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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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A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä

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Castelletto, Valeria
Kirkham, Steven
Hamley, Ian W.
Kowalczyk, Radoslaw
Rabe, Martin
Reza, Mehedi
Ruokolainen, Janne

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en

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10

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Biomacromolecules, Volume 17, issue 2, pp. 631-640

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.

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Castelletto, V, Kirkham, S, Hamley, I W, Kowalczyk, R, Rabe, M, Reza, M & Ruokolainen, J 2016, 'Self-Assembly of the Toll-Like Receptor Agonist Macrophage-Activating Lipopeptide MALP-2 and of Its Constituent Peptide', Biomacromolecules, vol. 17, no. 2, pp. 631-640. https://doi.org/10.1021/acs.biomac.5b01573

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