Self-Assembly and Antimicrobial Activity of Lipopeptides Containing Lysine-Rich Tripeptides
Tripeptide
Small-angle X-ray scattering
DOI:
10.1021/acs.biomac.3c01184
Publication Date:
2024-01-11T08:34:23Z
AUTHORS (8)
ABSTRACT
The conformation and self-assembly of two pairs model lipidated tripeptides in aqueous solution are probed using a combination spectroscopic methods along with cryogenic-transmission electron microscopy (cryo-TEM) small-angle X-ray scattering (SAXS). palmitoylated lipopeptides comprise C16-YKK or C16-WKK (with l-lysine residues) their respective derivatives containing d-lysine (k), i.e., C16-Ykk C16-Wkk. All four molecules self-assemble into spherical micelles which show structure factor effects SAXS profiles due to intermicellar packing solution. Consistent micellar structures, the coronas have largely unordered conformation, as methods. found good cytocompatibility fibroblasts at sufficiently low concentrations, although some loss cell viability is noted highest concentrations examined (above critical aggregation concentration lipopeptides, determined from fluorescence dye probe measurements). Preliminary tests also showed antimicrobial activity against both Gram-negative Gram-positive bacteria.
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