Dopamine cannot promote oligomerization of unoxidized α-synuclein

Shimotakahara, Sakurako and Matsui, Mika and Sakuma, Chiseko and Takahashi, Teruaki and Fujimoto, Takashi and Furihata, Kazuo and Kojima, Masaki and Seino, Shohei and Machinami, Tomoya and Shibusawa, Yoichi and Uéda, Kenji and Tashiro, Mitsuru (2013) Dopamine cannot promote oligomerization of unoxidized α-synuclein. Journal of Biophysical Chemistry, 04 (03). pp. 110-114. ISSN 2153-036X

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Abstract

α-Synuclein is the major component of the filamentous Lewy bodies and Lewy neurites that define neuropathological features of Parkinson’s disease and dementia with Lewy bodies. To investigate the oligomerization process of α-synuclein in association with dopamine (DA), the structural propensities to form oligomers were studied using NMR and other biophysical techniques. The1H-15N HSQC spectra indicated that both N- and C-termini interacted with DA. Although interactions with DA were also observed in the presence of glutathione by ESI-MS, the significant suppression of oligomerization was observed in the size exclusion chromatography, suggesting that oxidations of α-synuclein are required for its oligomerization.

Item Type: Article
Subjects: STM Library > Chemical Science
Depositing User: Managing Editor
Date Deposited: 11 Mar 2023 07:16
Last Modified: 22 May 2024 08:28
URI: http://open.journal4submit.com/id/eprint/889

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