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

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• 作者：Valeria Castelletto ; Steven Kirkham ; Ian W. Hamley ; Radoslaw Kowalczyk ; Martin Rabe ; Mehedi Reza ; Janne Ruokolainen
• 刊名：Biomacromolecules
• 出版年：2016
• 出版时间：February 8, 2016
• 年：2016
• 卷：17
• 期：2
• 页码：631-640
• 全文大小：734K
• ISSN：1526-4602

文摘

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.