Issue 27, 2013
From the journal:

Chemical Communications

Protein β-interfaces as a generic source of native peptide tectons†

Céline Valéry,*a   Rishi Pandeya  and  Juliet A. Gerrard*abcd  

* Corresponding authors

a Biomolecular Interaction Centre, University of Canterbury, Private Bag 4800, Christchurch 8140, New Zealand
E-mail: celine.valery@canterbury.ac.nz, juliet.gerrard@canterbury.ac.nz
Tel: +64 33642987

b Riddet Institute, Massey University, Palmerston North, New Zealand

c MacDiarmid Institute, University of Canterbury, New Zealand

d Callaghan Innovation Research Limited, P.O. Box 31310, Lower Hutt 5040, New Zealand

Abstract

Motifs of 7–8 amino acids were designed from the β-continuous interfaces of non-related homo-oligomeric proteins. These peptides intrinsically self-assembled into nanoarchitectures in water, while retaining some properties of their parent interfaces, especially reversibility of assembly. These results reveal a novel source of native peptide tectons.

Graphical abstract: Protein β-interfaces as a generic source of native peptide tectons

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Article information

DOI
https://doi.org/10.1039/C3CC39052G
Article type
Communication
Submitted
18 Dec 2012
Accepted
18 Feb 2013
First published
27 Feb 2013
This article is Open Access
Creative Commons BY license

Chem. Commun., 2013,49, 2825-2827

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Protein β-interfaces as a generic source of native peptide tectons

C. Valéry, R. Pandey and J. A. Gerrard, Chem. Commun., 2013, 49, 2825 DOI: 10.1039/C3CC39052G

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