Studies of an early stage amyloid formation for Parkinson`s Disease casual protein.
| Project/Area Number |
20550083
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Analytical chemistry
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| Research Institution | Tokyo University of Pharmacy and Life Science |
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Principal Investigator |
TASHIRO Sakurako Tokyo University of Pharmacy and Life Science, 薬学部, 講師 (40328555)
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| Co-Investigator(Kenkyū-buntansha) |
KOJIMA Masaki 東京薬科大学, 生命科学部, 教授 (90277252)
TASHIRO Mitsuru 明星大学, 理工学部, 准教授 (40315750)
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| Project Period (FY) |
2008 – 2010
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| Project Status |
Completed (Fiscal Year 2010)
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| Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2010: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2009: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2008: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | 生物学的分析 / a-synuclein / アミロイド線維 / パーキンソン病 / ドパミン / オリゴマー中間体 / 高分子構造・物性 / アミロイド / 脳神経疾患 / 生理物理 / 分析化学 / 生物物理 |
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| Research Abstract |
In this study, we have focused on α-synuclein, the major component of amyloid plaque in Parkinson's Disease (PD). The relationship between a detailed mechanism of amyloid formations and PD has been investigated. In particular, an interaction between α-synuclein and dopamine, a neurotransmitter and well known treatment for PD, has been elucidated in terms of its effect on amyloid formation, using fluorescence, CD, gelfilteration chromatography, NMR and MS. As a result, we have shown that the presence of dopamine suppresses the formation of amyloid fibrils, while theformation of oligomer intermediates is stabilized by addition of dopamine. Furthermore, the complex formation between α-synuclein and dopamine has been confirmed, with a binding ratio of 1 to 3 dopamine molecules per α-synuclein molecule. In conclusion, we have proposed a schematic model for the mechanism of α-synuclein oligomer intermediates and amyloid formations.
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Report
(4 results)
Research Products
(21 results)
