| Project/Area Number |
15K21680
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Biophysics
Functional biochemistry
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| Research Institution | Okazaki Research Facilities, National Institutes of Natural Sciences |
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Principal Investigator |
YAGI Maho 大学共同利用機関法人自然科学研究機構(岡崎共通研究施設), 岡崎統合バイオサイエンスセンター, 助教 (40608999)
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| Project Period (FY) |
2015-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2016: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2015: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
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| Keywords | アミロイドβ / ガングリオシド / 固体NMR / 糖脂質 / アルツハイマー病 / アミロイド / 脂質膜 |
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| Outline of Final Research Achievements |
In this study, solid-state nuclear magnetic resonance spectroscopy has elucidated the membrane-induced conformation of amyloid (Aβ), in which the disordered N-terminal segment is followed by the stable C-terminal β strand. The data obtained in this project provides insights into the molecular processes of the conformational transition of Aβ coupled with its assembly into parallel β structures.
Structural and kinetic analyses of the Flemish-type mutant (A21G) of Aβ(1-40) peptide were also performed in comparison with the wild type to examine the possible effects of the A21G mutation on the conformation of the Aβ(1-40) isoform. These findings suggest that the mutational perturbation to the membrane binding properties is coupled with the changes in nucleation behavior of Aβ during its fibril formation.
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