Structural and Dynamic Insights of the Interaction between Tritrpticin and Micelles: An NMR Study.

ABSTRACT: A large number of antimicrobial peptides (AMPs) acts with high selectivity and specificity through interactions with membrane lipid components. These peptides undergo complex conformational changes in solution; upon binding to an interface, one major conformation is stabilized. Here we describe a study of the interaction between tritrpticin (TRP3), a cathelicidin AMP, and micelles of different chemical composition. The peptide's structure and dynamics were examined using one-dimensional and two-dimensional NMR. Our data showed that the interaction occurred by conformational selection and the peptide acquired similar structures in all systems studied, despite differences in detergent headgroup charge or dipole orientation. Fluorescence and paramagnetic relaxation enhancement experiments sho

SUBMITTER: Santos TL 

PROVIDER: S-EPMC5194225 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature