es.
authors.forename: Victor L
authors.initials: VL
authors.lastname: Cruz
authors.forename: Javier
authors.initials: J
authors.lastname: Ramos
authors.forename: Manuel N
authors.initials: MN
authors.lastname: Melo
authors.forename: Javier
authors.initials: J
authors.lastname: Martinez-Salazar
mesh_terms: D001430:Bacteriocins / Q000737:chemistry / Q000378:metabolism*; D019281:Dimerization; D008051:Lipid Bilayers; D008567:Membranes, Artificial; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D014961:X-Ray Diffraction
chemical_list: D001430:Bacteriocins; D008051:Lipid Bilayers; D008567:Membranes, Artificial; C440289:bacteriocin AS-48, Enterococcus faecalis
keywords: AS-48 bacteriocin; Antimicrobial peptide; Coarse-grained simulation