Solvothermal Synthesis, Crystal Structure of a 1D Coordination Polymer [Er(CCA)3(H2O)2]n•2nH2O (HCCA＝Coumarin-3-Carboxylic Acid) and the Interaction between the Polymer and Bovine Serum Albumin (BSA)
Yang Shuping*,1 Han Lijun2 Wang Daqi3 Pan Yan4 Yu Zhiqun1 Ye Haiyan1
(1 School of Chemical Engineering, Huaihai Institute of Technology, Lianyungang 222005)
(2 School of Mathematics and Science, Huaihai Institute of Technology, Lianyungang 222005)
(3 School of Chemistry and Chemical Engineering, Liaocheng University, Liaocheng 252059)
(4 State Key Laboratory of Natural and Biomimetic Drugs, Department of Pharmacology, School of Basic Medical Sciences, Peking University and Institute of System Biomedicine, Peking University, Beijing 100191)
Abstract：A coordination polymer [Er(CCA)3(H2O)2]n•2nH2O (HCCA＝coumarin-3-carboxylic acid) has been prepared by solvent-thermal method and characterized by elemental analysis and IR spectra and single crystal X-ray diffraction. The crystal of erbium(III) complex belongs to monoclinic system with space group, P21/c, a＝0.6310(1) nm, b＝1.4165(2) nm, c＝3.1731(3) nm|β＝91.861(2)°, V＝2.8346(7) nm3, Dc＝1.890 g•cm－3, Z＝4, F(000)＝1596, residual factors R1＝0.0525, wR2＝0.0930 [I＞2σ(I)], S＝1.290. The Er(III) atom is eight-coordinated by eight O atoms from three ligands (CCA) and two coordinated water molecules, and the coordination polyhedron around the Er(III) atom can be best described as a distorted dodecahedron geometry. Two adjacent Er(III) atoms were bridged into a one-dimensional polymeric chain by the carboxylic group in a ligand (CCA). The interaction between complex and bovine serum albumin (BSA) was investigated by fluorescence spectroscopy at different temperature. The results indicated that the complex quenches the fluorescence of BSA through a static quenching procedure. The binding constants (Ka) and the number of binding sites (n) between the complex and BSA were calculated at different temperature. The corresponding thermodynamic parameters enthalpy changes (ΔH＞0) and entropy changes (ΔS＞0) were also obtained according to the vant Hoff equation. The primary binding pattern between complex and BSA was interpreted as hydrophobic interaction. The binding average distance r between the donor (BSA) and acceptor (complex) was obtained to be 2.85 nm based on the F?sters theory, which indicates the non-radiation energy transfer can occur from BSA to complex with high probability.
杨树平, 韩立军, 王大奇, 潘燕, 余志群, 叶海燕. 香豆素-3-羧酸铒(III)一维配位聚合物[Er(CCA)3(H2O)2]n•2nH2O的溶剂热法合成、晶体结构及与牛血清白蛋白(BSA)的相互作用[J]. 化学学报, 2011, 69(19): 2319-2327.
YANG Shu-Ping, HAN Li-Jun, WANG Da-Qi, PAN Yan, YU Zhi-Qun, YE Hai-Yan. Solvothermal Synthesis, Crystal Structure of a 1D Coordination Polymer [Er(CCA)3(H2O)2]n•2nH2O (HCCA＝Coumarin-3-Carboxylic Acid) and the Interaction between the Polymer and Bovine Serum Albumin (BSA). Acta Chimica Sinica, 2011, 69(19): 2319-2327.