Synthesis, characterization, and thermodynamic studies of the interaction of some new water-soluble Schiff-base complexes with bovine serum albumin

Some new water-soluble Schiff-base complexes Na-2[M(5-SO3-2,3-salpyr)(H2O)(n)] center dot 2H(2)O (5-SO3-2,3-salpyr = N,N'-bis(5-sulphosalicyliden)-2,3-diaminopyridine and M = Zn, Cu, Ni) were synthesized and characterized by elemental analysis, IR, H-1 NMR, magnetic susceptibility measurement, thermal analysis, and UV-Vis spectroscopy. The mechanism of binding of Na-2[M(5-SO3-2,3-salpyr)(H2O)(n)] center dot 2H(2)O with bovine serum albumin (BSA) was investigated by fluorescence spectroscopy. The fluorescence titration revealed that the intrinsic fluorescence of BSA was quenched by Na-2[M(5-SO3-2,3-salpyr)], which was rationalized in terms of the static quenching mechanism. The values of the Stern-Volmer constants, quenching rate constants, binding constants, binding sites, and average aggregation number of BSA were determined by this method. Thermodynamic parameters were calculated by the van't Hoff equation. The data clearly indicate that the binding is entropy driven and enthalpically disfavored. Based on the Forster theory of non-radiative energy transfer, the efficiency of energy transfer, and the distance between the donor (Trp residues) and the acceptor (Na-2[M(5-SO3-2,3-salpyr)]) were evaluated. Also the synchronous fluorescence spectra showed that the microenvironment of the tryptophan residues was not changed. Finally, our results indicate that the complexes can bind to BSA and be efficiently transported in the body, which could be helpful for further drug design.