| Project/Area Number |
16K13098
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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 |
Chemical biology
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| Research Institution | Shinshu University |
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Principal Investigator |
Ohkanda Junko 信州大学, 学術研究院農学系, 教授 (50233052)
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| Co-Investigator(Renkei-kenkyūsha) |
IMANISHI Miki 京都大学, 化学研究所, 講師 (80362391)
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| Research Collaborator |
HOSOYA Yusuke
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| Project Period (FY) |
2016-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥3,640,000 (Direct Cost: ¥2,800,000、Indirect Cost: ¥840,000)
Fiscal Year 2017: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2016: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Keywords | 非構造性たんぱく質 / 概日時計転写因子 / IDPs / 阻害剤探索 / Bmal1 / Clock / 蛍光偏光結合試験 / 組換えたんぱく質発現 / E-Box DNA / 蛍光サーマルシフト / 蛍光偏光 / 概日リズム / 転写因子 / 中分子ライブラリ / 非構造たんぱく質 / 阻害剤 |
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| Outline of Final Research Achievements |
Synthetic compounds that control the structural changes and interactions of intrinsically disordered proteins (IDPs) are expected to be a breakthrough that paves the way for new drug discovery. However, details of IDPs are still unknown, and almost no inhibitors that specifically disrupt IDP’s functions have been found. In this study, we focused on the Circadian Clock transcription factors Clock and Bmal 1 that are known as typical IDPs in which more than 30% in length are highly disordered. We obtained truncated version of recombinant Clock and Bmal1, and constructed a system of fluorescent polarization assay for heterodimer formation of Clock/Bmal 1. As a result of evaluation of low-molecular-weight aromatic compound library, we succeeded in finding a compound which significantly inhibits intermolecular interaction of Clock / Bmal1.
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