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In this study, the interaction of an anticonvulsant drug that used in the treatment of epilepsy, Lamotrigine (LTG) with the most important transport protein of the blood, human serum albumin (HSA) has been studied by using the electrochemical methods and molecular modeling techniques. For this purpose, a simple carbon paste electrode (CPE) was applied for electrocatalytic oxidation and investigation of LTG interaction with HSA. The stoichiometry of the complex between LTG and HSA and the binding constant (K b ) of the reaction were calculated from the calibration curves. The results show that binding of LTG to HSA formed two complexes with different stoichiometries with K b1  (2.46 × 10 3 ) and K b2  (1.75 × 10 7 ), respectively. In agreement with the experimental data, molecular modeling approach also confirmed that LTG can bind to the subdomain IIA and IB of HSA. Communicated by Ramaswamy H. Sarma

Determining the stoichiometry and binding constant of Lamotrigine with human serum albumin using voltammetry analysis and molecular modeling