عنوان	Comparison of the Effect of α-Pinene and Gallic Acid on Tyrosinase Activity
نوع پژوهش	مقاله چاپ‌شده در مجلات علمی
کلیدواژه‌ها	Tyrosinase, α-Pinene, Gallic acid, Melanin
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 work once done by using molecular docking methods. Then the work applied in laboratory, using mushroom tyrosinase, catechol as substrate and Kojic acid as standard inhibitor of the enzyme. Antioxidant activity of Gallic acid and α-Pinene was evaluated using DPPH radicals. Docking scores showed that Gallic acid has a very good 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 was only able to bind to the active pocket via hydrophobic interactions that is why it for scores very low binding affinity (ΔG = -3.89 Kcal/mol). Gallic acid showed highest inhibitory effect (IC50 = 0.130 mg/mL), α-Pinene showed a lower capacity of inhibition (IC50 = 0.392 mg/mL). The types of inhibition were competitive inhibition for Gallic acid and uncompetitive inhibition for α- Pinene. In DPPH radical scavenging test, EC50 value for Gallic acid and α-Pinene were 0.269 mg/mL and 251.2 mg/mL respectively. Both in silico and laboratory result nearly the same. While α- Pinene is not a powerful inhibitor as Gallic acid, perhaps by increasing its concentration its effect will be increase. Anti-oxidant potential of Gallic acid is so much higher than α-Pinene, so from this point of view also Gallic acid is more harmless and applicable with higher safety.
پژوهشگران	محمدعلی زارعی (نفر اول)، شاژیز محمد علی رسول (نفر دوم)