Inhibitory activity and mechanism of trilobatin on tyrosinase: kinetics, interaction mechanism and molecular docking
Shuyan Yu, Ming He, Yuhan Zhai, Zhike Xie, Shuo Xu, Shaoxuan Yu, Haifang Xiao, Yuanda Song
Abstract
. The intrinsic fluorescence of tyrosinase was quenched by trilobatin through a static quenching mechanism. Different spectroscopic measurements demonstrated that trilobatin could change the microenvironments and conformation of tyrosinase and molecular docking determined the binding site of quercetin on tyrosinase.
Topics & Concepts
TyrosinaseKineticsMechanism (biology)ChemistryDocking (animal)BiophysicsInhibitory postsynaptic potentialStereochemistryBiochemistryEnzymeBiologyPhilosophyNeurosciencePhysicsQuantum mechanicsEpistemologyMedicineNursingmelanin and skin pigmentationBiochemical Analysis and Sensing TechniquesPhytochemicals and Antioxidant Activities