Engineering amyloidogenicity towards the development of nanofibrillar materials.
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.
Hamada
Daizo
D
Department of Developmental Infectious Diseases, Research Institute, Osaka Medical Centre for Maternal and Child Health (MCHRI), 840 Murodo-cho, Izumi, 594-1011, Osaka, Japan. daizo@lab.mch.pref.osaka.jp
Yanagihara
Itaru
I
Tsumoto
Kouhei
K
D000682:Amyloid / Q000138:chemical synthesis / Q000737:chemistry*; D001709:Biotechnology / Q000295:instrumentation / Q000379:methods; D000075202:Contraindications; D003460:Crystallization / Q000379:methods*; D004581:Electronics / Q000295:instrumentation* / Q000379:methods*; D046911:Macromolecular Substances; D036103:Nanotechnology / Q000295:instrumentation* / Q000379:methods*; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D015202:Protein Engineering / Q000379:methods*
D000682:Amyloid; D046911:Macromolecular Substances; D010455:Peptides