Letter abstract
Nature Nanotechnology 4, 19 - 24 (2009)
Published online: 21 December 2008 | doi:10.1038/nnano.2008.378
Subject Categories: Molecular self-assembly | Surface patterning and imaging
Enzyme-assisted self-assembly under thermodynamic control
Richard J. Williams1,2, Andrew M. Smith1,2, Richard Collins2, Nigel Hodson3, Apurba K. Das1,2,4 & Rein V. Ulijn1,2,4
Abstract
The production of functional molecular architectures through self-assembly is commonplace in biology, but despite advances1, 2, 3, it is still a major challenge to achieve similar complexity in the laboratory. Self-assembled structures that are reproducible and virtually defect free are of interest for applications in three-dimensional cell culture4, 5, templating6, biosensing7 and supramolecular electronics8. Here, we report the use of reversible enzyme-catalysed reactions to drive self-assembly. In this approach, the self-assembly of aromatic short peptide derivatives9, 10 provides a driving force that enables a protease enzyme to produce building blocks in a reversible and spatially confined manner. We demonstrate that this system combines three features: (i) self-correction—fully reversible self-assembly under thermodynamic control; (ii) component-selection—the ability to amplify the most stable molecular self-assembly structures in dynamic combinatorial libraries11, 12, 13; and (iii) spatiotemporal confinement of nucleation and structure growth. Enzyme-assisted self-assembly therefore provides control in bottom-up fabrication of nanomaterials that could ultimately lead to functional nanostructures with enhanced complexities and fewer defects.
- School of Materials, The University of Manchester, Oxford Road, Manchester M13 9PL, UK
- Manchester Interdisciplinary Biocentre, The University of Manchester, Oxford Road, Manchester M13 9PL, UK
- Faculty of Life Sciences, The University of Manchester, Manchester M13 9PT, UK
- Present address: Department of Pure and Applied Chemistry/WestCHEM, The University of Strathclyde, Glasgow G1 1XL, UK
Correspondence to: Rein V. Ulijn1,2,4 e-mail: Rein.Ulijn@strath.ac.uk
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