The elucidation of Abeta aggregation mechanism using high-speed atomic force microscopy
Project/Area Number |
26461266
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Neurology
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Research Institution | Showa University (2015-2016) Kanazawa University (2014) |
Principal Investigator |
Ono Kenjiro 昭和大学, 医学部, 教授 (70377381)
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Co-Investigator(Renkei-kenkyūsha) |
YAMADA Masahito 金沢大学, 医学系, 教授 (80191336)
NAKAYAMA Takahiro 金沢大学, バイオAFM先端研究センター, 助教 (00532821)
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Project Period (FY) |
2014-04-01 – 2017-03-31
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Project Status |
Completed (Fiscal Year 2016)
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Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2016: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2014: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
|
Keywords | アルツハイマー病 / アミロイドβ蛋白 / 高速原子間力顕微鏡 |
Outline of Final Research Achievements |
Aggregation of amyloid β-protein (Aβ) into insoluble amyloid fibrils is implicated in Alzheimer's disease (AD). The elucidation of the structural features and assembly kinetics of Aβ has been an area of intense study. We performed high-speed atomic force microscopy (HS-AFM) studies of fibril formation and elongation by Aβ1-42. Our data demonstrate two different growth modes of Aβ1-42, one producing straight fibrils and the other producing spiral fibrils. Each mode depends on initial fibril nucleus structure, but switching from one growth mode to another was occasionally observed, suggesting that fibril end structure fluctuated between the two growth modes. This switching phenomenon was affected by buffer salt composition. Our findings indicate that polymorphism in fibril structure can occur after fibril nucleation and is affected by relatively modest changes in environmental conditions.
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Report
(4 results)
Research Products
(73 results)
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[Journal Article] Improvement in language function correlates with gait improvement in drug-naïve Parkinson’s disease patients taking dopaminergic medication.2016
Author(s)
Murakami H., Momma Y., Nohara T., Mori Y., Futamura A., Sugita T., Ishigaki S., Katoh H., Kezuka M., Ono K., Miller M.W., Kawamura M.
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Journal Title
Journal of Parkinson's Disease
Volume: 6
Issue: 1
Pages: 209-217
DOI
Related Report
Peer Reviewed / Open Access
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[Journal Article] Role of intestinal microbiota in the generation of polyphenol derived phenolic acid mediated attenuation of Alzheimer’s disease β-amyloid oligomerization.2015
Author(s)
Wang D., Ho L., Faith J., Ono K., Janle E.M., Lachcik P.J., Cooper B.R., Jannasch A.H., D’Arcy B.R., Williams B.A., Ferruzzi M.G., Levine S., Zhao W., Dubner L., Pasinetti G.M.
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Journal Title
Molecular Nutrition & Food Research
Volume: 59
Issue: 6
Pages: 1025-1040
DOI
Related Report
Peer Reviewed / Int'l Joint Research
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[Journal Article] Molecular topology as novel strategy for discovery of drugs with Aβ lowering and anti-aggregation dual activities for Alzheimer's disease2014
Author(s)
Wang J, Land D, Ono K, Galvez J, Zhao W, Vempati P, Steele JW, Cheng A, Yamada M, Levine S, Mazzola P, Pasinetti GM
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Journal Title
PLoS One
Volume: 9
Issue: 3
Pages: e92750-e92750
DOI
Related Report
Peer Reviewed / Open Access
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[Journal Article] Efficacy of diflunisal on autonomic dysfunction of late-onset familial amyloid polyneuropathy (TTR Val30Met) in a Japanese endemic area2014
Author(s)
Takahashi R, Ono K, Shibata S, Nakamura K, Komatsu J, Ikeda Y, Ikeda T, Samuraki M, Sakai K, Iwasa K, Kayano D, Yamada M
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Journal Title
J Neurol Sci
Volume: 345
Issue: 1-2
Pages: 231-235
DOI
Related Report
Peer Reviewed
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[Presentation] Aβ凝集過程と阻害薬開発2016
Author(s)
小野賢二郎
Organizer
第4回日本アミロイドーシス研究会学術集会
Place of Presentation
KKRホテル東京(東京)
Year and Date
2016-08-19
Related Report
Invited
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