Self-Assembly of the Toll-Like Receptor Agonist Macrophage-Activating 
Lipopeptide MALP-2 and of Its Constituent Peptide

Castelletto, Valeria; Kirkham, Steven; Hamley, Ian W.; Kowalczyk, Radosław M.; Rabe, Martin; Reza, Mehedi; Ruokolainen, Janne T.

doi:10.1021/acs.biomac.5b01573

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Self-Assembly of the Toll-Like Receptor Agonist Macrophage-Activating Lipopeptide MALP-2 and of Its Constituent Peptide

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Rabe, Martin
Interface Spectroscopy, Interface Chemistry and Surface Engineering, Max-Planck-Institut für Eisenforschung GmbH, Max Planck Society;

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Citation

Castelletto, V., Kirkham, S., Hamley, I. W., Kowalczyk, R. M., Rabe, M., Reza, M., et al. (2016). Self-Assembly of the Toll-Like Receptor Agonist Macrophage-Activating Lipopeptide MALP-2 and of Its Constituent Peptide. Biomacromolecules, 17(2), 631-640. doi:10.1021/acs.biomac.5b01573.

Cite as: https://hdl.handle.net/21.11116/0000-0001-B72E-E

Abstract

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. © 2016 American Chemical Society.