Issue 3, 2013

New cylindrical peptide assemblies defined by extended parallel β-sheets

Abstract

A new approach to non-covalent peptide-based nanotubular or rod-like structures is presented, whereby the monomeric units are preorganised into a β-strand geometry that templates the formation of an extended and unusual parallel β-sheet rod-like structure. The conformational constraint is introduced by Huisgen cycloaddition to give a triazole-based macrocycle, with the resulting self-assembled structures stabilized by a well-defined series of intermolecular hydrogen bonds.

Graphical abstract: New cylindrical peptide assemblies defined by extended parallel β-sheets

Supplementary files

Article information

Article type
Paper
Submitted
17 Aug 2012
Accepted
25 Sep 2012
First published
26 Sep 2012

Org. Biomol. Chem., 2013,11, 425-429

New cylindrical peptide assemblies defined by extended parallel β-sheets

A. D. Pehere, C. J. Sumby and A. D. Abell, Org. Biomol. Chem., 2013, 11, 425 DOI: 10.1039/C2OB26637G

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