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Title 

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

Authors 

C J PeiJinhyuk LeeY X SiS OhW A XuS J YinG Y QianH Y Han

Publisher 

Elsevier

Issue Date 

2013

Citation 

Process Biochemistry, vol. 48, no. 1, pp. 162-168

Keywords 

Docking simulationGastrodinInhibition kineticsMolecular dynamicsTyrosinase

Abstract 

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

ISSN 

0032-9592

Link 

http://dx.doi.org/10.1016/j.procbio.2012.11.004

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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