2011 Fiscal Year Final Research Report
The mechanism of amyloid fibril formation induced by D-amino acids
| Project/Area Number |
21590080
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Biological pharmacy
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| Research Institution | Musashino University |
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Principal Investigator |
TATE Naoko 武蔵野大学, 薬学研究所, 教授 (00201955)
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| Project Period (FY) |
2009 – 2011
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| Keywords | アルツハイマー病 / アミロイドβペプチド / 線維化 / 凝集 / D-アミノ酸 |
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| Research Abstract |
Amyloid β proteins(Aβ) extracted from the amyloid cores of neutritic plaques are considerably isomerized at their Asp residues. To asseses the impact of D-Asp on Aβ conformation. and on initiation of amyloid fibril formation, I used wild type Aβ and D-Asp-containing Aβ which D-Asp. was substituted for L-Asp at residues 1, 7, 23. Amyloid fibril formation was enhanced by D-Asp23. Moreover, I demonstrated that D-Asp containing Aβ showed no effect on fibril formation of wild-type Aβ. Lastly, I showed that A. fragment 1-23 promoted formation of fibrils and aggregates of wild-type Aβ.
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Research Products
(10 results)
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[Journal Article] Controlled structure and properties of silicate nanoparticle networks for incorporation of biosystem components2011
Author(s)
Sakai-Kato, K., Hasegawa, T., Takaoka, A., Kato, M, Toyo'oka, T., Utsunomiya-Tate, N. and Kawanishi, T
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Journal Title
Nanotechnology
Volume: 22
Pages: 1-8
Peer Reviewed
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