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

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.

  1. School of Materials, The University of Manchester, Oxford Road, Manchester M13 9PL, UK
  2. Manchester Interdisciplinary Biocentre, The University of Manchester, Oxford Road, Manchester M13 9PL, UK
  3. Faculty of Life Sciences, The University of Manchester, Manchester M13 9PT, UK
  4. 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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