生物有機金属化学におけるペプチド共役分子の不斉構造制御

Abstract

Ferrocene–peptide bioconjugates and urea–peptide bioconjugates are designed to induce chirality–organized structures in both solid and solution states. The ferrocene organometallic scaffold is found to serve as a reliable central reverse–turn unit for the construction of protein secondary structures via intramolecular hydrogen bonding, wherein the attached dipeptide strands are regulated in the appropriate dimensions. The configuration and sequence of the amino acids play an important role in the construction of the chirality–organized bio–inspired systems under controlled hydrogen bonding. Another noteworthy feature of ferrocene–peptide bioconjugates is their strong tendency to self–assemble through contribution of available hydrogen bonding donors in a solid state. Also, the complexation of ferrocene–peptide bioconjugates with palladium (II) compounds is demonstrated not only to stabilize the chirality conformational regulation but also to induce conformational regulation of the dipeptide chain through complexation and chirality organization based on intramolecular hydrogen bonding. Introduction of two dipeptide chains bearing the C–terminal pyridyl moiety (–L–Ala–L–Pro–NH–2–Py) into the urea scaffold is performed to form a hydrogen–bonded duplex, wherein a shuttle–like molecular dynamics based on recombination of the hydrogen bonds is observed in a solution state.