Self-assembly of the toll-like receptor agonist macrophage-activating lipopeptide MALP-2 and of its constituent peptide

Castelletto, V., Kirkham, S., Hamley, I. W. ORCID: https://orcid.org/0000-0002-4549-0926, Kowalczyk, R. ORCID: https://orcid.org/0000-0002-3926-6530, Rabe, M., Reza, M. and Ruokolainen, J. (2016) Self-assembly of the toll-like receptor agonist macrophage-activating lipopeptide MALP-2 and of its constituent peptide. Biomacromolecules, 17 (2). pp. 631-640. ISSN 1525-7797 doi: 10.1021/acs.biomac.5b01573

Abstract/Summary

The self-assembly of the macrophage-activating lipopeptide MALP-2 in aqueous solution has been investigated and is compared to that of the constituent peptide GNNDESNISFKEK. MALP-2 is a toll-like receptor agonist lipopeptide with diverse potential biomedical applications and its self-assembly has not previously been examined. It is found to self-assemble, above a critical aggregation concentration (cac), into remarkable “fibre raft” structures, based on lateral aggregation of β-sheet based bilayer tapes. Peptide GNNDESNISFKEK also forms β-sheet structures above a cac, although the morphology is distinct, comprising highly extended and twisted tape structures. A detailed insight into the molecular packing within the MALP-2 raft and GNNDESNISFKEK nanotape structures is obtained through X-ray diffraction and small-angle X-ray scattering. These results point to the significant influence of the attached lipid chains on the self-assembly motif, which lead to the raft structure for the lipopeptide assemblies.

Item Type	Article
URI	https://reading-clone.eprints-hosting.org/id/eprint/66313
Identification Number/DOI	10.1021/acs.biomac.5b01573
Refereed	Yes
Divisions	Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
Publisher	American Chemical Society
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