| Project/Area Number |
15K18518
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Biophysics
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| Research Institution | Osaka University |
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Principal Investigator |
YOUNG-HO LEE 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 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2016: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2015: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | Alpha-synuclein / Amyloid fibril / Cold denaturation / Heat denaturation / Kinetics / Protein aggregation / Protein misfolding / Thermodynamics |
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| Outline of Final Research Achievements |
I examined cold and heat denaturation of amyloid fibrils of intrinsically disordered alpha-synuclein (aSN) prepared at various temperatures (298, 310, 323, 333, and 343 K). Despite differences in temperature for aSN amyloidogenesis, all fibrils showed similar core regions and secondary structures with the distinct width. As temperature increased from 298 to 383 K, all types of aSN fibrils heat-denatured to monomers from approximately 343 K. Decreasing temperature from 298 to 273 K caused cold denaturation of fibrils to monomers. Intriguingly, the stability of aSN fibrils depended on temperature for preparing fibrils. aSN fibrils generated at higher temperature showed higher stability at high and low temperature as well as slower denaturation kinetics than fibrils formed at lower temperature. Taken together, the stability of aSN amyloid fibrils depended on growing temperature of fibrils which produced differences in higher order structures of amyloid fibrils.
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