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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. |
