Studies on the interactions of chloroquine diphosphate and phenelzine sulfate drugs with human serum albumin and human hemoglobin proteins by spectroscopic techniques

The interactions of chloroquine diphosphate (CQP) and phenelzine sulfate (PS) drugs with human serum albumin (HSA) and human hemoglobin (HMG) proteins were investigated by various spectroscopic methods. It was found that CQP caused the fluorescence quenching of protein molecules through a static quenching mechanism, but PS did not. The values of Stern–Volmer quenching constant, bimolecular quenching constant, binding constant and number of binding site on the protein molecules were calculated for HSA–CQP and HMG–CQP systems at pH 7.4 and different temperatures. For CQP, there was only one binding site on HSA and HMG proteins and the binding affinity of HSA was higher than that of HMG. The binding constants decreased with increasing temperature. The values of negative enthalpy change and positive entropy change indicated that electrostatic interactions play an important role in the binding processes. In addition, the binding processes were spontaneous and carried out by exothermic reactions. According to Förster resonance energy transfer theory, the average binding distance between proteins and CQP was calculated as 3.72nm for HSA–CQP system and 3.45nm for HMG–CQP system. Circular dichroism analysis displayed that the addition of CQP led to a decrease in the α-helix amount of HSA and HMG proteins. •Unlike PS, CQP was bounded by HSA and HMG proteins.•The fluorescence spectra of HSA and HMG were quenched by CQP through static mechanism.•HSA–CQP and HMG–CQP complexes were stabilized by electrostatic attraction forces.•Binding constants, thermodynamic parameters and binding distances were calculated.•The binding of CQP changed the conformational structure of HSA and HMG proteins.