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Complex Formation of 1,6-Anhydro-β-Maltose and Sodium Ions Using Single-Crystal X-Ray Crystallography and NMR Spectroscopy

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American Journal of Analytical Chemistry 2013年第8期4卷 361-367页

作者： Takashi Fujimoto Daisuke Miura Takayuki Kato Osamu Kamo Yuichi Shimoikeda Tomoya Machinami mitsuru tashiro Department of Chemistry School of Sciences and Engineering Meisei University Hino Japan Solution & Marketing Division JEOL RESONANCE Inc. Akishima Japan

Complex formation of 1,6-anhydro-β-maltose and sodium ions was characterized using single-crystal X-ray crystallography and solution- and solid-state NMR spectroscopy. The 7-coordination structure, comprising two 1,6-anhydro-β-maltoses, a thiocyanate ion and a sodium ion, was identified in the crystal of the complex, where a sodium ion was positioned in the center of the pentagon. In the NMR study, the line broadening of 23Na signals and the decrease of the spin-lattice relaxation times (T1) of 23Na were observed in CD3OD in the presence of 1,6-anhydro-β-maltose, indicating complex formation.

关键词： 1 6-Anhydro-β-Maltose Complex Formation Single-Crystal X-Ray Crystallography Solid-State NMR Spectroscopy

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Demonstration of three dopamine molecules bound to α-Synuclein: Implication of oligomerization at the initial stage

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Journal of Biophysical Chemistry 2012年第2期3卷 149-155页

作者： Sakurako Shimotakahara Yuuki Shiroyama Takashi Fujimoto Mai Akai Takaya Onoue Hiroko Seki Sayaka Kado Tomoya Machinami Yoichi Shibusawa Kenji Uéda mitsuru tashiro Chemical Analysis Center Chiba University Chiba Japan Department of Chemistry School of Sciences and Engineering Meisei University Tokyo Japan Department of Dementia and Higher Brain Function Tokyo Metropolitan Institute of Medical Science Tokyo Japan School of Life Science Tokyo University of Pharmacy and Life Science Tokyo Japan School of Pharmacy Tokyo University of Pharmacy and Life Science Tokyo Japan

α-Synuclein is the major component of the filamentous Lewy bodies and Lewy neurites that define neuropathological features and dementia with Lewy bodies. To investigate the role of dopamine (DA) in α-synuclein fibrillation, the structural propensities to form oligomers at the initial stage fibrillation were studied using size exclusion chromatography and various biophysical techniques. Interactions with DA were observed for wild-type α-synuclein and its mutants, A30P, E46K and A53T, using electrospray ionization mass spectrometry (ESI-MS). The results of ESI-MS indicate that an intact α-synuclein, which was not oxidized, had an ability to bind with three molecules of DA at the initial stage. Furthermore, upon binding to DA, α-synuclein oligomerizes to higher molecular weight species. These oligomers are structurally different from amyloid fibrils, as confirmed by thioflavin T and CD analysis.

关键词： α-Synuclein Dopamine Fibrillation Oligomerization Mass Spectrometry

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Dopamine cannot promote oligomerization of unoxidized α-synuclein

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Journal of Biophysical Chemistry 2013年第3期4卷 110-114页

作者： Sakurako Shimotakahara Mika Matsui Chiseko Sakuma Teruaki Takahashi Takashi Fujimoto Kazuo Furihata Masaki Kojima Shohei Seino Tomoya Machinami Yoichi Shibusawa Kenji Uéda mitsuru tashiro Department of Chemistry School of Sciences and Engineering Meisei University Tokyo Japan Division of Agriculture and Agricultural Life Sciences The University of Tokyo Tokyo Japan School of Life Science Tokyo University of Pharmacy and Life Science Tokyo Japan School of Pharmacy Tokyo University of Pharmacy and Life Sciences Tokyo Japan

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.

关键词： α-Synuclein Dopamine Glutathione Oligomerization

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Demonstration of Three Dopamine Molecules Bound to α-Synuclein:Implication of Oligomerization at the Initial Stage

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Journal of Biophysical Chemistry 2012年第2期

作者： Sakurako Shimotakahara Yuuki Shiroyama Takashi Fujimoto Mai Akai Takaya Onoue Hiroko Seki Sayaka Kado Tomoya Machinami Yoichi Shibusawa Kenji Uéda mitsuru tashiro

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