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Title 

The effect of validamycin A on tyrosinase: Inhibition kinetics and computational simulation

Authors 

Z J WangS JiY X SiJ M YangG Y QianJinhyuk LeeS J Yin

Publisher 

Elsevier

Issue Date 

2013

Citation 

International Journal of Biological Macromolecules, vol. 55, no. 0, pp. 15-23

Keywords 

Docking simulationInhibition kineticsMolecular dynamicsTyrosinaseValidamycin A

Abstract 

In this study, we investigated validamycin A as a tyrosinase inhibitor based on its structural properties. We found that the reversible inhibition of tyrosinase by validamycin A occurred in a mixed-type manner with Ki=5.893±0.038mM, as determined by integrating kinetics studies and computational simulations. Time-interval tyrosinase studies showed that the inhibition followed first-order kinetics with two phases. Fluorescence measurements of ANS binding showed that validamycin A induced changes in the tertiary protein structure of tyrosinase. To obtain further insight, computational docking and molecular dynamics were applied, and the results indicated that HIS85, HIS244, GLU256, HIS259, and ASN260 of tyrosinase interacted with validamycin A. This strategy of predicting tyrosinase inhibition based on hydroxyl group numbers might be useful in the design and screening of potential tyrosinase inhibitors.

ISSN 

0141-8130

Link 

http://dx.doi.org/10.1016/j.ijbiomac.2012.12.040

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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