Exploring the molecular interaction of mebendazole with bovine serum albumin using multi-spectroscopic approaches and molecular docking
Abstract This article presents the binding interaction between mebendazole (MBZ) and bovine serum albumin. The interaction has been studied using different techniques, such as fluorescence quenching spectroscopy, UV–visible spectroscopy, synchronous fluorescence spectroscopy, fourier transform infra...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2022-07-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-022-15696-4 |
| _version_ | 1811224127796674560 |
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| author | Reem N. El Gammal Heba Elmansi Ali A. El-Emam Fathalla Belal Mohammed E. A. Hammouda |
| author_facet | Reem N. El Gammal Heba Elmansi Ali A. El-Emam Fathalla Belal Mohammed E. A. Hammouda |
| author_sort | Reem N. El Gammal |
| collection | DOAJ |
| description | Abstract This article presents the binding interaction between mebendazole (MBZ) and bovine serum albumin. The interaction has been studied using different techniques, such as fluorescence quenching spectroscopy, UV–visible spectroscopy, synchronous fluorescence spectroscopy, fourier transform infrared, and fluorescence resonance energy transfer in addition to molecular docking. Results from Stern Volmer equation stated that the quenching for MBZ-BSA binding was static. The fluorescence quenching spectroscopic study was performed at three temperature settings. The binding constant (kq), the number of binding sites (n), thermodynamic parameters (ΔHο, ΔSο and ΔGο), and binding forces were determined. The results exhibited that the interaction was endothermic. It was revealed that intermolecular hydrophobic forces led to the stabilization of the drug-protein system. Using the site marker technique, the binding between MBZ and BSA was found to be located at subdomain IIA (site I). This was furtherly approved using the molecular docking technique with the most stable MBZ configuration. This research may aid in understanding the pharmacokinetics and toxicity of MBZ and give fundamental data for its safe usage to avoid its toxicity. |
| first_indexed | 2024-04-12T08:44:55Z |
| format | Article |
| id | doaj.art-445b15ecb1d24f43b30888c7478f531b |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-04-12T08:44:55Z |
| publishDate | 2022-07-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-445b15ecb1d24f43b30888c7478f531b2022-12-22T03:39:45ZengNature PortfolioScientific Reports2045-23222022-07-0112111310.1038/s41598-022-15696-4Exploring the molecular interaction of mebendazole with bovine serum albumin using multi-spectroscopic approaches and molecular dockingReem N. El Gammal0Heba Elmansi1Ali A. El-Emam2Fathalla Belal3Mohammed E. A. Hammouda4Department of Medicinal Chemistry, Faculty of Pharmacy, Mansoura UniversityPharmaceutical Analytical Chemistry Department, Faculty of Pharmacy, Mansoura UniversityDepartment of Medicinal Chemistry, Faculty of Pharmacy, Mansoura UniversityPharmaceutical Analytical Chemistry Department, Faculty of Pharmacy, Mansoura UniversityDepartment of Medicinal Chemistry, Faculty of Pharmacy, Mansoura UniversityAbstract This article presents the binding interaction between mebendazole (MBZ) and bovine serum albumin. The interaction has been studied using different techniques, such as fluorescence quenching spectroscopy, UV–visible spectroscopy, synchronous fluorescence spectroscopy, fourier transform infrared, and fluorescence resonance energy transfer in addition to molecular docking. Results from Stern Volmer equation stated that the quenching for MBZ-BSA binding was static. The fluorescence quenching spectroscopic study was performed at three temperature settings. The binding constant (kq), the number of binding sites (n), thermodynamic parameters (ΔHο, ΔSο and ΔGο), and binding forces were determined. The results exhibited that the interaction was endothermic. It was revealed that intermolecular hydrophobic forces led to the stabilization of the drug-protein system. Using the site marker technique, the binding between MBZ and BSA was found to be located at subdomain IIA (site I). This was furtherly approved using the molecular docking technique with the most stable MBZ configuration. This research may aid in understanding the pharmacokinetics and toxicity of MBZ and give fundamental data for its safe usage to avoid its toxicity.https://doi.org/10.1038/s41598-022-15696-4 |
| spellingShingle | Reem N. El Gammal Heba Elmansi Ali A. El-Emam Fathalla Belal Mohammed E. A. Hammouda Exploring the molecular interaction of mebendazole with bovine serum albumin using multi-spectroscopic approaches and molecular docking Scientific Reports |
| title | Exploring the molecular interaction of mebendazole with bovine serum albumin using multi-spectroscopic approaches and molecular docking |
| title_full | Exploring the molecular interaction of mebendazole with bovine serum albumin using multi-spectroscopic approaches and molecular docking |
| title_fullStr | Exploring the molecular interaction of mebendazole with bovine serum albumin using multi-spectroscopic approaches and molecular docking |
| title_full_unstemmed | Exploring the molecular interaction of mebendazole with bovine serum albumin using multi-spectroscopic approaches and molecular docking |
| title_short | Exploring the molecular interaction of mebendazole with bovine serum albumin using multi-spectroscopic approaches and molecular docking |
| title_sort | exploring the molecular interaction of mebendazole with bovine serum albumin using multi spectroscopic approaches and molecular docking |
| url | https://doi.org/10.1038/s41598-022-15696-4 |
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