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Zarei, Mohammad Ali, Abubakr Ibrahim, Hedi. (1404). In Silico and in Vitro Comparison of Anti-tyrosinase Potential of Crocin and Quercetin. سامانه مدیریت نشریات علمی, 15(1), 85-90. doi: 10.22034/jmpb.2025.369858.2001
Mohammad Ali Zarei; Hedi Abubakr Ibrahim. "In Silico and in Vitro Comparison of Anti-tyrosinase Potential of Crocin and Quercetin". سامانه مدیریت نشریات علمی, 15, 1, 1404, 85-90. doi: 10.22034/jmpb.2025.369858.2001
Zarei, Mohammad Ali, Abubakr Ibrahim, Hedi. (1404). 'In Silico and in Vitro Comparison of Anti-tyrosinase Potential of Crocin and Quercetin', سامانه مدیریت نشریات علمی, 15(1), pp. 85-90. doi: 10.22034/jmpb.2025.369858.2001
Zarei, Mohammad Ali, Abubakr Ibrahim, Hedi. In Silico and in Vitro Comparison of Anti-tyrosinase Potential of Crocin and Quercetin. سامانه مدیریت نشریات علمی, 1404; 15(1): 85-90. doi: 10.22034/jmpb.2025.369858.2001

In Silico and in Vitro Comparison of Anti-tyrosinase Potential of Crocin and Quercetin

Journal of Medicinal plants and By-products
مقاله 11، دوره 15، شماره 1، فروردین و اردیبهشت 2026، صفحه 85-90    اصل مقاله (885.66 K)
نوع مقاله: Research Article
شناسه دیجیتال (DOI): 10.22034/jmpb.2025.369858.2001
نویسندگان
Mohammad Ali Zarei* ؛ Hedi Abubakr Ibrahim
Department of Biological Sciences, Faculty of Science, University of Kurdistan, Sanandaj, Iran
چکیده
Tyrosinase inhibitors are often used in two primary ways: in the cosmetics industry to lighten skin and treat certain dermatological conditions, and in agriculture to stop fruit and vegetables from browning caused by enzymes. This study aimed to compare the anti-tyrosinase and antioxidant potential of Crocin and Quercetin. The work was started by molecular docking (in silico). The experiment was then carried out in a lab setting using a commercial mushroom tyrosinase, pyrocatechol as the substrate, and Kojic acid as a typical enzyme inhibitor. Crocin and Quercetin antioxidant activity was assessed using DPPH radicals. Docking scores presented that Crocin has a great binding affinity towards tyrosinase, ΔG = -6.1 Kcal/mol. Quercetin had a binding energy of ΔG = -8.0 (kcal/mol). Quercetin exhibited a higher tyrosinase inhibitory effect with an IC50 of 0.158 mM, whereas Crocin showed a lower capacity of inhibition with an IC50 of 2.49 mM. The types of inhibition were competitive inhibition for Quercetin and mixed inhibition for Crocin. For DPPH radical scavenging activity, the EC50 value for Ascorbic acid was 0.179 mM; this value for Crocin and Quercetin was 1.74 mM and 0.031 mM, respectively. Quercetin is a powerful and mechanistically simple inhibitor of mushroom tyrosinase, so it is a valuable candidate for several applications targeted at regulating enzymatic browning and melanogenesis. Despite having antioxidant and inhibitory qualities, Crocin may not be as efficient as it may be as a main tyrosinase inhibitor due to its mixed mechanism of inhibition and its lower inhibitory potential.
کلیدواژه‌ها
Tyrosinase؛ Crocin؛ Quercetin؛ Melanin
مراجع
  1. Chang T-S. An Updated Review of Tyrosinase Inhibitors. International Journal of Molecular Sciences. 2009; 10:2440–75.
  2. Afrasiabi A., Zarei M.A. Tyrosinase Inhibition, Antioxidant Activity and GC-MS Analysis of the Hexane Extracts of the Aerial Parts of Astragalus vegetus and Gundelia turnifortii L. Journal of Medicinal Plants. 2019; 2:73–86.
  3. Zolghadri S., Bahrami A., Hassan Khan M.T., Munoz-Munoz J., Garcia-Molina F., Garcia-Canovas F., Saboury A.A. A comprehensive review on tyrosinase inhibitors. Journal of Enzyme Inhibition and Medicinal Chemistry. 2019;34:279–309.
  4. Hasani A., Zarei M.A. Study of mushroom tyrosinase inhibitory activity among 70 plants from Kurdistan Provience. 2019;18:fa247–66, fa312.
  5. Cardoso R., Valente R., Souza Da Costa CH., Da S. Gonçalves Vianez J.L., Santana Da Costa K., De Molfetta F.A., Alves C.N. Analysis of Kojic Acid Derivatives as Competitive Inhibitors of Tyrosinase: A Molecular Modeling Approach. Molecules. 2021;26:2875.
  6. Song Y., Wang Y., Zheng Y., Liu T., Zhang C. Crocins: A comprehensive review of structural characteristics, pharmacokinetics and therapeutic effects. Fitoterapia. 2021;153:104969.
  7. Ali A., Yu L., Kousar S., Khalid W., Maqbool Z., Aziz A., Arshad M.S., Aadil R.M., Trif M., Riaz S., Shaukat H., Faisal Manzoor M., Qin H. Crocin: Functional characteristics, extraction, food applications and efficacy against brain related disorders. Frontiers in Nutrition. 2022;9:1009807.
  8. Cerdá-Bernad D., Valero-Cases E., Pastor J-J., Frutos M.J. Saffron bioactives crocin, crocetin and safranal: effect on oxidative stress and mechanisms of action. Critical Reviews in Food Science and Nutrition. 2022;62:3232–49.
  9. Ullah A., Munir S., Badshah S.L., Khan N., Ghani L., Poulson B.G., Emwas A.H., Jaremko M. Important Flavonoids and Their Role as a Therapeutic Agent. Molecules. 2020;25:5243.
  10. Deepika Maurya P.K. Health Benefits of Quercetin in Age-Related Diseases. Molecules. 2022;27:2498.
  11. Mamun A.A., Sufian M.A., Uddin Md.S., Sumsuzzman D.M., Jeandet P., Islam M.S., Zhang H.J., Kong A.N., Sarwar Md.Sh. Exploring the role of senescence inducers and senotherapeutics as targets for anticancer natural products. European Journal of Pharmacology. 2022;928:174991.
  12. Aghababaei F., Hadidi M. Recent Advances in Potential Health Benefits of Quercetin. Pharmaceuticals. 2023;16:1020.
  13. 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. Bioorganic & Medicinal Chemistry. 2005;13:433–41.
  14. Alelign T., Debella A., Petros B. Evaluations of Antioxidant Effects of Selected Medicinal Plant Extracts Claimed to Treat Kidney Stone Disease. Free Radic Antioxid. 2021;10:63–8.
  15.  
90
 
