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

Hamley, I. W. ORCID: https://orcid.org/0000-0002-4549-0926, Adak, A. and Castelletto, V. ORCID: https://orcid.org/0000-0002-3705-0162 (2024) Influence of chirality and sequence in lysine-rich lipopeptide biosurfactants and micellar model colloid systems. Nature Communications, 15. 6785. ISSN 2041-1723 doi: 10.1038/s41467-024-51234-8

Abstract/Summary

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 obtain the zeta potential from the SAXS structure factor which is in good agreement with directly measured values. Atomistic molecular dynamics simulations provide insights into molecular packing and conformation within the lipopeptide micelles which constitute model self-assembling colloidal systems and biomaterials.

Item Type	Article
URI	https://reading-clone.eprints-hosting.org/id/eprint/117649
Identification Number/DOI	10.1038/s41467-024-51234-8
Refereed	Yes
Divisions	Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
Publisher	Nature Publishing Group
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