Nano-domain formation on membrane fusion during cell division
Project/Area Number |
22740282
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Single-year Grants |
Research Field |
Biophysics/Chemical physics
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Research Institution | High Energy Accelerator Research Organization |
Principal Investigator |
YAMADA Norifumi 大学共同利用機関法人高エネルギー加速器研究機構, 物質構造科学研究所, 助教 (90425603)
|
Project Period (FY) |
2010 – 2012
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Project Status |
Completed (Fiscal Year 2012)
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Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2012: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2011: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2010: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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Keywords | 生物物理 / 脂質 / 自己組織化 / 量子ビーム / 生体模倣膜 / 相分離 / リン脂質 / X線・粒子線 |
Research Abstract |
A phospholipid is a main component of biomembranes, and spontaneously form bilayer structure in water. In this study, the effect of a phosphatidylethanolamine, a phospholipid related with a cell division, was investigated from the viewpoint of molecular shape. For this purpose, the phosphatidylethanolamine was mixed with a normal phospholipid as well as a phospholipid with short hydrocarbon chains which has an opposite molecular shape to phosphatidylethanolamine, and it was found that the membrane fusion was suppressed by the short-chain lipid. Also, the effect of short-chain phospholipid on the membrane structure was investigated, and it was found that the structural transformation caused by the short-chain phospholipid was induced by the phase separation between normal phospholipids and short-chain phospholipid.
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Report
(4 results)
Research Products
(18 results)
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[Journal Article] Design and Performance of Horizontal Type Neutron Reflectometer SOFIA at J-PARC/MLF2011
Author(s)
N.L.Yamada, N.Torikai, K.Mitamura, H.Sagehashi, S.Sato, H.Seto, T.Sugita, S.Goko, M.Furusaka, T.Oda, M.Hino, T.Fujiwara, H.Takahashi, A.Takahara
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Journal Title
Euro.Phys.J.Plus
Volume: 126
Issue: 11
Pages: 108-108
DOI
Related Report
Peer Reviewed
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