| Project/Area Number |
03452305
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
生物物性学
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| Research Institution | KYOTO UNIVERSITY |
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Principal Investigator |
TAKAHASHI Sho Kyoto University Inst. Chem. Res. Professor, 化学研究所, 教授 (20022593)
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| Project Period (FY) |
1991 – 1992
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| Project Status |
Completed (Fiscal Year 1992)
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| Budget Amount *help |
¥400,000 (Direct Cost: ¥400,000)
Fiscal Year 1992: ¥400,000 (Direct Cost: ¥400,000)
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| Keywords | Membrane fusion / Lipid bilayers / FTIR / ATR / alpha-Helix / Amphipathic helix / Spectroscopy / Synthetic peptide / ペプチド / リン脂質膜 / 分子配向 / 二次構造 / αーヘリックス |
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| Research Abstract |
Membrane fusion is a general biological process and governs the processes fundamental to cellular functions, such as cell-to-cell busion and intracellular vesicle or organelle fusion. Although specific proteins concern every instance of cellular membrane fusion, elementary process of membrane fusion itself can be induced by specific peptides which have amino acid sequences identical or closely related to the parts of those proteins. Those peptides are amphiphilic and strongly interact with lipid membranes. In this study: (1) membrane fusion activity and profiles of 20-aminoacid residues synthetic peptides which had modified amino acid sequences of influenza virus hem-agglutinin were established; (2) interaction of these membrane fusion-active peptides with lipid membranes to form an alpha-helical conformation was confirmed; and (3) from FTIR studies it was concluded that peptide alpha-helices oriented in lipid bilayers nearly parallel to the membrane plane.
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