Formation of microdomains in cell membranes investigated by microscopic analyses of structures of membranes and proteins
Project/Area Number |
21590037
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Physical pharmacy
|
Research Institution | Tohoku University |
Principal Investigator |
MIURA Takashi 東北大学, 大学院・薬学研究科, 准教授 (30222318)
|
Project Period (FY) |
2009 – 2011
|
Project Status |
Completed (Fiscal Year 2011)
|
Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2011: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2010: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2009: ¥2,860,000 (Direct Cost: ¥2,200,000、Indirect Cost: ¥660,000)
|
Keywords | 構造生物学 / 脂質膜 / 脂質ラフト / 細胞膜 / 神経変性疾患 / ラマン分光法 / 膜ドメイン |
Research Abstract |
The monomeric amyloid・peptide (A ・・ binds to the phosphatidylcholine membrane in the lamellar gel phase but not in the liquid crystalline phase. Tightly packed phosphatidylcholine membranes appear to serve as a platform for non-electrostatic binding and self-association of A・. On the other hand, aggregated A・peptides bind to the phosphatidylcholine membrane both in the lamellar gel and the liquid crystalline phases. The binding of aggregated A・significantly reduces fluidity of the membrane in the liquid crystalline phase.
|
Report
(4 results)
Research Products
(22 results)