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RESEARCH FRONT
Contents Vol 60(5)

Amyloid Fibrils: From Disease to Design. New Biomaterial Applications for Self-Assembling Cross-β Fibrils

Sally L. Gras A
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A Department of Chemical and Biomolecular Engineering and the Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, VIC 3010, Australia. Email: sgras@unimelb.edu.au




Dr Sally Gras is a lecturer in the Department of Chemical and Biomolecular Engineering, and research group leader at the Bio21 Molecular Science and Biotechnology Institute at the University of Melbourne, Australia. She received her Ph.D. from Cambridge University and her B.Sc. and B.Eng. degrees from the University of Melbourne. Her research interests include amyloid fibrils, the design and development of novel materials, and cell–material interactions.

Australian Journal of Chemistry 60(5) 333-342 https://doi.org/10.1071/CH06485
Submitted: 21 December 2006  Accepted: 21 March 2007   Published: 28 May 2007

Abstract

Amyloid fibrils are self-assembling protein aggregates. They are essentially insoluble and resilient nanofibres that offer great potential as materials for nanotechnology and bionanotechnology. Fibrils are associated with several debilitating diseases, for example Alzheimer’s disease, but recent advances suggest they also have positive functions in nature and can be formed in vitro from generic proteins. This article explores how the unique nanotopography and advantageous properties of fibrils may be used to develop tools for probing cell behaviour, protein-based biomimetic materials for supporting cells, or platforms for biosensors and enzyme immobilization.


Acknowledgments

Thank you to Dr C. E. MacPhee from the University of Edinburgh, and Professor C. M. Dobson and Dr M. H. Krebs, both from Cambridge University, for useful discussions.


References


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