Development of in vitro amyloid fibril formation systems that mimic the physiological fibrillogenesis conditions in vivo
Project/Area Number |
24570129
|
Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Structural biochemistry
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Research Institution | University of Fukui |
Principal Investigator |
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Co-Investigator(Kenkyū-buntansha) |
NAIKI Hironobu 福井大学, 医学部, 教授 (10227704)
|
Project Period (FY) |
2012-04-01 – 2015-03-31
|
Project Status |
Completed (Fiscal Year 2014)
|
Budget Amount *help |
¥5,590,000 (Direct Cost: ¥4,300,000、Indirect Cost: ¥1,290,000)
Fiscal Year 2014: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2013: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2012: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
|
Keywords | 蛋白質 / 脳神経疾患 / 病理学 / アミロイド / アルツハイマー病 |
Outline of Final Research Achievements |
We constructed several amyloid fibril formation systems in vitro to evaluate the roles of the various biological molecules or reaction conditions in the amyloid fibril formation. The key findings of this study are as follows: (1) We developed a near-physiological Alzheimer's disease amyloid β-peptide (Aβ) fibril formation system for evaluating the efficiency of protein components to induce the nucleation of Aβ-peptide. To suppress spontaneous Aβ nucleation, the system includes protein coated Sepharose beads and low concentration of Aβ peptide solution without air in the reaction vessel. Using the system, we indicated several basement membrane components accelerate Aβ fibril formation in vitro. (2) To further decrease the concentration of Aβ peptide in the reaction, we are developing an open flow system, where near physiological concentrations of Aβ peptide are continuously supplied to the reaction surface.
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Report
(4 results)
Research Products
(11 results)