The mechanism of the inhibition of protein aggregation that causes conformational diseases by low-moleculer compunds
Project/Area Number |
19570155
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Biophysics
|
Research Institution | Osaka Prefecture University |
Principal Investigator |
ONDA Maki Osaka Prefecture University, 理学系研究科, 助教 (60311916)
|
Project Period (FY) |
2007 – 2009
|
Project Status |
Completed (Fiscal Year 2009)
|
Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2009: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2008: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2007: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
|
Keywords | セルピン / コンフォメーション病 / 認知症 / 神経変性 / フォールディング / 痴呆 / タンパク質の折りたたみ / リフォールディング / 凝集体形成 / 脳 |
Research Abstract |
Neuroserpin is a neuronal protein predominantly expressed in the brain, and its mutants readily form aggregates that cause dementia. Several compounds that prevent aggregation of neuroserpin were found, and crystals of human neuroserpin were successfully obtained using them. The crystal structure was determined at 2.1Å, and interactions between the protein and the compound were analyzed. Furthermore, the compounds were effective in stabilizing a refolding intermediate of neuroserpin, which is promising for a target molecule in therapeutic drug design. Using the compounds, the intermediate was purified and characterized.
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Report
(4 results)
Research Products
(27 results)