| Project/Area Number |
60580124
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
物質生物化学
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| Research Institution | Gunma University |
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Principal Investigator |
KATAKAI Ryoichi College of Technology, Professor, 大学併設短期大学部, 教授 (10008500)
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| Project Period (FY) |
1985 – 1986
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| Project Status |
Completed (Fiscal Year 1986)
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| Budget Amount *help |
¥1,300,000 (Direct Cost: ¥1,300,000)
Fiscal Year 1986: ¥300,000 (Direct Cost: ¥300,000)
Fiscal Year 1985: ¥1,000,000 (Direct Cost: ¥1,000,000)
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| Keywords | Hydrphobic peptides / <alpha> -Helix / Liposomes / 膜厚 |
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| Research Abstract |
This research project has been carried out to find experimental evidences to the predicted transmembrane peptide toporaphy that hydrophobic <alpha> -helical moieties of the membrane proteins are in the membranes. For this purpose, hydrophobic <alpha> -helical oligopeptides soluble in lipophilic solvents suitable for the preparation of liposomes from lecitines Nps- <(Met-Met-Leu)_n> -OEt (n=6-10) were synthesized , and the liposomes consisting of these peptides and egg yolk lecitine and other lecitines were prepared by sonication method. Analyses of the content and conformation of the peptides incorporated into the liposomes showed that the peptides assume the <alpha> -helical conformation in the membranes and that the <alpha> -helical rods having the length comparable to the thickness of the membranes are best incorporated into the membranes. This result supports the predicted transmembrane hydrophobic peptide topography.
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