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

Cited 15 time in scopus
Metadata Downloads
Title
Inhibition of tyrosinase by gastrodin: An integrated kinetic-computational simulation analysis
Author(s)
C J Pei; Jinhyuk Lee; Y X Si; S Oh; W A Xu; S J Yin; G Y Qian; H Y Han
Bibliographic Citation
Process Biochemistry, vol. 48, no. 1, pp. 162-168
Publication Year
2013
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.
Keyword
Docking simulationGastrodinInhibition kineticsMolecular dynamicsTyrosinase
ISSN
0032-9592
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.procbio.2012.11.004
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.