| Project/Area Number |
25670058
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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 |
Drug development chemistry
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| Research Institution | The University of Tokushima |
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Principal Investigator |
OTAKA Akira 徳島大学, ヘルスバイオサイエンス研究部, 教授 (20201973)
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| Project Period (FY) |
2013-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2014: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2013: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | タンパク質 / ラベル化 / 標的タンパク質 / N-Sアシル転移 / タンパク質ラベル化 / チオエステル / ケミカルバイオロジー |
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| Outline of Final Research Achievements |
In cell labeling of proteins is an essential technology for elucidating the function of proteins in living cells. Among various strategies, an affinity labeling with the use of protein ligands and electrophilic moieties has been widely used. Achievement of an affinity labeling requires the tuning of reactivity of an electrophilic moiety to prevent non-specific labeling. Recently, we reported the N-sulfanylethylanilide (SEAlide) as a tunable electrophilic moiety. Although the SEAlide, an anilide compound, almost remains intact, addition of phosphate salts as acid-based catalyst induces conversion of the stable anilide linkage to the the electrophilic thioester via N-S acyl transfer. On the basis of this interesting feature of the SEAlide, we developed highly efficient labelling reagnets for proteins with practical application of labelling of model proteins using SEAlide based reagents.
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