Micellization of Lipopeptides Containing Toll-like Receptor Agonist and Integrin Binding Sequences.

ABSTRACT: Short bioactive peptide sequences are of great interest in biomaterials development. We investigate the self-assembly of a lipopeptide containing both the highly cationic CSK₄ toll-like receptor agonist hexapeptide sequence and RGDS integrin-binding motif, i.e., C₁₆-CSK₄RGDS, as well as the control containing a scrambled terminal sequence C₁₆-CSK₄GRDS. Both lipopeptides are found to form micelles, as revealed by small-angle X-ray scattering and cryogenic transmission electron microscopy, and modeled using atomistic molecular dynamics simulations. We carefully examined methods to probe the aggregation of the molecules, i.e. to obtain the critical micelle concentration (CMC). Fluorescent probe assays using 1-anilino-8-naphthalenesulfonat

SUBMITTER: Castelletto V 

PROVIDER: S-EPMC11660038 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature