Jump to main content
Jump to site search

Issue 5, 2013
Previous Article Next Article

Hierarchical self-assembly of a β-amyloid peptide derivative

Author affiliations

Abstract

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

Back to tab navigation

Supplementary files

Publication details

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

  •   Request permissions

    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

Search articles by author

Spotlight

Advertisements