In Vitro Inhibition of Xanthine Oxidase Purified from Arthritis Serum Patients by Nanocurcumin and Artemisinin Active Compounds
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 precip...
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MDPI AG
2023-06-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/28/13/5124 |
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| author | Waseem Yousif M. AL-dulaimy Asmaa A. Hussein Mohammed Asaad Mahdi Mohammed Kadhom |
| author_facet | Waseem Yousif M. AL-dulaimy Asmaa A. Hussein Mohammed Asaad Mahdi Mohammed Kadhom |
| author_sort | Waseem Yousif M. AL-dulaimy |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-11T01:34:06Z |
| format | Article |
| id | doaj.art-552a992bdee9443693b0871c07f12ed5 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-11T01:34:06Z |
| publishDate | 2023-06-01 |
| publisher | MDPI AG |
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| spelling | doaj.art-552a992bdee9443693b0871c07f12ed52023-11-18T17:08:31ZengMDPI AGMolecules1420-30492023-06-012813512410.3390/molecules28135124In Vitro Inhibition of Xanthine Oxidase Purified from Arthritis Serum Patients by Nanocurcumin and Artemisinin Active CompoundsWaseem Yousif M. AL-dulaimy0Asmaa A. Hussein1Mohammed Asaad Mahdi2Mohammed Kadhom3Department of Chemistry, College of Science, University of Diyala, Baquba 32001, IraqDepartment of Molecular and Medical Biotechnology, College of Biotechnology, Al-Nahrain University, Jadriya, Baghdad 64074, IraqDepartment of Chemistry, College of Science, University of Diyala, Baquba 32001, IraqDepartment of Environmental Science, College of Energy and Environmental Science, Al-Karkh University of Science, Baghdad 10081, IraqCurcumin 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.https://www.mdpi.com/1420-3049/28/13/5124xanthine oxidasecurcuminartemisininmolecular dockinginhibition |
| spellingShingle | Waseem Yousif M. AL-dulaimy Asmaa A. Hussein Mohammed Asaad Mahdi Mohammed Kadhom In Vitro Inhibition of Xanthine Oxidase Purified from Arthritis Serum Patients by Nanocurcumin and Artemisinin Active Compounds Molecules xanthine oxidase curcumin artemisinin molecular docking inhibition |
| title | In Vitro Inhibition of Xanthine Oxidase Purified from Arthritis Serum Patients by Nanocurcumin and Artemisinin Active Compounds |
| title_full | In Vitro Inhibition of Xanthine Oxidase Purified from Arthritis Serum Patients by Nanocurcumin and Artemisinin Active Compounds |
| title_fullStr | In Vitro Inhibition of Xanthine Oxidase Purified from Arthritis Serum Patients by Nanocurcumin and Artemisinin Active Compounds |
| title_full_unstemmed | In Vitro Inhibition of Xanthine Oxidase Purified from Arthritis Serum Patients by Nanocurcumin and Artemisinin Active Compounds |
| title_short | In Vitro Inhibition of Xanthine Oxidase Purified from Arthritis Serum Patients by Nanocurcumin and Artemisinin Active Compounds |
| title_sort | in vitro inhibition of xanthine oxidase purified from arthritis serum patients by nanocurcumin and artemisinin active compounds |
| topic | xanthine oxidase curcumin artemisinin molecular docking inhibition |
| url | https://www.mdpi.com/1420-3049/28/13/5124 |
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