Enzyme-assisted self-assembly under thermodynamic control

Williams, Richard and Smith, Andrew and Collins, Richard and Hodson, Nigel and Das, Apurba and Ulijn, Rein Vincent (2009) Enzyme-assisted self-assembly under thermodynamic control. Nature Nanotechnology, 4 (1). pp. 19-24. ISSN 1748-3387

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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 electronics. 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.

ORCID iDs

Williams, Richard, Smith, Andrew, Collins, Richard, Hodson, Nigel, Das, Apurba and Ulijn, Rein Vincent ORCID logoORCID: https://orcid.org/0000-0001-7974-3779;