Interaction between olanzapine and human serum albumin and effect of metal ions, caffeine and flavonoids on the binding: A spectroscopic study.

In this study, the binding of olanzapine (OLZ) to human serum albumin (HSA) and the influence of metal ions (Ca, Mg, Cu, Zn, Fe), caffeine (CAF) and flavonoids (diosmin (DIO), catechin (CAT), quercetin (QUE)), on their affinity, was investigated by fluorescence spectroscopy and UV-vis absorption spectroscopy. Fluorescence experiments suggest that OLZ quench the fluorescence of HSA through the mixed quenching mechanism and non-radiation energy transferring as a result of the HSA-OLZ complex formation. OLZ spontaneously bind in the site I on HSA, and according to thermodynamic parameters, the reaction was spontaneous and mainly driven by hydrogen bonds and van der Waals interactions. The presence of M ions, CAF, DIO and CAT decreased binding affinity between OLZ and HSA which indicates that they could compete against OLZ in the site I. Contrary, in the presence of QUE the binding affinity of the HSA-OLZ system enhanced, which may be explained by conformational changes in HSA (non-competitive interference).