| Project/Area Number |
21370044
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Structural biochemistry
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| Research Institution | Osaka University |
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Principal Investigator |
GOTO Yuji) 大阪大学, 蛋白質研究所, 教授 (40153770)
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| Co-Investigator(Kenkyū-buntansha) |
SAKURAI Kazumasa 大阪大学, 蛋白質研究所, 助教 (10403015)
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| Co-Investigator(Renkei-kenkyūsha) |
FUJIWARA Toshimichi 大阪大学, 蛋白質研究所, 教授 (20242381)
CHATANI Eri 神戸大学, 大学院・理学研究科, 准教授 (00432493)
NAIKI Hironobu 福井大学, 医学部, 教授 (10227704)
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| Project Period (FY) |
2009 – 2011
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| Project Status |
Completed (Fiscal Year 2011)
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| Budget Amount *help |
¥18,200,000 (Direct Cost: ¥14,000,000、Indirect Cost: ¥4,200,000)
Fiscal Year 2011: ¥3,250,000 (Direct Cost: ¥2,500,000、Indirect Cost: ¥750,000)
Fiscal Year 2010: ¥6,890,000 (Direct Cost: ¥5,300,000、Indirect Cost: ¥1,590,000)
Fiscal Year 2009: ¥8,060,000 (Direct Cost: ¥6,200,000、Indirect Cost: ¥1,860,000)
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| Keywords | 変性とフォールディング / アミロイド線維 / 蛋白質の凝集 / 蛍光顕微鏡 / 超音波 / アミロイド蛋白質 / 脳神経疾患 / 透析アミロイドーシス / アルツハイマー病 / 糖尿病 / NMR |
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| Research Abstract |
We studied the mechanism of amyloid fibrillation with a unique technique in which total internal reflection fluorescence microscopy is combined with amyloid-specific ThT. To gain insights into the possible kinetic intermediates, we performed hydrogen/ deuterium exchange of amide protons during fibril elongation. Combining the use of ultrasonication and a microplate reader, we propose an efficient approach to studying the potential of proteins to form amyloid fibrils. Taken all results together, we propose that the amyloid fibrils formed via a nucleation-dependent mechanism in a supersaturated solution, analogous to crystallization.
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