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.
It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing. To link to this item DOI: 10.1021/acs.biomac.5b01573 Abstract/SummaryThe 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.
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