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Computer simulation and structure analysis of polypeptide derivatives of cyclotriphosphazene

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Abstract

A quantum-chemical analysis and experimental investigation of the structure of poly(γ-methyl L-α-glutamate) and poly(γ-benzyl L-α-glutamate) linked with the triphosphazene ring via aminophenoxy groups were performed. The computer simulation showed that these compounds with a total degree of polymerization of amino acid sequences of n ≤ 60 are close to the rigid-rod conformation in struture, whereas the rod is distorted to the arch architecture at n > 60. According to X-ray data, the α helices of polypeptide segments are arranged into two-dimensional hexagonal packing. By means of the DSC technique, the glass transition associated with the freezing-out of the mobility of side chains was revealed, transitions to the mesophase were determined, and it was established that the helix type experiences a local change characteristic of poly(γ-benzyl glutamate) derivatives of cyclotriphosphazene in the solid state.

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Original Russian Text © M.A. Vantsyan, M.F. Bobrov, G.V. Popova, V.V. Kireev, V.G. Tzirel’son, 2007, published in Vysokomolekulyarnye Soedineniya, Ser. A, 2007, Vol. 49, No. 3, pp. 533–541.

This work was supported by the Russian Foundation for Basic Research, project no. 03-03-33157, and the Ministry of Education and Science of the Russian Federation, project no. 2.1.1.5051.

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Vantsyan, M.A., Bobrov, M.F., Popova, G.V. et al. Computer simulation and structure analysis of polypeptide derivatives of cyclotriphosphazene. Polym. Sci. Ser. A 49, 355–362 (2007). https://doi.org/10.1134/S0965545X07030170

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  • DOI: https://doi.org/10.1134/S0965545X07030170

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