A comparative study on the binding of single and double chain surfactant-cobalt(III) complexes with bovine serum albumin.

The comparative binding effect of single and double aliphatic chain containing surfactant-cobalt(III) complexes cis-Co(bpy)2(DA)23·2H2O (1), cis-Co(bpy)2(DA)Cl2·2H2O (2), cis-Co(phen)2(CA)23·2H2O (3), and cis-Co(phen)2(CA)Cl2·2H2O (4) with bovine serum albumin (BSA) under physiological condition was analyzed by steady state, time resolved fluorescence, synchronous, three-dimensional fluorescence, UV-Visible absorption and circular dichroism spectroscopic techniques. The results show that these complexes cause the fluorescence quenching of BSA through a static mechanism. The binding constants (Kb) and the number of binding sites were calculated and binding constant values are found in the range of 10(4)-10(5) M(-1). The results indicate that compared to single chain complex, double chain surfactant-cobalt(III) complex interacts strongly with BSA. Also the sign of thermodynamic parameters (ΔG°, ΔH°, and ΔS°) indicate that all the complexes interact with BSA through hydrophobic force. The binding distance (r) between complexes and BSA was calculated using Förster non-radiation energy transfer theory and found to be less than 7 nm. The results of synchronous, three dimensional fluorescence and circular dichroism spectroscopic methods indicate that the double chain surfactant-cobalt(III) complexes changed the conformation of the protein considerably than the respective single chain surfactant-cobalt(III) complexes. Antimicrobial studies of the complexes showed good activities against pathogenic microorganisms.