Insights into the interaction mechanism between tiagabine hydrochloride and two serum albumins.

ABSTRACT: Tiagabine hydrochloride (TGB) is a widely used anticonvulsive drug for the treatment of epilepsy. To better understand the interactions of TGB with plasma proteins, human serum albumin (HSA) and bovine serum albumin (BSA) were selected as model proteins. TGB slightly increased thermal stability of the proteins as confirmed by VP-capillary differential scanning calorimetric (DSC) measurements. Isothermal titration calorimeter (ITC) results showed that TGB could be combined with HSA and BSA moderately, which was also corroborated by fluorescence analysis. Besides, the thermodynamic parameters (ΔH > 0, ΔS > 0) indicated that hydrophobic forces played a major role in the formulation of TGB-HSA and TGB-BSA complexes. Moreover, the main binding sites of TGB to HSA and BSA were also

SUBMITTER: Zhuo W 

PROVIDER: S-EPMC9082336 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature