具抗凝血作用的三种钕配合物与人血清白蛋白的相互作用

采用荧光光谱法,紫外光谱法以及圆二色谱法研究了具抗凝血作用的水杨酸钕((NdL′3.2H2O,L′=水杨酸离子))、华法灵钕(NdL3.2H2O,L=华法灵离子)和华法灵水杨酸钕(NdL2L′.2H2O)3种配合物与人血清白蛋白的相互作用。结果表明:配合物对人血清白蛋白(HSA)的荧光产生猝灭现象;配合物的存在使得HSA紫外吸收光谱的强度增加;配合物的存在也对HSA的构象产生影响。水杨酸钕的猝灭方式为动态与静态猝灭,而华法灵钕和华法灵水杨酸钕的猝灭方式属于两者之间生成了不发荧光的复合物而导致的静态猝灭。并分别确定了它们的结合力类型:华法灵钕与HSA之间主要作用力是静电作用力;水杨酸钕与HSA之间主要作用力为典型的疏水作用力;华法灵水杨酸钕与HSA之间为氢键和范德华力。计算了配合物与人血清白蛋白的结合常数K和结合位点数n。

Interaction of the Complexes with Anticoagulant Property of Neodymium with Human Serum Albumin

For investigation the mechanism of the anticoagulant of the complexes of warfarin neodymium, salicylic neodymium and warfarin salicylate neodymium, fluorescence, UV spectroscopy and circular dichroism methods were used to study the interaction between human serum albumin (HSA) and neodymium complexes. It was observed that these complexes of neodymium could reduce the fluorescence intensity of human serum albumin. The way of fluorescence quenching was discussed according to the Stern-Volmer equation. The way of fluorescence quenching was static quenching for warfarin neodymium and warfarin salicylate neodymium complexes. The quenching of salicylic neodymium contains dynamic quenching and static quenching. The style of action of human serum albumin with complexes was gained according to the thermodynamic functions at different temperatures. The main forces between warfarin neodymium and HSA is the electrostatic force; the main force between salicylate neodymium and HAS is typical hydrophobic force; The main force between warfarin salicylate neodymium and HSA is hydrogen bonding and Vander Waals forces. The binding constant K and the binding sites n of complexes with HSA were gained according to the changes of fluorescence intensity of human serum albumin in the complexes presence and absence. And found this complexes have obviously changed the conformation of HSA. The possible reason for which the complexes makes human serum albumin conformational changes is discussed.