The current study investigates lamotrigine's binding to bovine serum albumin (BSA) using UV visible, fluorescence, synchronous fluorescence (SFS), CD spectroscopy, and molecular docking. The addition of lamotrigine at increasing concentrations suppressed the intensity of the BSA's fluorescence. Synchronous, and UV-vis fluorescence experiments demonstrated the effects of lamotrigine on the structure of BSA. CD spectroscopy was used to determine how the native BSA's stability changed when lamotrigine was included. To assess the binding sites and affinity of lamotrigine to BSA with simultaneous interactions, molecular docking studies were done using AutoDock. This work contributes to our perception of the mechanism underlying the drug-binding effect at higher concentrations by elucidating the molecular interactions and modifications between lamotrigine and BSA.