| Project/Area Number |
05402068
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| Research Category |
Grant-in-Aid for General Scientific Research (A)
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| Allocation Type | Single-year Grants |
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| Research Field |
Biophysics
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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) |
1993 – 1994
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| Project Status |
Completed (Fiscal Year 1994)
|
| Budget Amount *help |
¥31,000,000 (Direct Cost: ¥31,000,000)
Fiscal Year 1994: ¥2,600,000 (Direct Cost: ¥2,600,000)
Fiscal Year 1993: ¥28,400,000 (Direct Cost: ¥28,400,000)
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| Keywords | Membrane fusion / Lipid membranes / Artificial liposome / Synthetic peptide / Amino acid sequence / Amphiphilic peptide / Secondary structure / ペプチド立体構造 |
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| Research Abstract |
A synthetic 20-residue peptide which represents the amino terminal sequence of influenza hemagglutinin HA2 has been known to have the ability to induce fusion of liposome. Although some of peptides having a similar amino acid sequence also could cause liposome fusion, nevertheless, not all the peptides of similar sequences necessarily approve the fusion. There must be some critical sequences for fusion activity. In this study, we synthesized many peptides and determined fusion competence of the peptides, in order to reveal what amino acid sequence and structure were necessary for the activity. Each peptide had one substitution per peptide to another amino acid from the standard sequence, under the condition that the amphiphilicity of a peptide was maintained. As a result, some critical residues were identified as to be responsible for the fusion activity. We will conclude that a distribution of side chain bulkiness or helix stability along the peptide strongly affected the fusion activity of a peptide.
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