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Studies on the interaction between a Co(II) complex with salicylaldehyde-aminoacetic acid Schiff base and bovine serum albumin
Authors:L C Yu  H M Peng  S L Liu
Institution:1. Key Laboratory of Theoretical Chemistry and Molecular Simulation of Ministry of Education, Hunan Provincial University Key Laboratory of QSAR/QSPR, School of Chemistry and Chemical Engineering, Hunan University of Science and Technology, Xiangtan, Hunan, 411201, P.R. China
Abstract:A Co(II) complex Co3(L)4(H2O)6] · 2Cl (I), where L is salicylaldehyde-aminoacetic acid Schiff base, was synthesized and characterized via elemental analysis, UV, and single crystal X-ray crystallography. Complex I crystallizes in the orthorhombic system, space group Pbcn with lattice parameters a = 9.569(4), b = 12.301(5), c = 36.931(14) Å, V = 4347(3) Å3, Z = 4, ρcalcd = 1.608 mg m?3. At the same time, the binding reaction between complex I and bovine serum albumin (BSA) was studied by fluorescence spectroscopy combined with UV-Vis absorption measurements under simulative physiological conditions. The results indicated that its combination reaction is mainly a static quenching process. Complex I bound BSA with a molar ratio of 1: 1 and the binding constant K A values are 3.86 × 105 L mol?1 (25°C) and 1.17 × 105 L mol?1 (36°C). The shortest binding distance r between the donor BSA and acceptor (complex I) is 2.49 nm, which affirms that complex I has partly inserted into the hydrophobic pocket of BSA.
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