在有机溶剂中对封闭肽Z-Cys-Ala-Pro-His-OMe的Cd(II)配合物进行的1H、13C和113Cd核磁共振研究。
1H-, 13C-, and 113Cd-NMR study of the Cd(II) complex of a blocked peptide, Z-Cys-Ala-Pro-His-OMe, in organic solvents.
作者信息
Zaima H, Ueyama N, Adachi H, Nakamura A
机构信息
Department of Macromolecular Science, Faculty of Science, Osaka University, Japan.
出版信息
Biopolymers. 1995 Mar;35(3):319-29. doi: 10.1002/bip.360350307.
The Cd(II) complex of a peptide, Z-Cys-Ala-Pro-His-OMe was prepared and characterized by absorption, CD, 1H-, 13C-, and 113Cd-nmr, and nuclear Overhauser effect spectroscopy (NOESY) spectra to show the coordination of cysteine thiolate and histidine imizazole to Cd(II) ion. The NOESY spectra in dimethyl formamide showed that the cysteine residue was in proximity to the histidine residue. These results reveal the chelation of Z-Cys-Ala-Pro-His-OMe to Cd(II) ion in solution. Temperature-dependent dissociation equilibrium of histidine imidazole in solution was observed in this complex. Structural features of the chelating peptide are discussed.
制备了肽Z-Cys-Ala-Pro-His-OMe的Cd(II)配合物，并通过吸收光谱、圆二色光谱、1H-、13C-和113Cd-核磁共振以及核Overhauser效应光谱(NOESY)进行表征，以显示半胱氨酸硫醇盐和组氨酸咪唑与Cd(II)离子的配位情况。在二甲基甲酰胺中的NOESY光谱表明，半胱氨酸残基与组氨酸残基相邻。这些结果揭示了Z-Cys-Ala-Pro-His-OMe在溶液中与Cd(II)离子的螯合作用。在该配合物中观察到溶液中组氨酸咪唑的温度依赖性解离平衡。讨论了螯合肽的结构特征。
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