Departmental Bulletin Paper 分子医療に向けた安定で特異的なコイルドコイル構造形成(学内特別研究および国外研修)--(学内特別研究費報告書)

佐野, 健一  ,  Ken-Ichi, Sano

In the previous study, the artificial cationic coiled-coil protein, CCPC 140, was designed to have the structural frame of human skeletal muscle α-tropomyosin. This CCPC 140 showed superior cell-penetrating activity. Looking at thermal melting profiles of circular dichroism, although all the amino acid residues at the coiled-coil intramolecular interface in heptad repeat were conserved, the Tm of CCPC 140 was much higher than that of α-tropomyosin. This indicates that the residues at outer surface of coiled-coil motif can be a determinant of structure stability. In this study, I explored a novel mechanism for structure stabilization on coiled-coil proteins.

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