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

Amyloid Fibrils: From Disease to Design. New Biomaterial Applications for Self-Assembling Cross-β... 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Australian Journal of Chemistry CSIRO Publishing

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

Australian Journal of Chemistry , Volume 60 (5) – May 28, 2007

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References (144)

Publisher
CSIRO Publishing
Copyright
CSIRO
ISSN
0004-9425
eISSN
1445-0038
DOI
10.1071/CH06485
Publisher site
See Article on Publisher Site

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.

Journal

Australian Journal of ChemistryCSIRO Publishing

Published: May 28, 2007

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