Risperidone interacts with serum albumin forming complex

The aim of the work is to study the mechanisms of the interaction of risperidone with human and bovine serum albumins using the fluorescence quenching technique. Risperidone is an atypical antipsychotic drug used to treat many psychiatric disorders. We selectively excited the fluorescence of tryptophan residues with a 290 nm wavelength light, and observed quenching by titrating human and bovine serum albumin solutions with risperidone. Emission spectra were recorded in the range from 300 to 450 nm for each quencher addition. Stern–Volmer graphs were plotted and quenching constants were estimated. Results showed that the drug quenches the fluorescence of the human serum albumin by the formation of a complex risperidone-albumin. Association constants calculated from Stern–Volmer equation for low concentrations (lower than 1:10 ratio risperidone/albumin) were of 2.56 × 105 M−1, at 25 °C, and 1.43 × 105 M−1, at 37 °C. As the quenching intensity of bovine serum albumin, which contains two tryptophan residues, was found to be higher than that of human serum albumin, which contains only one tryptophan residue. Hence, we suggest that the primary binding site for risperidone in albumin should be located in sub domain IB.

► Interaction of risperidone to albumin was studied by fluorescence quenching technique.
► Risperidone forms complex with serum albumins.
► The primary binding site for risperidone in albumin could be located in sub domain IB.