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

Research output: Contribution to journalArticle

Researchers

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

Research units

  • University of Reading
  • Max-Planck-Institut für Eisenforschung

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.

Details

Original languageEnglish
Pages (from-to)631-640
Number of pages10
JournalBiomacromolecules
Volume17
Issue number2
Publication statusPublished - 8 Feb 2016
MoE publication typeA1 Journal article-refereed

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