NMR analysis of amyloid-beta soluble oligomer encapsulated in reverse micelle
| Project/Area Number |
18K06151
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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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| Review Section |
Basic Section 43040:Biophysics-related
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| Research Institution | Kyoto University |
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Principal Investigator |
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| Project Period (FY) |
2018-04-01 – 2021-03-31
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| Project Status |
Completed (Fiscal Year 2020)
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| Budget Amount *help |
¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2020: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2019: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2018: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
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| Keywords | アミロイドβ / 逆ミセル / 分子間相互作用 / NMR / 逆ミセル封入法 / アミロイド線維 / ＮＭＲ / 可溶性オリゴマー / 高分解能NMR |
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| Outline of Final Research Achievements |
It is difficult to analyze the process of oligomerization and fibril formation by amyloid-beta peptides, as it proceeds rapid and irreversibly. We developed the method to isolate each amyloid-beta molecule into reverse-micelle formed by AerosolAT (AOT) / n-hexane. We found that covalently-linked dimeric Abeta molecule adopted almost the same structure as that of wiled-type Abeta.
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| Academic Significance and Societal Importance of the Research Achievements |
アルツハイマー病以外にも、「アミロイド線維」という物質が蓄積することにより進行する病気は数多く存在する。どのようにして「アミロイド線維」が形成されるのかを明らかにすることは、これらの病気に共通した治療法の確立に欠かせない。本研究により「アミロイド線維」の形成反応が、分子同士の結合・解離を繰り返しつつ進行しているという様子が明らかになってきた。アルツハイマー病だけでなく、他の多くのアミロイド線維の形成機構に共通の反応だと考えられる。
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Report
(4 results)
Research Products
(14 results)
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[Journal Article] Structural characterization of the N-terminal kinase-interacting domain of an Hsp90-cochaperone Cdc37 by CD and solution NMR spectroscopy.2019
Author(s)
Ihama, F., Yamamoto, M., Kojima, C., Fujiwara, T., Matsuzaki, K., Miyata, Y., Hoshino, M.
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Journal Title
Biochim. Biophys. Acta-Proteins Proteom.
Volume: 1867
Issue: 9
Pages: 813-820
DOI
Related Report
Peer Reviewed
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