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Molecules 2014, 19(7), 9591-9605; doi:10.3390/molecules19079591

Combined Kinetic Studies and Computational Analysis on Kojic Acid Analogs as Tyrosinase Inhibitors

1
Laboratório de Planejamento e Desenvolvimento de Fármacos, Instituto de Ciências Exatas e Naturais, Universidade Federal do Pará, 66075-110 Belém, PA, Brazil
2
Programa de Pós-Graduação em Biotecnologia, Universidade Federal do Pará, 66075-110 Belém, PA, Brazil
3
Laboratório de Neuroquímica Molecular e Celular, Instituto de Ciências Biológicas, Universidade Federal do Pará, 66075-110 Belém, PA, Brazil
4
Laboratório de Biologia Estrutural, Instituto de Ciências Biológicas, Universidade Federal do Pará, 66075-110 Belém, PA, Brazil
5
Instituto de Tecnologia, Universidade Federal do Pará, 66075-110 Belém, PA, Brazil
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Received: 6 June 2014 / Revised: 1 July 2014 / Accepted: 2 July 2014 / Published: 7 July 2014
(This article belongs to the Section Molecular Diversity)
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Abstract

Tyrosinase is a key enzyme in melanin synthesis and widely distributed in plants and animals tissues. In mammals, this enzyme is related to pigment production, involved in wound healing, primary immune response and it can also contribute to catecholamines synthesis in the brain. Consequently, tyrosinase enzyme represents an attractive and selective target in the field of the medicine, cosmetics and bio-insecticides. In this paper, experimental kinetics and computational analysis were used to study the inhibition of tyrosinase by analogous of Kojic acid. The main interactions occurring between inhibitors-tyrosinase complexes and the influence of divalent cation (Cu2+) in enzymatic inhibition were investigated by using molecular docking, molecular dynamic simulations and electrostatic binding free energy by using the Linear Interaction Energy (LIE) method. The results showed that the electrostatic binding free energy are correlated with values of constant inhibition (r2 = 0.97).Thus, the model obtained here could contribute to future studies of this important system and, therefore, eventually facilitate development of tyrosinase inhibitors. View Full-Text
Keywords: tyrosinase; kojic acid; kinetic assays; inhibition; molecular docking; molecular dynamics; binding free energy; LIE tyrosinase; kojic acid; kinetic assays; inhibition; molecular docking; molecular dynamics; binding free energy; LIE
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MDPI and ACS Style

Lima, C.R.; Silva, J.R.A.; de Tássia Carvalho Cardoso, É.; Silva, E.O.; Lameira, J.; do Nascimento, J.L.M.; do Socorro Barros Brasil, D.; Alves, C.N. Combined Kinetic Studies and Computational Analysis on Kojic Acid Analogs as Tyrosinase Inhibitors. Molecules 2014, 19, 9591-9605.

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