2014 Fiscal Year Final Research Report
Role of supersaturation in the formation of amyloid fibrils
Project/Area Number |
24370067
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Research Category |
Grant-in-Aid for Scientific Research (B)
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Allocation Type | Partial Multi-year Fund |
Section | 一般 |
Research Field |
Biophysics
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Research Institution | Osaka University |
Principal Investigator |
GOTO Yuji 大阪大学, たんぱく質研究所, 教授 (40153770)
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Co-Investigator(Kenkyū-buntansha) |
YAGI Hisashi 鳥取大学, 工学部, 助教 (10432494)
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Co-Investigator(Renkei-kenkyūsha) |
SAKURAI Kazumasa 近畿大学, 先端科学研究所, 講師 (10403015)
KAJI Yuichi 筑波大学, 人間総合科学研究科, 准教授 (50361332)
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Project Period (FY) |
2012-04-01 – 2015-03-31
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Keywords | 蛋白質 / フォールディング / アミロイド線維 / 凝集 / 超音波 / β2ミクログロブリン / アミロイドβペプチド / αシヌクレイン |
Outline of Final Research Achievements |
Amyloid fibrils are fibrillar aggregates of denatured proteins associated with various amyloidoses. Amyloid fibrils form in the supersaturated solutions of precursor proteins through a nucleation and growth mechanism. We revisited "supersaturation" and studied its role in amyloid fibrillation. We showed that ultrasonication is one of the most effective agitations to force spontaneous fibrillation and constructed a HANdai Amyloid Burst Inducer (HANABI), which combines the use of a water-bath-type ultrasonicator and microplate reader. HANABI makes possible a high-throughput analysis of amyloid fibrillation. On the other hand, the term amorphous aggregate has been collectively used for other types of aggregates, which have not been the targets of intensive research. We showed that amyloid fibrils and amorphous aggregates were similar to the crystals and glasses of substances, respectively, explaining comprehensively the kinetics and thermodynamics of protein aggregation.
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Free Research Field |
蛋白質科学
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