||Structural characterization of amyloid fibrils of human α-synuclein by small-angle scattering
河野, 史明 ,
松尾, 龍人 ,
高田, 慎一 ,
杉本, 泰伸藤原, 悟
Amyloid fibrils of α-synuclein (α-Syn) (and/or its intermediate structures toward the mature fibrils) is involved with pathogenesis of Parkinson's disease. Structural characterization of amyloid fibrils is important for elucidation of the mechanism of the fibril formation of α-Syn and thereby elucidation of the mechanism of the pathogenesis. Here we characterize the structure of amyloid fibrils of α-Syn by small-angle X-ray and neutron scattering (SAXS and SANS). Combined analysis of the SAXS and SANS curves shows that the diameter of the fibrils is about 15 nm, and the density of the fibril increases towards its outer region. It is also suggested that significant hydration occurs in the α-Syn molecules within the fibrils.