2005 Fiscal Year Final Research Report Summary
Development of artificial receptors that can recognize a specific protein surface in aqueous solution
| Project/Area Number |
15350104
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Chemistry related to living body
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| Research Institution | Kyoto University (2005)
Kyushu University (2003-2004) |
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Principal Investigator |
HAMACHI Itaru Kyoto University, Engineering, Professor, 工学研究科, 教授 (90202259)
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| Co-Investigator(Kenkyū-buntansha) |
OJIDA Akio Kyoto University, Engineering, Assistant Professor, 工学研究科, 助手 (10343328)
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| Project Period (FY) |
2003 – 2005
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| Keywords | molecular recognition / chemosensor / phosphorylated protein / metal complex |
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| Research Abstract |
During the project term, molecular recognition chemistry toward phosphorylated proteins and peptides has greatly advanced both in fundamental science and application. My group newly developed artificial receptor molecules based on Zn-metal complexes which can recognize phosphorylated peptides and proteins and sense them by a fluorescence signal change. These can be carried out in aqueous solution and SDS-PAGE gel plates. Detailed study using isothermal titration calorimetry clearly demonstrates that the Zn sites of the receptors tightly bind to the anionic phospate sites of the peptide and thus shows the strong affinity. Further more, using this strong binding, we also tested the inhibition capability of the receptors for the phospho-protein protein interactions. In the case of the cross-linking binding mode of the dinuclear Zn complex type of receptors, it is clear that the effective disruption of the phospho-protein protein interactions between WW domain and the phosphorylated C-terminal domain of Polymerase. These results clearly indicate that artificial receptors can act not only as a simple fluorescent chemosensor for phosphorylated peptides and proteins, but also as a poteintial disruptor for the phospho-protein protein interactions. It is expected that the present accomplishment strongly stimulate the relevant research and may lead to a more sophisticated molecule in the near future.
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