Structural and NMR investigations of the ternary adducts of twenty α-amino acids and selected dipeptides with a chiral, diaqua–ytterbium complex
作者:Rachel S. Dickins、Andrei S. Batsanov、Judith A. K. Howard、David Parker、Horst Puschmann、Stefania Salamano
DOI:10.1039/b311791j
日期:——
A detailed investigation of the nature of the binding of each of the 20 common α-amino acids and various selected dipeptides to a chiral, diaqua–ytterbium complex in aqueous solution has been carried out. Analysis of the dipolar 1H NMR paramagnetic shifts suggests that the α-amino acids form a common chelated structure within a nine-coordinate mono-capped square antiprismatic coordination environment
详细研究20种常见α-氨基酸与各种选择的氨基酸的结合性质 二肽在水溶液中制备了手性的dia- complex配合物。对偶极1 H NMR顺磁位移的分析表明,α-氨基酸在九坐标单峰方形反棱柱配位环境中形成了常见的螯合结构,胺N轴向布置。九种螯合YbL 1 –的晶体结构氨基酸 加合物(Gly,Ala,Ser, 苏氨酸,遇到了)确认这一点。三元配合物二肽(例如 甘氨酸, 甘氨酸, 甘氨酸, 甘氨酸, 甘氨酸, 甘氨酸, 蛋氨酸, 天冬氨酸, 他的甘氨酸)也偏爱航站楼 胺如轴向供体与邻近的酰胺基结合,生成五环螯合物。仅在N末端Asp的情况下才发现通过侧链功能螯合的证据。关于upon离子的手性环境氨基酸 还使用近红外探测了结合 圆二色光谱。