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Inhibitory effect of morin on tyrosinase: Insights from spectroscopic and molecular docking studies
- Wang, Yajie, Zhang, Guowen, Yan, Jiakai, Gong, Deming
- Food chemistry 2014 v.163 pp. 226-233
- L-dopa, active sites, binding sites, circular dichroism spectroscopy, flavonoids, humans, hydrogen bonding, melanin, molecular models, plant-based foods, skin diseases, van der Waals forces
- Tyrosinase is a key enzyme in the production of melanin in the human body, excessive accumulation of melanin can lead to skin disorders. Morin is an important bioactive flavonoid compound widely distributed in plants and foods of plant origin. In this study, the inhibitory kinetics of morin on tyrosinase and their binding mechanism were determined using spectroscopic and molecular docking techniques. The results indicate that morin reversibly inhibited tyrosinase in a competitive manner through a multi-phase kinetic process. Morin was found to bind to tyrosinase at a single binding site mainly by hydrogen bonds and van der Waals forces. Analysis of circular dichroism spectra revealed that the binding of morin to tyrosinase induced rearrangement and conformational changes of the enzyme. Moreover, molecular docking results suggested that morin competitively bound to the active site of tyrosinase with the substrate levodopa.