硫黄素
纤维
化学
生物物理学
淀粉样纤维
淀粉样蛋白(真菌学)
荧光
超氧化物歧化酶
SOD1
蛋白质聚集
生物化学
淀粉样β
氧化应激
病理
生物
阿尔茨海默病
无机化学
物理
疾病
医学
量子力学
作者
Naoto Iwakawa,Daichi Morimoto,Erik Walinda,Yasushi Kawata,Masahiro Shirakawa,Kenji Sugase
摘要
Amyloid fibril formation is associated with numerous neurodegenerative diseases. To elucidate the mechanism of fibril formation, the thioflavin T (ThT) fluorescence assay is widely used. ThT is a fluorescent dye that selectively binds to amyloid fibrils and exhibits fluorescence enhancement, which enables quantitative analysis of the fibril formation process. However, the detailed binding mechanism has remained unclear. Here we acquire real-time profiles of fibril formation of superoxide dismutase 1 (SOD1) using high-sensitivity Rheo-NMR spectroscopy and detect weak and strong interactions between ThT and SOD1 fibrils in a time-dependent manner. Real-time information on the interaction between ThT and fibrils will contribute to the understanding of the binding mechanism of ThT to fibrils. In addition, our method provides an alternative way to analyze fibril formation.
科研通智能强力驱动
Strongly Powered by AbleSci AI