The mechanism of amyloid fibril formation induced by D-amino acids
| Project/Area Number |
21590080
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (C)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 一般 |
|---|
| Research Field |
Biological pharmacy
|
|---|
| Research Institution | Musashino University |
|---|
Principal Investigator |
TATE Naoko 武蔵野大学, 薬学研究所, 教授 (00201955)
|
|---|
| Project Period (FY) |
2009 – 2011
|
| Project Status |
Completed (Fiscal Year 2011)
|
| Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2011: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2010: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2009: ¥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ペプチド / 線維化 / 凝集 / D-アミノ酸 / アミロイドβペプチド(Aβ) / Aβフラグメント / アミロイドβペブチド / 老人斑 / 老年性脳疾患 / 構造 / 物性 / 神経細胞毒性 |
|---|
| 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.
|
Report
(4 results)
Research Products
(22 results)
-
-
-
[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
-
Journal Title
Nanotechnology
Volume: 22
Pages: 1-8
Related Report
Peer Reviewed
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
