Quasielastic neutron scattering study of human -synuclein; Implication for propensity for amyloid fibril formation
ヒト-シヌクレインの中性子準弾性散乱研究; アミロイド線維形成のしやすさとの関連
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*
A protein -synuclein (-Syn) forms amyloid fibrils. This abnormal protein aggregation is related to pathogenesis of a neuro-degenerative disorder, Parkinson's disease. Propensity for amyloid fibril formation depends on environmental conditions such as pH. We carried out quasielastic neutron scattering experiments to investigate the "dynamic" behavior of -Syn to investigate the relationship between the dynamics and propensity for amyloid fibril formation. The measurements on the solution samples of -Syn in different pH were carried out using a high energy resolution near-backscattering spectrometer, BL02 (DNA), at MLF/J-PARC, Japan. Differences in flexibility of the protein were detected between the different conditions. Since the difference in flexibility is likely to arise from different distributions of conformational substates of -Syn, the results obtained suggest an entropy-driven mechanism of the amyloid fibril formation.