| Project/Area Number |
15K07038
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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 |
Biophysics
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| Research Institution | Kindai University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
李 映昊 大阪大学, たんぱく質研究所, 講師 (70589431)
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2017: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2016: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2015: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
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| Keywords | アミロイド線維 / フォールディング / 凝集中間体 / 高圧NMR / 温度圧力依存性 / 温度圧力変性 |
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| Outline of Final Research Achievements |
Amyloid fibrils are insoluble proteinaceous aggregates, related with several diseases. During their formation reactions, oligomeric intermediates were known to appear. Knowledge of thermodynamics of such intermediate states are relevant to understanding the mechanism of fibrillogenesis. We planned to control the population of the fibril and intermediate states by adjusting the pressure and temperature conditions, then spectroscopically characterize the targeted states. Unfortunately, since irreversibility of fibrillogenesis was confirmed, ideal thermodynamic analysis was considered to be inappropriate. Therefore, we focused our efforts on finding the conditions where the intermediate states will dominantly populate and characterizations of structural properties of such states. According to this aim, we investigated condition-dependent structural changes of β2m、αSyn、Aβ and discussed the contributions of these intermediate state to the fibrillogenesis based on the obtained results.
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