Self-Assembly and Antimicrobial Activity of Lipopeptides Containing Lysine-Rich Tripeptides.

ABSTRACT: The conformation and self-assembly of two pairs of model lipidated tripeptides in aqueous solution are probed using a combination of spectroscopic methods along with cryogenic-transmission electron microscopy (cryo-TEM) and small-angle X-ray scattering (SAXS). The palmitoylated lipopeptides comprise C₁₆-YKK or C₁₆-WKK (with two l-lysine residues) or their respective derivatives containing d-lysine (k), i.e., C₁₆-Ykk and C₁₆-Wkk. All four molecules self-assemble into spherical micelles which show structure factor effects in SAXS profiles due to intermicellar packing in aqueous solution. Consistent with micellar structures, the tripeptides in the coronas have a largely unordered conformation, as probed using spectroscopic methods. The molecules are

SUBMITTER: Adak A 

PROVIDER: S-EPMC10865344 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature