Abstract

The interaction of tiemonium methylsulfate (TMS), an antispasmodic drug with bovine serum albumin (s), has been studied. The
study has been investigated by fluorescence, ultraviolet–visible absorbance, viscometry, and molecular modeling techniques.
The binding constants between TMS and bovine serum albumin (BSA) were calculated based on fluorescence quenching data at
different temperatures. The negative ΔG° implied that the binding process was spontaneous and positive ΔH° and ΔS° suggested
that hydrogen bonding force most likely played a major role in the binding of TMS to BSA. Moreover, the results obtained from
molecular docking corroborate the experimental results obtained from spectroscopic investigations.