Abstract
A cyclic oligopeptide, linear sequential polypeptides, and glycopeptides were synthesized and their activities in lipid assemblies were investigated in relation to conformational properties. First, a cyclic octapeptide, cyclo(D-Leu-L-Pro)4, transported efficiently Ba2+ across CHCl3 membrane. It transported calcium picrate across a liposomal membrane, which was evidenced by the fluorescence of chlorotetracyclin dissolved in the interior of the liposome. Secondly, sequential peptides, Boc-(Leu-Leu-D-Phe-Pro)n-OBzl (n=3 and 4), and a sequential polymer, poly(Leu-Lue-D-Phe-Pro) took 310 helix conformation in nonpolar organic solvent, and the polymer yielded an electric current under an electric field, when it was added to bilayer lipid membrane (BLM) composed of oxidized cholesterol. This result indicates the formation of pores on the BLM through which ions permeate. The pores were possibly formed by folding and intramolecular association of the sequential polymer with 310 helix conformation in BLM. Thirdly, a linear dipeptide Boc-Asp-ε-Lys-OMe was prepared, in which the α-amino group of the Lys unit was protected with pyrene butyryl group as a fluorecent probe and the β-carboxyl group of Asp unit was linked by an amide bond to 1-β-amino-acetylglucosamine which interacts specifically with a lectin, wheat germ agglutinin (WGA). Liposomes containing the glycodipeptide were as-sociated by the addition of WGA. The association did not occur by the addition of unspecific lectin, phytohemagglutinin. The fluidity of liposome decreased on adding the glycodipeptide, but was restored by the further addition of WGA. Similar phenomena were observed when Ca2+ was added to liposomes containing a dipeptide without the sugar group.
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Imanishi, Y. Polypeptides as Models for Membrane-Active Proteins. Polym J 17, 167–178 (1985). https://doi.org/10.1295/polymj.17.167
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DOI: https://doi.org/10.1295/polymj.17.167