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Zarei, Mohammad Ali, Mohammad Ali Rasul, shazhir. (1404). Comparison of the Effect of α-Pinene and Gallic Acid on Tyrosinase Activity. سامانه مدیریت نشریات علمی, 14(3), 297-303. doi: 10.22034/jmpb.2024.367021.1761
Mohammad Ali Zarei; shazhir Mohammad Ali Rasul. "Comparison of the Effect of α-Pinene and Gallic Acid on Tyrosinase Activity". سامانه مدیریت نشریات علمی, 14, 3, 1404, 297-303. doi: 10.22034/jmpb.2024.367021.1761
Zarei, Mohammad Ali, Mohammad Ali Rasul, shazhir. (1404). 'Comparison of the Effect of α-Pinene and Gallic Acid on Tyrosinase Activity', سامانه مدیریت نشریات علمی, 14(3), pp. 297-303. doi: 10.22034/jmpb.2024.367021.1761
Zarei, Mohammad Ali, Mohammad Ali Rasul, shazhir. Comparison of the Effect of α-Pinene and Gallic Acid on Tyrosinase Activity. سامانه مدیریت نشریات علمی, 1404; 14(3): 297-303. doi: 10.22034/jmpb.2024.367021.1761

Comparison of the Effect of α-Pinene and Gallic Acid on Tyrosinase Activity

Journal of Medicinal plants and By-products
مقاله 12، دوره 14، شماره 3، مرداد و شهریور 2025، صفحه 297-303    اصل مقاله (1.05 M)
نوع مقاله: Research Paper
شناسه دیجیتال (DOI): 10.22034/jmpb.2024.367021.1761
نویسندگان
Mohammad Ali Zarei* ؛ shazhir Mohammad Ali Rasul
Department of Biological Sciences, Faculty of Science, University of Kurdistan, Sanandaj, Iran
چکیده
Tyrosinase is the key enzyme in melanin synthesis. Therefore, many Tyrosinase inhibitors have been tested in cosmetics and pharmaceuticals. The aim of this study was to compare the anti-Tyrosinase potential of Gallic acid and α-Pinene. The initial analysis was conducted using molecular docking methods. Then, laboratory experiments were performed using mushroom Tyrosinase, with catechol as the substrate and Kojic acid as the standard inhibitor of the enzyme. The antioxidant activity of Gallic acid and α-Pinene was evaluated using DPPH radicals. Docking scores showed that Gallic acid has a strong binding affinity towards Tyrosinase (ΔG = -6.33 Kcal/mol) forming an H-bond with Met 280 and a pi-pi stacking with His 263. α-Pinene could only bind to the active pocket via hydrophobic interactions, resulting in a lower binding affinity (ΔG = ˗3.89 Kcal/mol). Gallic acid showed the highest inhibitory effect (IC50 = 0.130 mg/mL), whereas α-Pinene showed a lower inhibitory capacity (IC50 = 0.392 mg/mL). The types of inhibition were competitive inhibition for Kojic acid and uncompetitive inhibition for Gallic acid. In the DPPH radical scavenging test, EC50 value for Gallic acid and α-Pinene was 0.269 mg/mL and 251.2 mg/mL, respectively. Both in silico and laboratory results were nearly identical. While α- Pinene is not as powerful an inhibitor of Tyrosinase as Gallic acid is, its effect will be increased perhaps by increasing its concentration. The anti-oxidant potential of Gallic acid is significantly higher than that of α-Pinene, so from this point of view also Gallic acid is more harmless and applicable with a higher degree of safeness.
کلیدواژه‌ها
Tyrosinase؛ α-Pinene؛ Gallic acid؛ Melanin
مراجع
  1. Decker H., Schweikardt T., Nillius D., Salzbrunn U., Jaenicke E., Tuczek F. Similar enzyme activation and catalysis in hemocyanins and Tyrosinases. Gene. 2007;398:183-191.
  2. Kanteev M., Goldfeder M., Fishman A. Structure-function correlations in Tyrosinases. Protein Sci. 2015;24(9):1360-1369. doi:10.1002/pro.2734
  3. Coates C.J., Nairn J. Diverse immune functions of hemocyanins. Dev. Comp. Immunol. 2014;45:43-55.
  4. Fairhead M., Thöny-Meyer L. Bacterial Tyrosinases: old enzymes with new relevance to biotechnology. Nat. Biotechnol. 2012;29(2):183-191.
  5. Yi W., Dubois C., Yahiaoui S., et al. Refinement of arylthiosemicarbazone pharmacophore in inhibition of mushroom Tyrosinase. Eur. J. Med. Chem. 2011;46:4330-4335.
