Modeling the interaction of dodecylphosphocholine micelles with the anticoccidial peptide PW2 guided by NMR data.

ABSTRACT: Antimicrobial peptides are highly dynamic entities that acquire structure upon binding to a membrane interface. To better understand the structure and the mechanism for the molecular recognition of dodecylphosphocholine (DPC) micelles by the anticoccidial peptide PW2, we performed molecular dynamics (MD) simulations guided by NMR experimental data, focusing on strategies to explore the transient nature of micelles, which rearrange on a millisecond to second timescale. We simulated the association of PW2 with a pre-built DPC micelle and with free-DPC molecules that spontaneously forms micelles in the presence of the peptide along the simulation. The simulation with spontaneous micelle formation provided the adequate environment which replicated the experimental data. The unrestrained MD sim

SUBMITTER: Gomes-Neto F 

PROVIDER: S-EPMC6270265 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature