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 × 10⁶ M⁻¹ to 6.4 ± 0.2 × 10⁶ M⁻¹ at 298 K. Multiple ligands simultaneous docking (MLSD) also confirmed an increase in the binding affinity of PGL to catalase.

阿司匹林（ASP）和吡格列酮（PGL）是糖尿病患者最常用的药物，可用于控制血糖和阻碍心血管疾病。PGL和ASP之间的相互作用是阐明这些药物共同给药安全性的重要医学问题之一。在本研究中，研究了ASP和PGL共同使用对过氧化氢酶的结构和催化功能的影响，而过氧化氢酶是肝脏的潜在靶标。根据我们的数据，与单独使用PGL相比，ASP-PGL的共同给药显着增强了过氧化氢酶的活性。但是，ASP对过氧化氢酶的催化功能没有任何影响。此外，透析测量和CD光谱研究表明，ASP与过氧化氢酶的结合可以增加过氧化氢酶-PGL复合物的稳定性。根据获得的数据，表明ASP与过氧化氢酶的结合导致过氧化氢酶对PGL的亲和力增加。结合分析表明，在存在ASP的情况下，过氧化氢酶-PGL的缔合常数从12.19±0.1×10显着降低。 在298 K时为⁶  M ^-1至6.4±0.2×10 ⁶  M ^-1。多个配体同时对接（MLSD）也证实了PGL与过氧化氢酶的结合亲和力增加。