| Project/Area Number |
25450188
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Food science
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| Research Institution | Kawasaki University of Medical Welfare (2015-2016)
Osaka Aoyama University (2013-2014) |
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Principal Investigator |
OKU Kazuyuki 川崎医療福祉大学, 医療技術学部, 教授 (40549797)
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| Project Period (FY) |
2013-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2015: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2014: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2013: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | トレハロース / 疎水性相互作用 / タンパク質凝集抑制 / βアミロイド / 生体間相互作用解析 / 核磁気共鳴分析ｂ / βアミロイドペプチド / 老化促進モデルマウス / βアミロイドタンパク / 生体間相互作用解析装置 / 核磁気共鳴分析法 / 老化促進マウス（SAM/P1） / 疎水性アミノ酸 / 分子動力学法 / トレハロース誘導体 |
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| Outline of Final Research Achievements |
We proposed a novel mechanism from the viewpoint of hydration characteristics on the protective and stabilizing effect of trehalose on biological constituents. In this study, experimental and theoretical analysis made it clear that trehalose directly interacts with aromatic amino acids. Next, as an inhibitory action on protein aggregation of trehalose, we examined the agglutination reaction of β-amyloid, and it was found that trehalose directly acts with β-amyloid to suppress aggregation of β-amyloid. These results suggest that the hydrophobic group of β-amyloid acts on the hydrophobic pocket of trehalose and suppresses the interaction between the hydrophobic groups, suggesting a new hydration property of trehalose
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