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

Paper ID Volume ID Publish Year Pages File Format Full-Text
34860 45052 2013 7 PDF Available
Title
Inhibition of tyrosinase by gastrodin: An integrated kinetic-computational simulation analysis
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.

Keywords
Docking simulation; Gastrodin; Molecular dynamics; Inhibition kinetics; Tyrosinasel-DOPA, 3,4-dihydroxyphenylalanine; ns, nano-second; MD, molecular dynamics
First Page Preview
Inhibition of tyrosinase by gastrodin: An integrated kinetic-computational simulation analysis
Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 48, Issue 1, January 2013, Pages 162–168
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering