Abstract
In 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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Acknowledgements
The authors acknowledge support from Nokia Research Cambridge, the UK Engineering and Physical Sciences Research Council (EPSRC), the Interdisciplinary Research Council (IRC) in Nanotechnology, St John's College, Cambridge, and the Wellcome Trust. We thank C. Dobson, E. Eiser, M. Haddow and C. Meier for valuable discussions, and A. Rayment and I. Ganney for assistance with the mechanical measurements.
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T.P.J.K., T.W.O., A.K.B. and D.Y.C. performed the experiments. T.P.J.K., T.W.O., D.Y.C. and M.E.W. analysed the data. T.P.J.K., A.K.B. and M.E.W. co-wrote the paper. All authors discussed the results and commented on the manuscript.
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Knowles, T., Oppenheim, T., Buell, A. et al. Nanostructured films from hierarchical self-assembly of amyloidogenic proteins. Nature Nanotech 5, 204–207 (2010). https://doi.org/10.1038/nnano.2010.26
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DOI: https://doi.org/10.1038/nnano.2010.26
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