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Issue 5, 2013
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Hierarchical self-assembly of a β-amyloid peptide derivative

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Neurodegenerative diseases including Alzheimer's, Parkinson's, and type II diabetes are recognized to be related to proteins misfolding into amyloid fibrils and other aggregates with a β-sheet conformation. Herein, self-assembled peptide micro/nanoarchitectures were designed and prepared to mimic those aggregates. A short β-amyloid peptide derivative with a diphenylalanine moiety was synthesized, which could self-assemble into nanofibers via β-sheet conformation in an aqueous solution with a concentration of 1 mg mL−1 at pH about 8. By adjusting the pH to around 6.5, a peptide solution with a concentration of 15 mg mL−1 could change to a supramolecular hydrogel. The influence of self-assembly conditions including peptide concentration, temperature, pressure, and self-assembly time were investigated in detail. It was found that the self-assembled nanofibers could further aggregate into catenulate microfibers in solution as well as layer-by-layer plaques in the hydrogel under particular conditions.

Graphical abstract: Hierarchical self-assembly of a β-amyloid peptide derivative

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The article was received on 12 Sep 2012, accepted on 15 Nov 2012 and first published on 16 Nov 2012

Article type: Paper
DOI: 10.1039/C2TB00105E
Citation: J. Mater. Chem. B, 2013,1, 668-675

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    Hierarchical self-assembly of a β-amyloid peptide derivative

    S. Qin, Y. Pei, X. Liu, R. Zhuo and X. Zhang, J. Mater. Chem. B, 2013, 1, 668
    DOI: 10.1039/C2TB00105E

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