Enzyme-assisted self-assembly under thermodynamic control

Williams, Richard J., Smith, Andrew M., Collins, Richard, Hodson, Nigel, Das, Apurba K. and Ulijn, Rein V. 2009, Enzyme-assisted self-assembly under thermodynamic control, Nature nanotechnology, vol. 4, no. 1, pp. 19-24.

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Title Enzyme-assisted self-assembly under thermodynamic control
Author(s) Williams, Richard J.
Smith, Andrew M.
Collins, Richard
Hodson, Nigel
Das, Apurba K.
Ulijn, Rein V.
Journal name Nature nanotechnology
Volume number 4
Issue number 1
Start page 19
End page 24
Total pages 6
Publisher Nature Publishing Group
Place of publication London, England
Publication date 2009-01
ISSN 1748-3387
1748-3395
Keyword(s) amino acids
fluorenes
nanostructures
peptides
secondary protein structure
thermodynamics
thermolysin
Summary 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.
Language eng
Field of Research 069999 Biological Sciences not elsewhere classified
Socio Economic Objective 970106 Expanding Knowledge in the Biological Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2009, Macmillan Publishers Limited. All rights reserved.
Persistent URL http://hdl.handle.net/10536/DRO/DU:30047889

Document type: Journal Article
Collection: School of Life and Environmental Sciences
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