The Levothyroxine Effects On The Catalytic Activity And Structural Stability Of Bovine Liver Catalase

Levothyroxine (LEV, Fig. 1), is a manufactured form of the thyroid hormone, thyroxine.It is used to treat hypothyroidism, a condition where the thyroid gland does not produce enough thyroid hormone [1, 2]. To explore the possible side effects of LEV on the antioxidant defense system of the liver, we analyzed the conformational and functional changes of bovine liver catalase (BLC) in the presence of LEV, using different spectroscopic and molecular docking techniques. Fluorescence studies revealed that LEV quenches intrinsic emission of BLC via static quenching process. Thermodynamic data suggested that hydrophobic interactions play a major role in the binding reaction of LEV on BLC. Structural studies indicated that the binding LEV to the enzyme is responsible for the changes of the percentage of secondary structures’ elements especially α-helix. Despite remarkable structural changes of BLC due to hydrophobic interactions with ligands, its function was not influenced considerably. The molecular docking results are in well agreement with the experimental data confirming that there exists one binding site for LEV on BLC at the distance of Forster theory.

کلیدواژه ها:

Catalase ، Enzymatic activity ، Fuorescence ، Molecular docking