| Project/Area Number |
24654112
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Single-year Grants |
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| Research Field |
Condensed matter physics II
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| Research Institution | Institute for Molecular Science |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
YAMAMORI Tohru 北海道大学, 大学院獣医学研究科, 准教授 (00512675)
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| Project Period (FY) |
2012-04-01 – 2014-03-31
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2013: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2012: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
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| Keywords | プリオン凝集体 / クロイツフェルト・ヤコブ病（CJD） / 狂牛病(ウシ海綿状脳症、BSE) / 電子スピン共鳴法（ESR） / 電子-電子二重共鳴法（DEER） / 電子間相互作用 / 距離計測 / 電子スピン共鳴 / スピンラベル |
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| Research Abstract |
This research was performed to clarify the mechanism of formation of the prion filaments. The structure of prion monomer consists of a tertiary C-terminal domain (three alpha-helices, H1, H2 and H3) and an N-terminal random domain. In the experiments, recombinant prion protein with a cysteine mutation was created by E. Coli expression system and the cysteine residue was labeled by nitroxide spin probe. After aggregated prion filaments induced by detergent, the spin-spin interaction was measured by X-band continuous-wave (CW) electron spin resonance (ESR) or Q-band pulse ESR spectrometer. The inter-spin distance was determined by Monte Carlo fitting for electron-electron interaction signals. The inter-spin distance of prion filaments spin-labeled at H1 or H2 is shorter than that of H3. However, the inter-spin distance of N-terminal domain was not estimated because of polydispersity in distance. These data suggested that H1 and H2 were involved in formation of prion filaments.
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