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Dynamic Properties of Human alpha-Synuclein Related to Propensity to Amyloid Fibril Formation
https://repo.qst.go.jp/records/76744
https://repo.qst.go.jp/records/76744332d6115-30c2-400a-b8f0-57865ae93f79
| Item type | 学術雑誌論文 / Journal Article(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2019-06-24 | |||||
| タイトル | ||||||
| タイトル | Dynamic Properties of Human alpha-Synuclein Related to Propensity to Amyloid Fibril Formation | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
| 資源タイプ | journal article | |||||
| アクセス権 | ||||||
| アクセス権 | metadata only access | |||||
| アクセス権URI | http://purl.org/coar/access_right/c_14cb | |||||
| 著者 |
Fujiwara, Satoru
× Fujiwara, Satoru× Kono, Fumiaki× Matsuo, Tatsuhito× Sugimoto, Yasunobu× Matsumoto, Tomoharu× Narita, Akihiro× Shibata, Kaoru× Satoru, Fujiwara× Fumiaki, Kono× Tatsuhito, Matsuo |
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| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | Alpha-synuclein (aSyn) is an intrinsically disordered protein (IDP) that can form amyloid fibrils. Fibrils of aSyn are implicated with the pathogenesis of Parkinson's disease and other synucleinopathies. Elucidating the mechanism of fibril formation of aSyn is therefore important for understanding the mechanism of the pathogenesis of these diseases. Fibril formation of aSyn is sensitive to solution conditions, suggesting that fibril formation of aSyn arises from the changes in its inherent physico-chemical properties, particularly its dynamic properties because IDPs such as aSyn utilize their inherent flexibility to function. Characterizing these properties under various conditions should provide insights into the mechanism of fibril formation. Here, using the quasielastic neutron scattering (QENS) and small-angle X-ray scattering (SAXS) techniques, we investigated the dynamic and structural properties of aSyn under the conditions, where mature fibrils are formed (pH 7.4 with a high salt concentration), where clumping of short fibrils occurs (pH 4.0), and where fibril formation is not completed (pH 7.4). The SAXS measurements showed that the extended structures at pH 7.4 with a high salt concentration become compact at pH 4.0 and 7.4. The QENS measurements showed that both intra-molecular segmental motions and local motions such as side-chain motions are enhanced at pH 7.4 with a high salt concentration, compared to those at pH 7.4 without salt, whereas only the local motions are enhanced at pH 4.0. These results imply that fibril formation of aSyn requires not only the enhanced local motions but also the segmental motions such that proper inter-molecular interactions are possible. | |||||
| 書誌情報 |
Journal of Molecular Biology 巻 431, 号 17, p. 3229-3245, 発行日 2019-08 |
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| 出版者 | ||||||
| 出版者 | Elsevier | |||||
| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 0022-2836 | |||||
| DOI | ||||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | 10.1016/j.jmb.2019.05.047 | |||||
| 関連サイト | ||||||
| 識別子タイプ | URI | |||||
| 関連識別子 | https://www.sciencedirect.com/journal/journal-of-molecular-biology/vol/431/issue/17 | |||||
