An Integrated Study of Tyrosinase Inhibition by Rutin: Progress using a Computational Simulation

TLDR: The strategy of predicting tyrosinase inhibition based on hydroxyl group number and computational simulation may prove useful for the screening of potential tyrosIn inhibition studies and rutin has the potential to be a potent antipigment agent.

Abstract: Tyrosinase inhibition studies have recently gained the attention of researchers due to their potential application values We simulated docking (binding energies for AutoDock Vina: -91 kcal/mol) and performed a molecular dynamics simulation to verify docking results between tyrosinase and rutin The docking results suggest that rutin mostly interacts with histidine residues located in the active site A 10 ns molecular dynamics simulation showed that one copper ion at the tyrosinase active site was responsible for the interaction with rutin Kinetic analyses showed that rutin-mediated inactivation followed a first-order reaction and mono- and biphasic rate constants occurred with rutin The inhibition was a typical competitive type with K(i) = 110±025 mM Measurements of intrinsic and ANS-binding fluorescences showed that rutin showed a relatively strong binding affinity for tyrosinase and one possible binding site that could be a copper was detected accompanying with a hydrophobic exposure of tyrosinase Cell viability testing with rutin in HaCaT keratinocytes showed that no toxic effects were produced Taken together, rutin has the potential to be a potent anti-pigment agent The strategy of predicting tyrosinase inhibition based on hydroxyl group number and computational simulation may prove useful for the screening of potential tyrosinase inhibitors