Studies of structure-function relationship and self-aggregation mechanism of tau protein for development of the therapeutic drug of Alzheimer's disease.
| Project/Area Number |
21590050
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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 |
Physical pharmacy
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| Research Institution | Osaka University of Pharmaceutical Sciences |
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Principal Investigator |
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| Co-Investigator(Renkei-kenkyūsha) |
TOMOO Koji 大阪薬科大学, 薬学部, 准教授 (70257898)
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| Project Period (FY) |
2009 – 2011
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| Project Status |
Completed (Fiscal Year 2011)
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| Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2011: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2010: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2009: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | 生物物理化学 / タウ蛋白質 / 微小管結合ドメイン / 自己重合 / 認知症治療薬 / 抗体 |
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| Research Abstract |
Information on the structural scaffold for tau aggregation is important in developing a method of preventing Alzheimer's disease. Therefore, we studied the elucidation of a common structural element necessary for the self-assembly of full-length tau using various physico-chemical methods. As the result, it was revealed that the C-H…πinteraction between the Ile308 and Tyr310 side chains in the third repeat of MBD is indispensable for the self-assembly of full-length tau. Moreover, we have determined the crystal structure of the Fab2r coexisted with its partial antigen peptide VQIINK and clarified the recognition mode of antigen peptide by the antigen. The detailed structural information will help to understand tau polymerization and the affinity maturation for inhibition of AD progress.
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Report
(4 results)
Research Products
(29 results)
