Molecular Docking And Analysis Of Binding Interaction Between Levothyroxine And Bovine Liver Catalase

Here, the structure and enzyme activity of bovine liver catalase (BLC) were evaluated in the presence of levothyroxine (LEV) by using spectroscopic techniques and molecular docking simulation. According our results in the kinetics section, LEV inhibited BLC through a mixed-type inhibitory mechanism. Both kinetics and molecular docking results showed that LEV did not directly bind into the activity site of catalase. The interaction of this drug with the cavity of BLC influenced the microenvironment of the enzyme activity site; so the activity of the enzyme is reduced. The structure of the enzyme changes in the presence of the LEV by decreasing α-helix and increasing β-sheet content. Fluorescence quenching of BLC was occurred in the binding interaction via a static mechanism. Thermodynamic and also molecular docking results confirmed that the main forces in the LEV-BLC interaction were hydrogen bonds and Van der Waals forces.