Molecular Docking Studies of Some Hydroxy Nitrodiphenyl Ether Analogues as Tyrosinase Inhibitors
Background & Objective: Tyrosinase is a key enzyme in pigment synthesis.Overproduction of melanin in parts of the skin results in hyperpigmentation diseases. Thus, its inhibitors are highly important in the medical, cosmetic and agricultural fields. The aim of this research is the bioinformatica...
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| Format: | Article |
| Language: | English |
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Fasa University of Medical Sciences
2016-12-01
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| Series: | Journal of Advanced Biomedical Sciences |
| Subjects: | |
| Online Access: | http://jabs.fums.ac.ir/article-1-1097-en.pdf |
| _version_ | 1797679611503443968 |
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| author | Fatemeh Sholehvar Azizeh Asadzadeh Hooria Seyedhosseini |
| author_facet | Fatemeh Sholehvar Azizeh Asadzadeh Hooria Seyedhosseini |
| author_sort | Fatemeh Sholehvar |
| collection | DOAJ |
| description | Background & Objective: Tyrosinase is a key enzyme in pigment synthesis.Overproduction of melanin in parts of the skin results in hyperpigmentation diseases. Thus, its inhibitors are highly important in the medical, cosmetic and agricultural fields. The aim of this research is the bioinformatical study of tyrosinase inhibition by a number of hydroxy nitrodiphenyl ether derivatives.
Material & Methods: This is a descriptive-analytic study. In order to investigate the mode of interaction of the compounds with tyrosinase active site, the chemical structures of all compounds were designed using ChemDraw program, then transferred into Hyperchem software for energy minimization. Docking study was performed by AutoDock 4.2 program and the resulting docking poses were analyzed in AutoDockTools, DS Visualizer 3.5 and Ligplot software.
Results: Among the all studied compounds, the best docking results were related to 4-Hydroxy- 2'-nitrodiphenyl etherdisplayed. In fact, this compound had the most negative ΔGbind (-12.79 Kcal/mol) that indicated favorable interactions with the key amino acid residues at active site of tyrosinase. Docking results for this compound are in accordance with those of co-crystallized ligand (tropolone). In this compound, the oxygen of nitro group has an efficient metal-ligand interaction with the Cu2+ ions in the active site.
Conclusion: Finally, in respect to high effectiveness and docking results, we can conclude that the compound 4-Hydroxy- 2'-nitrodiphenyl ether may be regarded as an effective anti-tyrosinase inhibitor. |
| first_indexed | 2024-03-11T23:17:18Z |
| format | Article |
| id | doaj.art-2bcc6a8d0186449fa1ca4d71f4f1055a |
| institution | Directory Open Access Journal |
| issn | 2228-5105 2783-1523 |
| language | English |
| last_indexed | 2024-03-11T23:17:18Z |
| publishDate | 2016-12-01 |
| publisher | Fasa University of Medical Sciences |
| record_format | Article |
| series | Journal of Advanced Biomedical Sciences |
| spelling | doaj.art-2bcc6a8d0186449fa1ca4d71f4f1055a2023-09-20T21:22:33ZengFasa University of Medical SciencesJournal of Advanced Biomedical Sciences2228-51052783-15232016-12-0164548555Molecular Docking Studies of Some Hydroxy Nitrodiphenyl Ether Analogues as Tyrosinase InhibitorsFatemeh Sholehvar0Azizeh Asadzadeh1Hooria Seyedhosseini2 Young Researchers and Elites club, zarghan Branch, Islamic Azad University, zarghan, Iran Department of biology, faculty of science, Nour Danesh institute of higher education, Meymeh, Isfahan, Iran Young Researchers and Elites club, Science and Research Branch, Islamic Azad University, Tehran, Iran Background & Objective: Tyrosinase is a key enzyme in pigment synthesis.Overproduction of melanin in parts of the skin results in hyperpigmentation diseases. Thus, its inhibitors are highly important in the medical, cosmetic and agricultural fields. The aim of this research is the bioinformatical study of tyrosinase inhibition by a number of hydroxy nitrodiphenyl ether derivatives. Material & Methods: This is a descriptive-analytic study. In order to investigate the mode of interaction of the compounds with tyrosinase active site, the chemical structures of all compounds were designed using ChemDraw program, then transferred into Hyperchem software for energy minimization. Docking study was performed by AutoDock 4.2 program and the resulting docking poses were analyzed in AutoDockTools, DS Visualizer 3.5 and Ligplot software. Results: Among the all studied compounds, the best docking results were related to 4-Hydroxy- 2'-nitrodiphenyl etherdisplayed. In fact, this compound had the most negative ΔGbind (-12.79 Kcal/mol) that indicated favorable interactions with the key amino acid residues at active site of tyrosinase. Docking results for this compound are in accordance with those of co-crystallized ligand (tropolone). In this compound, the oxygen of nitro group has an efficient metal-ligand interaction with the Cu2+ ions in the active site. Conclusion: Finally, in respect to high effectiveness and docking results, we can conclude that the compound 4-Hydroxy- 2'-nitrodiphenyl ether may be regarded as an effective anti-tyrosinase inhibitor.http://jabs.fums.ac.ir/article-1-1097-en.pdfbioinformaticdockinghydroxy nitrodiphenyl ethertyrosinase |
| spellingShingle | Fatemeh Sholehvar Azizeh Asadzadeh Hooria Seyedhosseini Molecular Docking Studies of Some Hydroxy Nitrodiphenyl Ether Analogues as Tyrosinase Inhibitors Journal of Advanced Biomedical Sciences bioinformatic docking hydroxy nitrodiphenyl ether tyrosinase |
| title | Molecular Docking Studies of Some Hydroxy Nitrodiphenyl Ether Analogues as Tyrosinase Inhibitors |
| title_full | Molecular Docking Studies of Some Hydroxy Nitrodiphenyl Ether Analogues as Tyrosinase Inhibitors |
| title_fullStr | Molecular Docking Studies of Some Hydroxy Nitrodiphenyl Ether Analogues as Tyrosinase Inhibitors |
| title_full_unstemmed | Molecular Docking Studies of Some Hydroxy Nitrodiphenyl Ether Analogues as Tyrosinase Inhibitors |
| title_short | Molecular Docking Studies of Some Hydroxy Nitrodiphenyl Ether Analogues as Tyrosinase Inhibitors |
| title_sort | molecular docking studies of some hydroxy nitrodiphenyl ether analogues as tyrosinase inhibitors |
| topic | bioinformatic docking hydroxy nitrodiphenyl ether tyrosinase |
| url | http://jabs.fums.ac.ir/article-1-1097-en.pdf |
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