Abstract
The interaction of Solifenacin succinate (SFS) with bovine serum albumin (BSA) has been investigated by UV-visible spectrophotometric, spectrofluorometric viscometric and molecular modeling methods. Fluorescence spectra suggested that the quenching mechanism of the interaction of SFS to BSA was a static quenching type. By the analysis of UV/vis spectra, it was observed that SFS had a high affinity with BSA which was indicated by the large binding constant. The thermodynamic parameters, ΔH and ΔS for the interaction of SFS and BSA have been calculated at different temperatures. The thermodynamic studies suggested that the interaction processes were endothermic disfavoured (ΔH > 0) and entropy favoured (ΔS > 0), which indicated that the SFS might interact with BSA by a non-traditional intercalation mode of binding via hydrophobic force. Moreover, the results obtained from molecular docking corroborate the experimental results obtained from spectroscopic investigations.
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