| Project/Area Number |
01470104
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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 |
高分子物性
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| Research Institution | Nagoya Institute of Technology |
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Principal Investigator |
TAKIZAWA Akira Nagoya Institute of Technology, Faculty of Engineering, Department of Materials Science & Engineering, Professor, 工学部, 教授 (90016262)
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| Co-Investigator(Kenkyū-buntansha) |
KINOSHITA Takatoshi Nagoya Institute of Technology, Faculty of Engineering, Department of Materials, 工学部, 講師 (60135407)
TSUJITA Yoshiharu Nagoya Institute of Technology, Faculty of Engineering, Department of Materials, 工学部, 教授 (70016591)
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| Project Period (FY) |
1989 – 1990
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| Project Status |
Completed (Fiscal Year 1990)
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| Budget Amount *help |
¥6,100,000 (Direct Cost: ¥6,100,000)
Fiscal Year 1990: ¥4,000,000 (Direct Cost: ¥4,000,000)
Fiscal Year 1989: ¥2,100,000 (Direct Cost: ¥2,100,000)
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| Keywords | Poly (alky1 L-glutamate) / Monolayer Method / hydrolysis / Sequential Polypeptide / Amphiphilic / Micelle / Ion Channel / Artificial Model of Cell Membrane / 構造形成 / 電子顕微鏡 / ポリ(γ-メチルLグルタメ-ト) / 単分子膜 / 両親媒性シ-クエンシャルポリアミノ酸 / 二分子膜系 / リポソ-ム複合体 / 会合体 / ミサイルドラッグ |
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| Research Abstract |
Amphiphilic sequential polypeptides whose alpha-helix is hydrophilic on one face and hydrophobic on the opposite face were prepared by a novel and simple technique by using a polypeptide monolayer saponification method. This method involves the formation of a solid condensed monolayer of poly (ganma-methy1 L-glutamate)(PMG), poly (n-hexy1 L-glutamate)(PHeLG) and poly (N^<epsilon>-trifluoroacethy1 L-lysine)(PLys (Tfa)), respectively, at an air-water interface, and a saponification of the polypeptides side chains hydrated in the aqueous phase, keeping the remaining side chains oriented away from the aqueous phase unreacted. The resulting polypeptides, PMG with 34mol% L-glutamic residues, PHeLG with 27mol% L-glutamic acid and PLys (Tfa) with 34mol% L-lysine residues, had the unique amino acid sequence to form an amphiphilic alpha-helix structure. Moreover, the content of L-glutamic acid residue of PMG could be regulated by intruducing dimethylformamide into the aqueous phase at the monolayer saponification reaction. The polypeptides obtained formed a reversed micelle in aqueous solution, on the other hand, in the lipid bilayer membrane the polypeptides formed the cylindrical aggregate consisting of 6 trans-membrane helix rods act as an ion channel through the bilayer membrane.
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