Interaction of .ALPHA.-helical glycopeptides with lipid bilayer membrane.
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概要
- 論文の詳細を見る
α-Helical polypeptides having a glyco moiety at one end and a fluorescent probe at the other were prepared and investigated on the interaction with a lipid bilayer membrane. A glycopeptide composed of poly(alanine) and maltose was incorporated into the lipid membrane with the glyco moiety exposed to the aqueous phase and the peptide chain buried in membrane above the phase-transition temperature of the lipid membrane. However, below the phase-transition temperature, the glycopeptide induced the aggregation of dimyristoylphosphatidylcholine (DMPC) small unilamellar vesicles (SUV). Another glycopeptide composed of poly(γ-benzyl glutamate) and glucose also induced the aggregation of DMPC SUV, indicating that such the hydrophobic peptide tends to disturb the membrane structure significantly upon binding. The arrangement of the glycopeptide in a membrane was investigated by using a fluorescent probe connected to the end of the peptide chain. The terminal region of the peptide chain was located at the hydrophobic core of lipid membrane. However, the glycopeptide composed of 25 Ala residues had a smaller fraction taking perpendicular orientation to the membrane than that composed of 15 Ala residues. It was therefore considered that a part of the former glycopeptide molecules exits on the membrane surface, forming aggregates.
- 公益社団法人 日本化学会の論文
著者
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Kimura Shunsaku
Department Of Material Chemistry Graduate School Of Engineering Kyoto University
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Imanishi Yukio
Department Of Material Chemistry Graduate School Of Engineering Kyoto Univeresity
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IMANISHI Yukio
Department of Polymer Chemistry, Kyoto University
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Otoda Kazuya
Department of Polymer Chemistry, Kyoto University
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