Influence of chirality and sequence in lysine-rich lipopeptide biosurfactants and micellar model colloid systems.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
08 Aug 2024
08 Aug 2024
Historique:
received:
17
03
2024
accepted:
01
08
2024
medline:
9
8
2024
pubmed:
9
8
2024
entrez:
8
8
2024
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 39117639
doi: 10.1038/s41467-024-51234-8
pii: 10.1038/s41467-024-51234-8
doi:
Substances chimiques
Micelles
0
Lipopeptides
0
Surface-Active Agents
0
Colloids
0
Lysine
K3Z4F929H6
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
6785Subventions
Organisme : RCUK | Engineering and Physical Sciences Research Council (EPSRC)
ID : EP/V053396/1
Informations de copyright
© 2024. The Author(s).
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