期刊
NATURE NANOTECHNOLOGY
卷 4, 期 1, 页码 19-24出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/NNANO.2008.378
关键词
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资金
- Engineering and Physical Sciences Research Council
- Leverhulme Trust
- Engineering and Physical Sciences Research Council [EP/D07410X/1] Funding Source: researchfish
- EPSRC [EP/D07410X/1] Funding Source: UKRI
The production of functional molecular architectures through self-assembly is commonplace in biology, but despite advances(1-3), 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 culture(4,5), templating(6), biosensing(7) and supramolecular electronics(8). Here, we report the use of reversible enzyme-catalysed reactions to drive self-assembly. In this approach, the self-assembly of aromatic short peptide derivatives(9,10) 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-correctionfully reversible self-assembly under thermodynamic control; (ii) component-selection-the ability to amplify the most stable molecular self-assembly structures in dynamic combinatorial libraries(11-13); 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.
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