Development of the peptide array which can distinguish metals, and its medical application
| Project/Area Number |
23500546
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Biomedical engineering/Biological material science
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| Research Institution | Meiji University |
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Principal Investigator |
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| Project Period (FY) |
2011 – 2013
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2013: ¥650,000 (Direct Cost: ¥500,000、Indirect Cost: ¥150,000)
Fiscal Year 2012: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
Fiscal Year 2011: ¥3,770,000 (Direct Cost: ¥2,900,000、Indirect Cost: ¥870,000)
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| Keywords | 機能性ペプチド / 金属認識 / ＣＤ / ＥＳＲ / 相互作用 / 自己組織化 / ペプチド / 金属イオン / 電位差滴定 / プリオン / 銅イオン / 金属タンパク / ペプチドアレイ |
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| Research Abstract |
Clarifying the mechanism of binding of peptides to various metals leads to development of self-organization and medical application. Binding of protein to metal is important as a function of active center of enzyme reactions and also may result in the misfolding of neurodegenerative protein. To elucidate the mechanism of metal recognition of peptide toward the development of new peptide array, we investigated the short peptides of human prion protein (PrP) that bind to divalent metal ions and the stability of these bound structure. UV, CD and ESR spectra indicated two kinds of coordination modes for the binding of peptide-Cu. By potentiometric titration, competitive binding of other divalent metal ions, such as Co, Ni, Zn, and Mn, to peptide-Cu revealed that these metal ions were substitute for Cu. Variation of amino-acid sequence of peptide affected the quantity of each metal substituted.
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Report
(4 results)
Research Products
(16 results)
