Volume 33, Issue 6 (9-2025)
JSSU 2025, 33(6): 9124-9134 |
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Kalhor H, Siroosi M. Identification of Phenazines with Potential Inhibitory Activity against OXA-48 Carbapenemase by Using Molecular Docking Approach to Combat Antibiotic Resistance. JSSU 2025; 33 (6) :9124-9134
URL: http://jssu.ssu.ac.ir/article-1-6375-en.html
URL: http://jssu.ssu.ac.ir/article-1-6375-en.html
Abstract: (155 Views)
Introduction: Antibiotic resistance, particularly carbapenem resistance, poses a serious global health challenge, with the OXA-48 carbapenemase being a key factor in providing this resistance. This study employed molecular docking approaches to identify novel compounds capable of inhibiting the OXA-48 carbapenemase.
Methods: This study was descriptive-analytical. To investigate the binding mode of the selected phenazine compounds, the crystal structure of the OXA-48 carbapenemase was retrieved from the Protein Data Bank and prepared using AutoDock Tools 4.2. The compounds’ chemical structures were obtained from the PubChem database and optimized with ChemDraw (3D). Molecular docking was performed utilizing AutoDock Vina.
Results: The findings from the docking studies indicated that hydrophobic interactions played a crucial role in the binding of phenazine compounds to the OXA-48 carbapenemase. Among all the compounds analyzed, Aotaphenazine, PhenazinolinE, and BaraphenazineD exhibited the most favorable docking results. These compounds showed a higher affinity for binding to the key amino acids of the enzyme's active site, with binding energies of -9.9, -6.9, and -6.9 kcal/mol, respectively.
Conclusion: The molecular docking results suggest that the selected phenazine compounds, particularly Aotaphenazine, PhenazinolinE, and BaraphenazineD, may serve as potential inhibitors of the OXA-48 carbapenemase. Nonetheless, the therapeutic efficacy of these compounds needs to be confirmed through in vitro and in vivo studies.
Methods: This study was descriptive-analytical. To investigate the binding mode of the selected phenazine compounds, the crystal structure of the OXA-48 carbapenemase was retrieved from the Protein Data Bank and prepared using AutoDock Tools 4.2. The compounds’ chemical structures were obtained from the PubChem database and optimized with ChemDraw (3D). Molecular docking was performed utilizing AutoDock Vina.
Results: The findings from the docking studies indicated that hydrophobic interactions played a crucial role in the binding of phenazine compounds to the OXA-48 carbapenemase. Among all the compounds analyzed, Aotaphenazine, PhenazinolinE, and BaraphenazineD exhibited the most favorable docking results. These compounds showed a higher affinity for binding to the key amino acids of the enzyme's active site, with binding energies of -9.9, -6.9, and -6.9 kcal/mol, respectively.
Conclusion: The molecular docking results suggest that the selected phenazine compounds, particularly Aotaphenazine, PhenazinolinE, and BaraphenazineD, may serve as potential inhibitors of the OXA-48 carbapenemase. Nonetheless, the therapeutic efficacy of these compounds needs to be confirmed through in vitro and in vivo studies.
Type of Study: Original article |
Subject:
Microbiology
Received: 2025/01/28 | Accepted: 2025/03/9 | Published: 2025/09/6
Received: 2025/01/28 | Accepted: 2025/03/9 | Published: 2025/09/6
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