  • Rao F., Yuting Zh., Yiran G., Fang Ch. Antioxidant and tyrosinase inhibition activities of the ethanol-insoluble fraction of water extract of Sapium sebiferum (L.) Roxb. leaves. South African Journal of Botany. 2014;93:98–104.
  1. Basit H., Godse K.V., Al Aboud A.M. Melasma. StatPearls [Internet]. In: Treasure Island (FL): StatPearls Publishing; 2025. Accessed April 19, 2025. Available from: http://www.ncbi.nlm.nih.gov/books/NBK459271/
  2. Praetorius C., Sturm R.A., Steingrimsson E. Sun‐induced freckling: ephelides and solar lentigines. Pigment Cell & Melanoma Research. 2014;27:339–50.
  3. Lawrence E., Syed H.A., Al Aboud K.M. Postinflammatory Hyperpigmentation. In: StatPearls [Internet]. Treasure Island (FL): StatPearls Publishing; 2025. Accessed April 19, 2025. Available from: http://www.ncbi.nlm.nih.gov/books/NBK559150/
  4. Patil S., Srinivas S., Jadhav J. Evaluation of crocin and curcumin affinity on mushroom tyrosinase using surface plasmon resonance. International Journal of Biological Macromolecules. 2014;65:163–6.
  5. Fan M., Zhang G., Hu X., Xu X., Gong D. Quercetin as a tyrosinase inhibitor: Inhibitory activity, conformational change and mechanism. Food Research International. 2017;100:226–33.
  6. Şahin İ., Bingöl Z., Onur S., Güngör S.A., Köse M., Gülçin İ., Tümer F. Enzyme Inhibition Properties and Molecular Docking Studies of 4‐Sulfonate Containing Aryl α‐Hydroxyphosphonates Based Hybrid Molecules. Chemistry & Biodiversity. 2022;19:e202100787.
  7. Schlessinger D.I., Anoruo M., Schlessinger J. Biochemistry, Melanin. In: StatPearls [Internet]. Treasure Island (FL): StatPearls Publishing; 2025. Accessed April 19, 2025. Available from: http://www.ncbi.nlm.nih.gov/books/NBK459156/
  8. Strelow J., Dewe W., Iversen P.W., Brooks H.B,. Radding J.A., McGee J., et al. Mechanism of Action Assays for Enzymes. In: Markossian S, Grossman A., Baskir H., Arkin M., Auld D., Austin C., et al., In: Assay Guid Man [Internet]. Bethesda (MD): Eli Lilly & Company and the National Center for Advancing Translational Sciences; 2004. Accessed April 19, 2025. Available from: http://www.ncbi.nlm.nih.gov/books/NBK92001/
  9. Dhiman N., Kharkwal H. Biosynthesis and Derivatization of the Major Phytoconstituents of Saffron. In: Saffron [Internet]. Elsevier; 2020; 83–92. Accessed April 19, 2025. Available from: https://linkinghub.elsevier.com/retrieve/pii/B9780128184622000073
  10. Magar R.T., Sohng J.K. A Review on Structure, Modifications and Structure-Activity Relation of Quercetin and Its Derivatives. Journal Microbiology Biotechnology. 2020;30:11–20.
  11. Hire R.R., Srivastava S., Davis M.B., Kumar Konreddy A., Panda D. Antiproliferative Activity of Crocin Involves Targeting of Microtubules in Breast Cancer Cells. Scientific Reports. 2017;7:44984.
  12. Aykul S., Martinez-Hackert E. Determination of half-maximal inhibitory concentration using biosensor-based protein interaction analysis. Analytical Biochemistry. 2016;508:97–103.
  13. Li C-Y., Wu T-S. Constituents of the Stigmas of Crocus sativus and Their Tyrosinase Inhibitory Activity. Journal of Natural Products. 2002;65:1452–6.
  14. Arung E.T., Wijaya Kusuma I., Shimizu K., Kondo R. Tyrosinase inhibitory effect of Quercetin 4′- O -β- D -glucopyranoside from dried skin of red onion (Allium cepa). Natural Product Research. 2011;25:256–63.
  15. Chen X., McClements D.J., Zhu Y., Chen Y., Zou L., Liu W., Cheng C., Fu D., Liu CH. Enhancement of the solubility, stability and bioaccessibility of Quercetin using protein-based excipient emulsions. Food Research International. 2018;114:30–7.
  16. Rossi M., Rickles L.F., Halpin W.A. The crystal and molecular structure of Quercetin: A biologically active and naturally occurring flavonoid. Bioorganic Chemistry. 1986;14:55–69.
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