Influence of chirality and sequence in lysine-rich lipopeptide biosurfactants and micellar model colloid systems.

ABSTRACT: Lipopeptides can self-assemble into diverse nanostructures which can be programmed to incorporate peptide sequences to achieve a remarkable range of bioactivities. Here, the influence of peptide sequence and chirality on micelle structure and interactions is investigated in a series of lipopeptides bearing two lysine or D-lysine residues and tyrosine or tryptophan residues, attached to a hexadecyl lipid chain. All molecules self-assemble into micelles above a critical micelle concentration (CMC). Small-angle x-ray scattering (SAXS) is used to probe micelle shape and structure from the form factor and to probe inter-micellar interactions via analysis of structure factor. The CMC is obtained consistently from surface tension and electrical conductivity measurements. We introduce a method to

SUBMITTER: Hamley IW 

PROVIDER: S-EPMC11310517 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature