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Enzyme-assisted self-assembly under thermodynamic control
journal contributionposted on 01.01.2009, 00:00 authored by Richard WilliamsRichard Williams, A Smith, R Collins, N Hodson, A Das, R Ulijn
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.
Pagination19 - 24
PublisherNature Publishing Group
Publication classificationC1.1 Refereed article in a scholarly journal
Copyright notice2009, Macmillan Publishers Limited. All rights reserved.
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amino acidsfluorenesnanostructurespeptidessecondary protein structurethermodynamicsthermolysinScience & TechnologyTechnologyNanoscience & NanotechnologyMaterials Science, MultidisciplinaryScience & Technology - Other TopicsMaterials ScienceDYNAMIC COVALENT CHEMISTRYSUPRAMOLECULAR HYDROGELSIN-VITROHYDROLYSISNANOFIBERSGENERATIONNANOWIRESLIBRARY