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

Anindyasundar Adak, Valeria Castelletto, Ana de Sousa, Kimon Andreas Karatzas, Callum Wilkinson, Nikul Khunti, Jani Seitsonen, Ian W. Hamley*

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

1 Citation (Scopus)
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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 found to have good cytocompatibility with fibroblasts at sufficiently low concentrations, although some loss of cell viability is noted at the highest concentrations examined (above the critical aggregation concentration of the lipopeptides, determined from fluorescence dye probe measurements). Preliminary tests also showed antimicrobial activity against both Gram-negative and Gram-positive bacteria.

Original languageEnglish
Pages (from-to)1205-1213
Number of pages9
JournalBiomacromolecules
Volume25
Issue number2
DOIs
Publication statusPublished - 12 Feb 2024
MoE publication typeA1 Journal article-refereed

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