| Project/Area Number |
25860089
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Drug development chemistry
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| Research Institution | Teikyo University (2015)
Showa University (2013-2014) |
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Principal Investigator |
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| Project Period (FY) |
2013-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2015: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2014: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2013: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
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| Keywords | 個別化医療 / X線結晶構造解析 / ワルファリン / VKORC1 / 構造生物学 / ゲノム薬理 / コドンの最適化 / 計算科学 |
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| Outline of Final Research Achievements |
To increase the expression of Homo Sapience VKORC1 (HsVKORC1) and Rattus Norvegicus VKORC1 (RnVKORC1), we performed the codon optimization and cloned the HsVKORC1 and RnVKORC1 gene into the expression vector. After co-transfection of insect cells with baculovirus DNA and the expression vector, the recombinant baculovirus was amplified to obtain a higher titer stock solution. Virus titer was detected virus infections and plaque formation.
While we performed homology modeling of HsVKORC1, RnVKORC1, and Bos taurus VKORC1(BtVKORC1), as their three-dimensional (3D) structures had not been reported. Then, we performed molecular docking of Warfarin bound to HsVKORC1 and RnVKORC1 in molecular docking studies. As a result, our study revealed the binding site and binding mode of Warfarin into HsVKORC1, RnVKORC1, and BtVKORC1 from our docking model.
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