Structural analysis of proteins in amyloid fibrils using a new method of small-angle neutron scattering
| Project/Area Number |
16K13730
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Quantum beam science
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| Research Institution | National Institutes for Quantum and Radiological Science and Technology |
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Principal Investigator |
FUJIWARA Satoru 国立研究開発法人量子科学技術研究開発機構, 高崎量子応用研究所 東海量子ビーム応用研究センター, 上席研究員(定常) (10354888)
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| Research Collaborator |
MATSUO tatsuhito
KONO fumiaki
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| Project Period (FY) |
2016-04-01 – 2019-03-31
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| Project Status |
Completed (Fiscal Year 2018)
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| Budget Amount *help |
¥3,640,000 (Direct Cost: ¥2,800,000、Indirect Cost: ¥840,000)
Fiscal Year 2017: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
Fiscal Year 2016: ¥2,860,000 (Direct Cost: ¥2,200,000、Indirect Cost: ¥660,000)
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| Keywords | 中性子小角散乱 / 重水素化蛋白質 / アミロイド線維 / シヌクレイン / 量子ビーム / 蛋白質 |
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| Outline of Final Research Achievements |
The purpose of this study is to develop a new method of small-angle neutron scattering (SANS) for analyzing the structure of individual proteins with eliminating the effects of the inter-protein interferences. This enables one to analyze the structure of proteins within disordered aggregates. Using this method, we analyzed the structure of the protein, alpha-synuclein (aSyn), within amyloid fibrils. This system is important because formation of amyloid fibrils of aSyn is closely related to the pathogenesis of Parkinson's disease. This new method employs deuterated proteins, so we deuterated aSyn, and verified that this deuterated protein has similar characteristics to the usual hydrogenated proteins. We carried out the SANS measurements on amyloid fibrils of aSyn using the new method. Comparison of the observed SANS curves with the theory indicated the feasibility of this method. Analysis of the curves obtained suggested that in the fibrils, aSyn adopts extended structures.
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| Academic Significance and Societal Importance of the Research Achievements |
本研究では、中性子小角散乱の新しい測定法を開発する。この方法により小角散乱曲線を歪める粒子間干渉効果を分離して個々の蛋白質の散乱曲線を解析することができる。この方法により初めてアミロイド線維のような配列の乱れた蛋白質凝集体中の個々の蛋白質の構造解析が可能となる。このように、この新しい測定法により、これまで解析することができなかった様々な不規則構造系の構造解析が可能となり、中性子小角散乱の有用性がさらに大きく広がるとともに、不規則構造系の研究の大きな進展が期待される。
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Report
(4 results)
Research Products
(16 results)
