Interaction of arginine-rich surfactant-like peptide nanotubes with liposomes

Castelletto, V. ORCID: https://orcid.org/0000-0002-3705-0162, Seitsonen, J., de Mello, L. R. and Hamley, I. W. ORCID: https://orcid.org/0000-0002-4549-0926 (2024) Interaction of arginine-rich surfactant-like peptide nanotubes with liposomes. Biomacromolecules. ISSN 1525-7797 doi: 10.1021/acs.biomac.4c01072

Abstract/Summary

The interaction of the surfactant-like peptide (SLP) R3L12 bearing three cationic arginine residues with model liposomes is investigated in aqueous solution at various pH values, under conditions for which the SLP self-assembles into nanotubes. The structure of liposomes of model anionic lipid DPPG [1,2-dipalmitoyl-sn-glycero-3-phospho-rac-(1-glycerol)], or zwitterionic lipid DPPE [1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine] is probed using small-angle X-ray scattering and cryogenic-transmission electron microscopy. The unilamellar vesicles of DPPG are significantly restructured in the presence of R3L12, especially at low pH, and multilamellar vesicles of DPPE are also restructured under these conditions. The SLP promotes the release of cargo encapsulated in the vesicles as probed by calcein fluorescence, with notably higher release for anionic DPPG vesicles. Laurdan fluorescence experiments to probe membrane fluidity (lipid chain ordering) show that R3L12 destabilizes the lipid gel phase, especially for anionic DPPG. This model nanotube-forming SLP has promise as a pH-sensitive release system for vesicle-encapsulated cargo.

Item Type	Article
URI	https://reading-clone.eprints-hosting.org/id/eprint/119196
Identification Number/DOI	10.1021/acs.biomac.4c01072
Refereed	Yes
Divisions	Interdisciplinary centres and themes > Chemical Analysis Facility (CAF) Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
Publisher	American Chemical Society
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