超声
过饱和度
纤维
纤颤
淀粉样蛋白(真菌学)
化学
亚稳态
淀粉样纤维
生物物理学
结晶
色谱法
淀粉样β
生物化学
有机化学
无机化学
内科学
生物
疾病
心房颤动
医学
作者
Yuichi Yoshimura,Masatomo So,Hisashi Yagi,Yuji Goto
标识
DOI:10.7567/jjap.52.07ha01
摘要
Amyloid fibrils are self-assemblies of proteins with an ordered cross-β architecture. Because they are associated with serious disorders, understanding their structure and mechanism of fibrillation is important. Irradiation with ultrasonication leads to fragmentation of amyloid fibrils, useful for seeding experiments. Recently, ultrasonication has been found to trigger the spontaneous formation of fibrils in solutions of monomeric amyloidogenic proteins. The results indicate that amyloid fibrillation is similar to the crystallization of solutes from a supersaturated solution. The accelerating effects of ultrasonication on amyloid fibrillation suggest that cavitation microbubbles play a key role in effectively converting the metastable state of supersaturation to the labile state, leading to spontaneous fibrillation. Moreover, ultrasonic irradiation would be promising for a high-throughput screening assay of amyloid fibrillation, advancing the study of supersaturation-limited amyloidogenesis.
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