Abstract

Aspirin (ASP) and pioglitazone (PGL) are the most common drugs that are widely used by diabetic patients to control the blood sugar and hinder cardiovascular diseases. The interaction between PGL and ASP is one of the important medical issues to clarify the safety of co-administration of these drugs. In the present study, the effect of co-administered ASP with PGL was investigated on the structure and catalytic function of catalase as a potential target in the liver. Based on our data, co-administration of ASP-PGL significantly enhanced the catalase activity in comparison with PGL alone. However, ASP does not have any effects on the catalytic function of catalase. Moreover, the dialysis measurement and CD spectroscopy study revealed that binding of ASP to catalase could increase the stability of catalase-PGL complex. Based on the obtained data, it is shown that the binding of ASP to catalase led to increase the affinity of catalase to PGL. Binding analysis showed that the association constant of catalase-PGL was reduced considerably in the presence of ASP from 12.19 +/- 0.1 x 10(6) M-1 to 6.4 +/- 0.2 x 10(6) M-1 at 298 K. Multiple ligands simultaneous docking (MLSD) also confirmed an increase in the binding affinity of PGL to catalase. (C) 2018 Elsevier B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM). All rights reserved.