Inhibition of tyrosinase by gastrodin: An integrated kinetic-computational simulation analysis

摘要: Abstract We studied the inhibitory effect of gastrodin on tyrosinase using inhibition kinetics and computational simulation. Gastrodin reversibly inhibited in a mixed-type manner with K i  = 123.8 ± 20.2 mM. Time-interval revealed to be first-order process mono- bi-phasic components. Using AutoDock Vina, we calculated binding energy −6.3 kcal/mol for tyrosinase, performed molecular dynamics simulation tyrosinase–gastrodin interaction. The results suggested that interacts primarily histidine residues active site. A 10-ns showed one copper ion site was responsible interaction gastrodin. Our study provides insight into by hydroxyl groups combination calculations may help confirm action define mechanisms inhibition.