2013 Fiscal Year Final Research Report
DISTANCE MEASUREMENTS OF FIBROUS PRION PROTEINS BY PULSE ESR SPECTROSCOPY
| 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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| 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 |
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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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Research Products
(16 results)
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[Journal Article] Radiosensitization of tumor cells through endoplasmic reticulum stress induced by PEGylated nanogel containing gold nanoparticles2014
Author(s)
Yasui H, Takeuchi R, Nagane M, Meike S, Nakamura Y, Yamamori T, Ikenaka Y, Kon Y, Murotani H, Oishi M, Nagasaki Y, Inanami O.
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Journal Title
Cancer Lett
Volume: 347(1)
Pages: 151-158
DOI
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