Department of Chemistry, College of Science, University of Diyala, Baquba 32001, Iraq.
Department of Molecular and Medical Biotechnology, College of Biotechnology, Al-Nahrain University, Jadriya, Baghdad 64074, Iraq.
Molecules. 2023 Jun 29;28(13):5124. doi: 10.3390/molecules28135124.
Curcumin and artemisinin are commonly used in traditional East Asian medicine. In this study, we investigated the inhibitory effects of these active compounds on xanthine oxidase (XO) using allopurinol as a control. XO was purified from the serum of arthritis patients through ammonium sulfate precipitation (65%) and ion exchange chromatography on diethylaminoethyl (DEAE)-cellulose. The specific activity of the purified enzyme was 32.5 U/mg protein, resulting in a 7-fold purification with a yield of 66.8%. Molecular docking analysis revealed that curcumin had the strongest interaction energy with XO, with a binding energy of -9.28 kcal/mol. The amino acid residues Thr1077, Gln762, Phe914, Ala1078, Val1011, Glu1194, and Ala1079 were located closer to the binding site of curcumin than artemisinin, which had a binding energy of -7.2 kcal/mol. In vitro inhibition assays were performed using nanocurcumin and artemisinin at concentrations of 5, 10, 15, 20, and 25 µg/mL. Curcumin inhibited enzyme activity by 67-91%, while artemisinin had a lower inhibition ratio, which ranged from 40-70% compared to allopurinol as a control.
姜黄素和青蒿素是传统东亚医学中常用的药物。在这项研究中，我们使用别嘌呤醇作为对照，研究了这些活性化合物对黄嘌呤氧化酶 (XO) 的抑制作用。通过硫酸铵沉淀（65%）和二乙基氨基乙基（DEAE）-纤维素离子交换层析，从关节炎患者的血清中纯化 XO。纯化酶的比活性为 32.5 U/mg 蛋白，得率为 66.8%，酶的纯化倍数为 7 倍。分子对接分析表明，姜黄素与 XO 的相互作用能最强，结合能为-9.28 kcal/mol。与青蒿素相比，姜黄素的结合位点更接近氨基酸残基 Thr1077、Gln762、Phe914、Ala1078、Val1011、Glu1194 和 Ala1079，其结合能为-7.2 kcal/mol。在浓度为 5、10、15、20 和 25 µg/mL 时，使用纳米姜黄素和青蒿素进行了体外抑制实验。姜黄素抑制酶活性的能力为 67-91%，而青蒿素的抑制率较低，与作为对照的别嘌呤醇相比，抑制率在 40-70%之间。
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