Thermodynamic analysis of pressure- and temperature-dependent structural changes of amyloid fibril and its oligomeric intermediates
Project/Area Number |
15K07038
|
Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Biophysics
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Research Institution | Kindai University |
Principal Investigator |
|
Co-Investigator(Kenkyū-buntansha) |
李 映昊 大阪大学, たんぱく質研究所, 講師 (70589431)
|
Project Period (FY) |
2015-04-01 – 2018-03-31
|
Project Status |
Completed (Fiscal Year 2017)
|
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)
|
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 |
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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Report
(4 results)
Research Products
(32 results)
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[Journal Article] Non-native alpha-helices in the initial folding intermediate facilitate the ordered assembly of the beta-barrel in beta-lactoglobulin2017
Author(s)
Sakurai, K., Yagi, M., Konuma, T., Takahashi, S., Nishimura, C., Goto, Y.
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Journal Title
Biochemistry
Volume: 56
Issue: 36
Pages: 4799-4807
DOI
Related Report
Peer Reviewed / Open Access
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[Journal Article] A. Reduced Lipid Bilayer Thickness Regulates the Aggregation and Cytotoxicity of Amyloid-β2017
Author(s)
Kyle J. Korshavn, Cristina Satriano, Yuxi Lin, Rongchun Zhang, Mark Dulchavsky, Anirban Bhunia, Magdalena I. Ivanova, Young-Ho Lee, Carmelo La Rosa, Mi Hee Lim, Ayyalusamy Ramamoorthy
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Journal Title
J. Biol. Chem.
Volume: 292
Issue: 11
Pages: 4638-4650
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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[Journal Article] Energetic basis on interactions between ferredoxin and ferredoxin NADP+ reductase at varying physiological conditions.2016
Author(s)
Kinoshita, M., Kim, J.Y., S., Lin, Y., Hun Mok K., Kataoka, Y., Ishimori, K., Markova, N., Kurisu, G., Hase, T., Lee, Y.H.
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Journal Title
Biochem. Biophys. Res. Commun.
Volume: 482
Issue: 4
Pages: 909-915
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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