Structural basis of the self-propagation of amyloid fibrils and its manifestation
| Project/Area Number |
25440071
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Biophysics
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| Research Institution | Kobe University |
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Principal Investigator |
Chatani Eri 神戸大学, 理学(系)研究科(研究院), 准教授 (00432493)
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| Project Period (FY) |
2013-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2015: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2014: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2013: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | 蛋白質 / フォールディング / ミスフォールディング / アミロイド線維 / 中間体 / インスリン / 伝播性 / アミロイド / 伝播 / タンパク質 / 凝集 |
|---|
| Outline of Final Research Achievements |
Amyloid fibrils are a form of protein aggregates associated with numerous diseases. One of the most unique and essential properties is their ability to self-propagate, which leads to the explosive amplification of amyloid fibrils and then the onset of the diseases; however, much remains to be elucidated regarding its molecular details how and when the propagating nuclei initially emerge.
In this study, we have trapped and characterized structural properties of prefibrillar intermediate species of insulin and an insulin-derived short peptide, and as for insulin, we have clarified time-dependent formation and evolution of the prefibrillar intermediates by time-resolved small angle X-ray scattering measurement. We also performed time-resolved NIR spectral measurement to clarify more details of the water molecular system dynamics during the nucleation.
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Report
(4 results)
Research Products
(86 results)
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[Presentation] アミロイド線維構造の面白さ2015
Author(s)
茶谷 絵理
Organizer
第55回日本生物物理若手の会夏の学校
Place of Presentation
琵琶湖畔・近江白浜・白浜荘（滋賀県・高島市）
Year and Date
2015-08-23
Related Report
Invited
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