Multispectroscopic insight, morphological analysis and molecular docking studies of CuII-based chemotherapeutic drug entity with human serum albumin (HSA) and bovine serum albumin (BSA)

AbstractThe interaction studies of CuII nalidixic acid–DACH chemotherapeutic drug entity, [C36H50N8O6Cu] with serum albumin proteins, viz., human serum albumin (HSA) and bovine serum albumin (BSA) employing UV–vis, fluorescence, CD, FTIR and molecular docking techniques have been carried out. Complex [C36H50N8O6Cu] demonstrated strong binding affinity towards serum albumin proteins via hydrophobic contacts with binding constants, K = 3.18 × 105 and 7.44 × 104 M–1 for HSA and BSA, respectively implicating a higher binding affinity for HSA. The thermodynamic parameters ΔG, ΔH and ΔS at different temperatures were also calculated and the interaction of complex [C36H50N8O6Cu] with HSA and BSA was found to be enthalpy and entropy favoured, nevertheless, complex [C36H50N8O6Cu] demonstrated higher binding affinity towards HSA than BSA evidenced from its higher binding constant values. Time resolved fluorescence spectroscopy (TRFS) was carried out to validate the static quenching mechanism of HSA/BSA fluorescence...