| Project/Area Number |
15K13740
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Bio-related chemistry
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| Research Institution | Nagoya University |
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Principal Investigator |
Shoji Osami 名古屋大学, 理学(系)研究科(研究院), 准教授 (90379587)
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| Project Period (FY) |
2015-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2015: ¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
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| Keywords | 変性蛋白質 / 自己集合 / 繊毛 / ベータシート構造 / アミロイド繊維 / アルツハイマー病 / アミロイド線維 |
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| Outline of Final Research Achievements |
The pilus part of Type I fimbria found on the surface of Gram-negative bacteria is composed of multiple copies of FimA and the last piece of FimA is linked to FimH via FimF and FimG. Each structural unit has an immunoglobulin (Ig)-like fold, which is formed from two-layered β-sheets. We have found that a soluble but denatured form of FimG protein can accommodate various hydrophobic molecules. Inhibiting the self-assembly of β-amyloid (Aβ) is considered to be one of the strategies through which to treat Alzheimer’s disease. Thus, we have tried to inhibit the self-assembly of Aβ using the denatured form of FimG and demonstrated that the denatured form of FimG prevents Aβ oligomerization.
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