Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 48, Issue 4, Pages 700-704Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijbiomac.2011.02.015
Keywords
Tyrosinase; Inhibition kinetics; Isophthalic acid; Hydroxyl group; Docking simulation
Funding
- Key Science and Technology Innovation Teams of Zhejiang Province from the Science and Technology Department of Zhejiang Province [2009R50031]
- Ministry of Health, Welfare and Family Affairs, Republic of Korea [01-PJ3-PG6-01GN12-0001, A030003]
- Zhejiang Provincial Natural Science Foundation of China [Y2091212]
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Using inhibition kinetics and computational simulation, we studied the reversible inhibition of tyrosinase by isophthalic acid (IPA). IPA inhibited tyrosinase in a complex manner with K-i = 17.8 +/- 1.8 mM. Measurements of intrinsic and ANS-binding fluorescence showed that IPA induced no changes in tertiary protein structure. For further insight, we predicted the 3D structure of tyrosinase and used a docking algorithm to simulate binding between tyrosinase and IPA. Simulation was successful (binding energies for Dock6.3: -25.19 kcal/mol and for AutoDock4.2: -4.28 kcal/mol), suggesting that IPA interacts with PRO175 or VAL190. This strategy of predicting tyrosinase inhibition based on hydroxyl group number and orientation may prove useful for the screening of potential tyrosinase inhibitors. (C) 2011 Elsevier B.V. All rights reserved.
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