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*

*Tämän työn vastaava kirjoittaja

Tutkimustuotos: LehtiartikkeliArticleScientificvertaisarvioitu

1 Sitaatiot (Scopus)
14 Lataukset (Pure)

Abstrakti

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.

AlkuperäiskieliEnglanti
Sivut1205-1213
Sivumäärä9
JulkaisuBiomacromolecules
Vuosikerta25
Numero2
DOI - pysyväislinkit
TilaJulkaistu - 12 helmik. 2024
OKM-julkaisutyyppiA1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä

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