Spatiotemporal formation of amyloid assembly by optical trapping and fluorescence analysis of its dynamics
| Project/Area Number |
17K14427
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Physical chemistry
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| Research Institution | Hokkaido University |
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Principal Investigator |
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| Project Period (FY) |
2017-04-01 – 2019-03-31
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| Project Status |
Completed (Fiscal Year 2018)
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| Budget Amount *help |
¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2018: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2017: ¥3,120,000 (Direct Cost: ¥2,400,000、Indirect Cost: ¥720,000)
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| Keywords | 光ピンセット / 光圧 / アミロイド / タンパク質 / 顕微分光 / 顕微イメージング / レーザー / ナノバイオ / 顕微計測 |
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| Outline of Final Research Achievements |
We successfully demonstrated spatially- and temporally- controlled formation of an amyloid assembly by optical trapping of partially unfolded proteins in solution. The fluorescence analysis during the trapping process revealed that the formation of an amyloid assembly proceeds in two steps; aggregation of proteins and their amyloid fibrillation. It was found that the assembly formed in the first step consists of the entangled single fibrillar structure. Thus, it was implied that intermediate proteins prior to amyloid nucleation can form the fibrillar structure like amyloid during their assembling process.
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| Academic Significance and Societal Importance of the Research Achievements |
アミロイドは、様々な疾患と関係している不溶性のタンパク質凝集体である。確率的に起こるアミロイド核形成を溶液中で時空間制御することは難しく、溶液全体のアンサンブル測定を通してその形成過程が調べられてきた。本研究で示した新しいアミロイド集合体形成手法は、一集合体レベルでの解析を可能にし、アミロイド線維形成メカニズムの解明に大きく貢献できると期待される。
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Report
(3 results)
Research Products
(21 results)
