Authors: M. Garvey, S.L. Gras, S. Meehan, S.J. Meade, J.A. Carver, J.A. Gerrard
Addresses: School of Chemistry & Physics, The University of Adelaide, Adelaide, South Australia 5005, Australia; School of Biological Sciences, University of Canterbury, Christchurch, New Zealand. ' Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, 30 Flemington Road, Victoria 3010, Australia. ' Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, UK. ' Crop and Food Research, Private Bag 4704, Christchurch, New Zealand. ' School of Chemistry & Physics, The University of Adelaide, Adelaide, South Australia 5005, Australia. ' School of Biological Sciences, University of Canterbury, Christchurch, New Zealand
Abstract: Self assembling protein nanofibres have great potential within the nanotechnology industry. To realise this potential, nanofibres need to be manufactured on a commercial scale. To date, amyloid fibrils, a form of protein nanofibre with desirable bionanotechnological properties, have only been produced using expensive and time-costly, small-scale methods. This paper describes the production of protein nanofibres from semi-pure and crude mixtures of bovine crystallin proteins, currently a waste product in the meat industry. These nanofibres displayed amyloid fibril characteristics. Moreover, distinct fibre morphologies were observed dependent upon the formation conditions adopted. This research shows that amyloid fibrils can be inexpensively produced from crude crystallin protein mixtures, making them a potential industrial source for protein nanofibres.
Keywords: amyloid fibrils; protein nanofibres; bovine crystallins; WAXS; TEM; self assembly; nanotechnology; fibre morphologies.
International Journal of Nanotechnology, 2009 Vol.6 No.3/4, pp.258 - 273
Published online: 03 Feb 2009 *Full-text access for editors Access for subscribers Purchase this article Comment on this article