Effects of boldine on tyrosinase: Inhibition kinetics and computational simulation

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Title
Effects of boldine on tyrosinase: Inhibition kinetics and computational simulation
Author(s)
Y X Si; S Ji; W Wang; N Y Fang; Q X Jin; Y D Park; G Y Qian; Jinhyuk Lee; H Y Han; S J Yin
Bibliographic Citation
Process Biochemistry, vol. 48, no. 1, pp. 152-161
Publication Year
2013
Abstract
Boldine is one of the most potent natural antioxidants and displays some important pharmacological activities, such as cytoprotective and anti-inflammatory activities. Based on its antioxidant properties, we studied the effects of boldine on l-DOPA oxidation by evaluating the inhibitory kinetics and a computational simulation between boldine and tyrosinase. Boldine reversibly inhibited tyrosinase from mushroom (Agaricus bisporus) in a mixed-type manner, with a Ki = 7.203 ± 0.933 mM. To gain insight into the inactivation process, we computed the kinetics via time-interval measurements and continuous substrate reactions. The results indicated that the inactivation induced by boldine was a first-order reaction with biphasic processes and that the substrate can promote the inactivation process. To gain further insight, we performed computational docking and molecular dynamics simulations, and the results showed that boldine can interact with several residues near the tyrosinase active site. Our study provides insight into the inhibition of tyrosinase in response to alkaloids. Based on its tyrosinase-inhibiting effect and low toxicity, boldine is a potential natural anti-pigmentation agent.
Keyword
BoldineDocking simulationInhibition kineticsMixed-type inhibitorMolecular dynamicsPhenolic hydroxylTyrosinase
ISSN
0032-9592
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.procbio.2012.11.001
Type
Article
Appears in Collections:
Division of Biomedical Research > Genome Editing Research Center > 1. Journal Articles
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