Toward the inhibitory effect of acetylsalicylic acid on tyrosinase: Integrating kinetics studies and computational simulations

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Title
Toward the inhibitory effect of acetylsalicylic acid on tyrosinase: Integrating kinetics studies and computational simulations
Author(s)
Z J Wang; Jinhyuk Lee; Y X Si; Sang Ho Oh; J M Yang; D Shen; G Y Qian; S J Yin
Bibliographic Citation
Process Biochemistry, vol. 48, no. 2, pp. 260-266
Publication Year
2013
Abstract
Acetylsalicylic acid (ASA), generally well known as aspirin, has various biomedical functions. In this study, we revealed that ASA reversibly inhibits tyrosinase (EC 1.14.18.1) in a mixed-type manner with a Ki = 11.778 ± 2.01 mM. Time-interval kinetics showed that the inhibition followed first-order reaction kinetics. Measurements of ANS-binding fluorescence showed that ASA did not induce significant detectable changes in the hydrophobic surface of tyrosinase. For further insight, we performed molecular dynamics simulations to predict the key interactions between tyrosinase and ASA and found that the acetate and carboxylic acid groups of ASA play a critical role in binding to several residues (HIS61, HIS85, HIS94, HIS259, HIS263, and ALA286) on tyrosinase that are thought to be pivotal for docking. Our study suggested that ASA could be a useful depigmentation agent due to the structural functions of the acetic and carboxyl groups on tyrosinase.
Keyword
Acetylsalicylic acidDocking simulationInhibitionKineticsMolecular dynamicsTyrosinase
ISSN
0032-9592
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.procbio.2012.12.019
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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