Protein nanofibres of defined morphology prepared from mixtures of crude crystallins

被引:17
作者
Garvey, M. [1 ,2 ]
Gras, S. L. [3 ]
Meehan, S. [4 ]
Meade, S. J. [5 ]
Carver, J. A. [2 ]
Gerrard, J. A. [1 ]
机构
[1] Univ Canterbury, Sch Biol Sci, Christchurch 1, New Zealand
[2] Univ Adelaide, Sch Chem & Phys, Adelaide, SA 5005, Australia
[3] Univ Melbourne, Mol Sci & Biotechnol Inst Bio21, Melbourne, Vic 3010, Australia
[4] Univ Cambridge, Dept Chem, Cambridge CB2 1EW, England
[5] Crop & Food Res, Christchurch, New Zealand
关键词
amyloid fibril; protein nanofibre; crystallin; WAXS; TEM; AMYLOID FIBRIL FORMATION; APOLIPOPROTEIN-C-II; ALPHA-A-CRYSTALLIN; AGGREGATION; NANOTUBES; CONSTRAINTS; PREDICTION; CHAPERONE; PEPTIDES; CATARACT;
D O I
10.1504/IJNT.2009.022918
中图分类号
TB3 [工程材料学];
学科分类号
0805 ; 080502 ;
摘要
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.
引用
收藏
页码:258 / 273
页数:16
相关论文
共 51 条
[1]   Responsive gels formed by the spontaneous self-assembly of peptides into polymeric beta-sheet tapes [J].
Aggeli, A ;
Bell, M ;
Boden, N ;
Keen, JN ;
Knowles, PF ;
McLeish, TCB ;
Pitkeathly, M ;
Radford, SE .
NATURE, 1997, 386 (6622) :259-262
[2]   Cytochrome display on amyloid fibrils [J].
Baldwin, AJ ;
Bader, R ;
Christodoulou, J ;
MacPhee, CE ;
Dobson, CM ;
Barker, PD .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2006, 128 (07) :2162-2163
[3]   Protein reconstitution and three-dimensional domain swapping: Benefits and constraints of covalency [J].
Carey, Jannette ;
Lindman, Stina ;
Bauer, Mikael ;
Linse, Sara .
PROTEIN SCIENCE, 2007, 16 (11) :2317-2333
[4]   Age-related changes in bovine alpha-crystallin and high-molecular-weight protein [J].
Carver, JA ;
Nicholls, KA ;
Aquilina, JA ;
Truscott, RJW .
EXPERIMENTAL EYE RESEARCH, 1996, 63 (06) :639-647
[5]   Protein misfolding, functional amyloid, and human disease [J].
Chiti, Fabrizio ;
Dobson, Christopher M. .
ANNUAL REVIEW OF BIOCHEMISTRY, 2006, 75 :333-366
[6]   Controlling the morphology of cross β-sheet assemblies by rational design [J].
Deechongkit, S ;
Powers, ET ;
You, SL ;
Kelly, JW .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2005, 127 (23) :8562-8570
[7]   Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains [J].
Dubay, KF ;
Pawar, AP ;
Chiti, F ;
Zurdo, J ;
Dobson, CM ;
Vendruscolo, M .
JOURNAL OF MOLECULAR BIOLOGY, 2004, 341 (05) :1317-1326
[8]   A de novo designed helix-turn-helix peptide forms nontoxic amyloid fibrils [J].
Fezoui, Y ;
Hartley, DM ;
Walsh, DM ;
Selkoe, DJ ;
Osterhout, JJ ;
Teplow, DB .
NATURE STRUCTURAL BIOLOGY, 2000, 7 (12) :1095-1099
[9]   Functional amyloid formation within mammalian tissue [J].
Fowler, DM ;
Koulov, AV ;
Alory-Jost, C ;
Marks, MS ;
Balch, WE ;
Kelly, JW .
PLOS BIOLOGY, 2006, 4 (01) :100-107
[10]   A possible role for π-stacking in the self-assembly of amyloid fibrils [J].
Gazit, E .
FASEB JOURNAL, 2002, 16 (01) :77-83