Synthesis of benzamide derivatives and evaluation of their in vitro and in silico tyrosinase inhibitory activities
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https://doi.org/10.15625/2525-2518/18302Keywords:
benzamide derivatives, tyrosinase inhibitory activity, docking studiesAbstract
In this research, six benzamide derivatives were traditionally synthesized using hydrazine, carbazide, and hydroxylamine derivatives through the pre- or in situ activation of the carboxylic acid functionality. Their chemical structures were identified as N′-phenylbenzohydrazide, N′-(2,4-dinitrophenyl)benzohydrazide, N′-(benzoyloxy)benzamide, N-dibenzoylurea, 2-amino-5-(4-phenyl)-1,3,4-thiadiazole, and benzohydrazide based on the interpretation of NMR spectroscopic data. Among these products, N′-phenylbenzohydrazide and N-(benzoyloxy)benzamide showed potent tyrosinase inhibitory activity with the IC50 values of 10.5 and 2.5 μM, respectively, stronger than that of kojic acid (44.6 μM). Docking studies between oxy-tyrosinase and the two active compounds have been carried out to analyze their binding interactions. Both two active compounds showed negative binding free energy values (S values) and some more interactions than the positive control (kojic acid). This discovery provided evidence for the potent tyrosinase inhibitory activity of these two compounds, making them promising candidates for the development of anti-tyrosinase agents in medicine and cosmetics.Downloads
References
Chawla S., Delong M. A., Visscher M. O., Wickett R. R., Manga P., Boissy R. E. - Mechanism of tyrosinase inhibition by deoxyArbutin and its second-generation derivatives, Br. J. Dermatol. 159 (2008) 1267-1274. doi.org/10.1111/j.1365-2133.2008.08864.x.
Rodriguez-Lopez J. N., Tudela J., Varon R., Garcia-Carmona F., Garcia-Canovas F. - Analysis of a kinetic model for melanin biosynthesis pathway, J. Biol. Chem. 267 (1992) 3801-3810. doi.org/10.1016/S0021-9258(19)50597-X.
Decker H., Tuczek F. - Tyrosinase/catecholoxidase activity of hemocyanins: structural basis and molecular mechanism, Trends. Biochem. Sci. 25 (2000) 392-397. doi.org/10.1016/s0968-0004(00)01602-9.
Pillaiyar T., Manickam M., Namasivayam V. - Skin whitening agents: medicinal chemistry perspective of tyrosinase inhibitors, J. Enzyme Inhib. Med. Chem. 32 (2017) 403-425. doi.org/10.1080/14756366.2016.1256882.
Kushwaha N., Saini R. K., Kushwaha S. K. - Synthesis of some amide derivatives and their biological activity, Int. J. ChemTech. Res. 3 (2011) 203-209.
Khan S. B., Khan M. T. H., Jang E. S., Akhtar K., Seo J., Han H. - Tyrosinase inhibitory effect of benzoic acid derivatives and their structure-activity relationships, J. Enzyme Inhib. Med. Chem. 25 (2010) 812-817. doi.org/10.3109/14756366.2010.482529.
Lee S., Ullah S., Park C., Lee H. W., Kang D., Yang J., Akter J., Park Y., Chun P., Moon H. R. - Inhibitory effects of N-(acryloyl)benzamide derivatives on tyrosinase and melanogenesis, Bioorg. Med. Chem. 27 (2019) 3929-3937. doi.org/10.1016/j.bmc.2019.07.034.
McMurry J. - Organic Chemistry, 9th ed., Cornell University, United States (2015).
Isabella R., Giorgio F. - Different Schiff basesStructure, importance and classification, Molecules. 27 (2022) 787-795. doi.org/10.3390/molecules27030787.
Christopher A. R., Patrick A. R. - Tyrosinase: The four oxidation states of the active site and their relevance to enzymatic activation, oxidation and inactivation, Bioorg. Med. Chem. 22 (2014) 2388-2395. doi.org/10.1016/j.bmc.2014.02.048.
Matoba Y., Kumagai T., Yamamoto A., Yoshitsu H., Sugiyama M. - Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis, J. Biol. Chem. 281 (2006) 8981-8990. doi.org/10.1074/jbc.M509785200.
Choi J., Lee Y. M., Jee J. G. - Thiopurine drugs repositioned as tyrosinase inhibitors, Int. J. Mol. Sci. 19 (2018) 77-92. doi.org/10.3390/ijms19010077.
Chemical Computing Group. - Molecular operating environment (MOE) 2016, Chemical Computing Group, Montreal, QC, Canada, 2016.
Dassault Systèmes BIOVIA. - BIOVIA Discovery Studio Visualizer, Dassault Systèmes BIOVIA, San Diego, CA, USA, 2016.
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