Changes in the dynamics of human -synuclein detected by neutron scattering

中性子散乱により検出したヒト-シヌクレインのダイナミクス変化

藤原 悟; 荒木 克哉*; 松尾 龍人; 八木 寿梓*; 山田 武*; 柴田 薫  ; 望月 秀樹*

Fujiwara, Satoru; Araki, Katsuya*; Matsuo, Tatsuhito; Yagi, Hisashi*; Yamada, Takeshi*; Shibata, Kaoru; Mochizuki, Hideki*

The protein, -synuclein (-Syn) forms amyloid fibrils. Formation of amyloid fibrils is associated with the pathogenesis of a neuro-degenerative disorder, Parkinson's disease. In order to obtain insights into the role of the protein dynamics in the mechanism of amyloid fibril formation, we carried out quasielastic neutron scattering experiments and characterized the "dynamic" behavior of -Syn. The measurements on the solution samples of -Syn in the monomeric and fibril states were carried out using a high energy resolution near-backscattering spectrometer, BL02 (DNA), at MLF/J-PARC, Japan. Differences in the dynamical behavior of the protein were detected between the monomeric and fibril states. Analysis of the spectra obtained suggested an entropy-driven mechanism of amyloid fibril formation.