Amyloid fibrils:: From disease to design.: New biomaterial applications for self-assembling cross-β fibrils

被引:48
作者
Gras, Sally L. [1 ]
机构
[1] Univ Melbourne, Dept Chem & Biomol Engn, Parkville, Vic 3010, Australia
[2] Univ Melbourne, Bio21 Mol Sci & Biotechnol Inst, Parkville, Vic 3010, Australia
关键词
PROTEIN-A AMYLOIDOSIS; EXTRACELLULAR-MATRIX; PEPTIDE FIBRILS; PARKINSONS-DISEASE; AGGREGATION-PRONE; PROGENITOR CELLS; CORE STRUCTURE; MODEL SYSTEMS; THIOFLAVIN-T; PREDICTION;
D O I
10.1071/CH06485
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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.
引用
收藏
页码:333 / 342
页数:10
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