| Project/Area Number |
58430016
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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 |
Synthetic chemistry
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| Research Institution | Kyushu University |
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Principal Investigator |
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| Project Period (FY) |
1983 – 1985
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| Project Status |
Completed (Fiscal Year 1985)
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| Budget Amount *help |
¥32,100,000 (Direct Cost: ¥32,100,000)
Fiscal Year 1985: ¥3,100,000 (Direct Cost: ¥3,100,000)
Fiscal Year 1984: ¥3,500,000 (Direct Cost: ¥3,500,000)
Fiscal Year 1983: ¥25,500,000 (Direct Cost: ¥25,500,000)
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| Keywords | Bilayer Membrane / Stereospecific / Organic Reaction / Peptide Lipid / Nonbilayer Structure / Vitamin B6 / Vitamin B12 / アミノ基転移反応 |
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| Research Abstract |
1. Aggregate Morphology of Synthetic Peptide Lipids. -- Peptide lipids, which can form chemically and morphologically stable single-walled vesicles in aqueous media, were desinged by incorporation of amino acid residues as their structural components. Those peptide lipids having cationic, anionic, and nonionic head moieties were successfully prepared, and their morphological behavior in aqueous media was examined. In particular, nonbilayer aggregates, cubic and hexagonal phases, were constructed for the first time with these synthetic lipids.
2. Fusion Behavior of Single-Walled Vesicles. -- Sintle-walled vesicles formed with equimolar mixtures of nonionic and anionic peptide lipids underwent fusion by adjusting pH or temperature via formation of nonbilayer aggregates. Single-walled vesicles having ionic head moieties underwent fusion instantaneously upon addition of ionic polymers having the opposite charges.
3. Functional Model of Vitamin <B_6> -dependent Enzyme. -- A holoenzyme model formed with single-walled vesicles of the peptide lipid and a hydrophobic vitamin <B_6> catalyzed the transamination reaction between an amino acid and a keto acid with turnover behavior. Here, an artificial transaminase was obtained for the first time.
4. Functional Model of Vitamin <B_(12)> -dependent Enzyme. -- A holoenzyme model formed with single-walled vesicles of the peptide lipid and a hydrophobic vitamin <B_(12)> catalyzed the carbon-skeletal rearrangement in a manner as observed with methylmalonyl-CoA mutase.
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