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2010-06-26 19:09 |
Nature Nanotechnology 5, 204 - 207 (2010)
Published online: 28 February 2010 | doi:10.1038/nnano.2010.26
Subject Category: Nanomaterials
Nanostructured films from hierarchical self-assembly of amyloidogenic proteins
Tuomas P. J. Knowles1, Tomas W. Oppenheim1, Alexander K. Buell1, Dimitri Y. Chirgadze2 & Mark E. Welland1
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AbstractIn nature, sophisticated functional materials are created through hierarchical self-assembly of simple nanoscale motifs1, 2, 3, 4. In the laboratory, much progress has been made in the controlled assembly of molecules into one-5, 6, 7, two-6, 8, 9 and three-dimensional10 artificial nanostructures, but bridging from the nanoscale to the macroscale to create useful macroscopic materials remains a challenge. Here we show a scalable self-assembly approach to making free-standing films from amyloid protein fibrils. The films were well ordered and highly rigid, with a Young's modulus of up to 5–7 GPa, which is comparable to the highest values for proteinaceous materials found in nature. We show that the self-organizing protein scaffolds can align otherwise unstructured components (such as fluorophores) within the macroscopic films. Multiscale self-assembly that relies on highly specific biomolecular interactions is an attractive path for realizing new multifunctional materials built from the bottom up.
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1.Nanoscience Centre, J J Thomson Avenue, University of Cambridge, Cambridge CB3 0FF, UK
2.Department of Biochemistry, Tennis Court Road, University of Cambridge, Cambridge CB2 1GA, UK
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