Engineering amyloidogenicity towards the development of nanofibrillar materials

被引:80
作者
Hamada, D
Yanagihara, I
Tsumoto, K
机构
[1] Osaka Med Ctr Maternal & Child Hlth, Res Inst, Dept Dev Infect Dis, Osaka 5941011, Japan
[2] Tohoku Univ, Grad Sch Engn, Dept Biomol Engn, Aoba Ku, Sendai, Miyagi 9808579, Japan
基金
日本学术振兴会;
关键词
D O I
10.1016/j.tibtech.2003.12.003
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
When folded into their native structures, proteins in biological systems function as nanostructured machines. By contrast, some polypeptides tend to aggregate into other well-ordered structures, namely amyloid fibrils. Such well-ordered protein fibrils are attractive materials for nanobiotechnology because they self-associate through noncovalent bonds under controlled conditions - a property that is shared with small organic molecules called organogelators. Recently, the use of amyloid fibrils as structural templates for constructing nanowires has been demonstrated. Such applications will potentially become one of the next trends in protein engineering and nanobiotechnology.
引用
收藏
页码:93 / 97
页数:5
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