  6. van Gelder C.W., Flurkey W.H., Wichers H.J. Sequence and structural features of plant and fungal Tyrosinases. Phytochemistry. 1997;45:1309-1323.
  7. Chang T.S. An updated review of Tyrosinase inhibitors. Int. J. Mol. Sci. 2009;10:2440-2475.
  8. Jeon S.H., Kim K.H., Koh J.U., Kong K.H. Inhibitory effects on L-dopa oxidation of Tyrosinase by skin-whitening agents. Bull. Korean Chem. Soc. 2005;26:1135-1137.
  9. Lee G.Y., Cho B.O., Shin J.Y., et al. Tyrosinase inhibitory components from the seeds of Cassia tora. Arch. Pharm. Res. 2018;41:490-496.
  10. Chiari M.E., Joray M.B., Ruiz G., Palacios S.M., Carpinella M.C. Tyrosinase inhibitory activity of native plants from central Argentina: Isolation of an active principle from Lithrea molleoides. Food Chem. 2010;120:10-14.
  11. Arndt K.A., Fitzpatrick T.B. Topical use of hydroquinone as a depigmenting agent. JAMA 1965;194:965-967.
  12. Zhou H., Kepa J.K., Siegel D., Miura S., Hiraki Y., Ross D. Benzene metabolite hydroquinone up-regulates chondromodulin-I and inhibits tube formation in human bone marrow endothelial cells. Mol. Pharmacol. 2009;76:579-587.
  13. Curto E.V., Kwong C., Hermersdörfer H., et al. Inhibitors of mammalian melanocyte Tyrosinase: in vitro comparisons of alkyl esters of gentisic acid with other putative inhibitors. Biochem. Pharmacol. 1999;57:663-672.
  14. Cabanes J., Chazarra S., Garcia-Carmona F. Kojic acid, a cosmetic skin whitening agent, is a slow-binding inhibitor of catecholase activity of Tyrosinase. J. Pharm. Pharmacol. 1994;46:982-985.
  15. Shimogaki H., Tanaka Y., Tamai H., Masuda M. In vitro and in vivo evaluation of ellagic acid on melanogenesis inhibition. Int. J. Cosmet. Sci. 2000;22:291-303.
  16. Spínola V., Mendes B., Câmara J.S., Castilho P.C. Effect of time and temperature on vitamin C stability in horticultural extracts. UHPLC-PDA vs iodometric titration as analytical methods. LWT-Food Sci. Tech. 2013;50:489-495.
  17. Ha Y.M., Park Y.J., Lee J.Y., et al. Design, synthesis and biological evaluation of 2- (substituted phenyl) thiazolidine-4-carboxylic acid derivatives as novel Tyrosinase inhibitors. Biochimie. 2012;94:533-540.
  18. Chawla S., Kvalnes K., deLong M.A., Wickett R., Manga P., Boissy R.E. DeoxyArbutin and its derivatives inhibit Tyrosinase activity and melanin synthesis without inducing reactive oxygen species or apoptosis. J. Drugs Dermatol. 2012;11:e28-e34.
  19. Khatib S., Nerya O., Musa R., Shmuel M., Tamir S., Vaya J. Chalcones as potent Tyrosinase inhibitors: the importance of a 2,4-substituted resorcinol moiety. Bioorg. Med. Chem. 2005;13:433-441.
  20. Fu R., Zhang Y., Guo Y., Chen F. Antioxidant and Tyrosinase inhibition activities of the ethanol-insoluble fraction of water extract of Sapium sebiferum (L.) Roxb. leaves. S. Afr. J. Bot. 2014;93:98-104.
  21. Peng Z., Li Y., Tan L., et al. Anti-tyrosinase, antioxidant and antibacterial activities of gallic acid-benzylidenehydrazine hybrids and their application in preservation of fresh-cut apples and shrimps. Food Chem. 2022;378:132127.
  22. Kim Y.J. Antimelanogenic and antioxidant properties of gallic acid. Biol. Pharm. Bull. 2007;30:1052-1055.
  23. Kumar K.J., Vani M.G., Wang S.Y., et al. In vitro and in vivo studies disclosed the depigmenting effects of gallic acid: a novel skin lightening agent for hyperpigmentary skin diseases. Biofactors. 2013;39:259-270.
  24. Kürkçüoğlu M., Ağalar H., Temiz B., Duran A., Paksoy M., Baser K. Antioxidant, Tyrosinase activities and composition of essential oils obtained from roots and fruits of Ferulago longistylis Boiss. J. Res. Pharm. 2002;26:790-798
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