Development of copper(I) fluorescent sensors based on photoinduced electron transfer mechanism and their application to optical imaging of cells
| Project/Area Number |
21750168
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Chemistry related to living body
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| Research Institution | Kyoto University |
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Principal Investigator |
TAKI Masayasu Kyoto University, 地球環境学堂, 助教 (70378850)
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| Project Period (FY) |
2009 – 2010
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| Project Status |
Completed (Fiscal Year 2010)
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| Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2010: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2009: ¥3,380,000 (Direct Cost: ¥2,600,000、Indirect Cost: ¥780,000)
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| Keywords | 生物無機化学 / バイオセンサー / 銅一価蛍光プローブ / 蛍光イメージング / 還元型フルオレセイン / ミトコンドリア局在型 / ローダミン誘導体 / チオエーテル配位子 / 光誘起電子移動 / 銅一価イオン / 蛍光プローブ / 結晶構造 / 酸化還元電位 |
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| Research Abstract |
We have developed copper(I)-selective fluorescent probes as a chemical tool for monitoring behavior of copper ions in living cells. We initially synthesized various tioether-containing ligands and prepared the corresponding copper(I) complexes. Spectroscopic measurements and X-ray crystal structure analysis of these copper(I) complexes indicate that the linker chain length of the thioether ligand strongly affect the affinity toward copper(I) ion, binding fashion, and redox potential of copper. We next developed novel copper(I) fluorescent probes based on the oxidative cleavage mechanism. These probes contain a reduced form of fluorescein and TPA tetradentate ligand, those are linked through a benzyl ether group. We found that strong fluorescence is observed when copper(I) is added to the probe solution containing sub mM of gluthatione in water. The same reaction undergoes even in cells. Therefore, this will be useful chemical tool to probe intracellular copper(I) ion behavior.
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Report
(3 results)
Research Products
(39 results)
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[Journal Article] Electron microscopic visualization of the filament binding mode of actin binding proteins.2011
Author(s)
T.Ito, T.Hirayama, M.Taki, S.Iyoshi, S.Dai, S.Takeda, C.Kimura-Sakiyama, T.Oda, Y.Yamamoto, Y.Maeda, A.Narita
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Journal Title
Journal of Molecular Biology 408
Pages: 26-39
Related Report
Peer Reviewed
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[Journal Article] Electron Microscopic Visualization of the Filament Binding Mode of Actin-Binding Proteins2011
Author(s)
T.Ito, T.Hirayama, M.Taki, S.Iyoshi, S.Dai, S.Takeda, C.Kimura-Sakiyama, T.Oda, Y.Yamamoto, Y.Maeda, A.Narita
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Journal Title
Journal of Molecular Biology
Volume: 408
Pages: 26-39
Related Report
Peer Reviewed
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