Project/Area Number |
01580262
|
Research Category |
Grant-in-Aid for General Scientific Research (C)
|
Allocation Type | Single-year Grants |
Research Field |
生物物性学
|
Research Institution | Nagoya University |
Principal Investigator |
OHKI Kazuo Nagoya University Associate Professor Faculty of Engineering, 工学部, 助教授 (80115394)
|
Co-Investigator(Kenkyū-buntansha) |
松岡 審爾 名古屋大学, 工学部, 助手 (90190420)
|
Project Period (FY) |
1989 – 1991
|
Project Status |
Completed (Fiscal Year 1991)
|
Budget Amount *help |
¥2,500,000 (Direct Cost: ¥2,500,000)
Fiscal Year 1991: ¥300,000 (Direct Cost: ¥300,000)
Fiscal Year 1990: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1989: ¥1,500,000 (Direct Cost: ¥1,500,000)
|
Keywords | inositol phospholipid / phosphatidic acid / calcium ion / Structure of biomembrane / lipid-protein interaction / signal transduction / physical property of membrane / phase separation / 静電相互作用 / 疎水相互作用 |
Research Abstract |
Phosphatidic acids play an important role in cellular function ; for example, proliferation of a cell, signal transduction on plasma membranes and mobilization of calcium ions. In the present study, interactions of phosphatidic acid with poly (L-lysine) and calcium ions were investigated by differential scanning calorimetry and X-ray diffraction technique. Results on phosphatidic acid/poly (L-lysine) system indicate that poly (L-lysine) interacts with phosphatidic acid electrostatically without affecting the chain-packing of the lipid bilayer membranes and that the interaction does not obey the one-to-one sto ichiometry. Further analysis of X-ray diffraction data gives a probable model of phosphatidic acid/poly (L-lysine) membranes. Calorimetric study on phosphatidic acid/ (phosphatidylcholine and/or phosphatidylethanolamine) /Ca2+ system elucidates a fine structure of membranes composed of the mixed phospholipids. In these membranes, phosphatidic acid is not completely segregated by Ca2+ but studded in the membranes. The present study is helpful to proceed a research of relationship between membrane structure and function.
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