2017 Fiscal Year Final Research Report
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)
|
| Allocation Type | Multi-year Fund |
|---|
| Section | 一般 |
|---|
| Research Field |
Biophysics
|
|---|
| 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
|
| Keywords | アミロイド線維 / フォールディング / 凝集中間体 / 高圧NMR |
|---|
| 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.
|
| Free Research Field |
蛋白質物理化学
|
