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- Title
Combined Kinetic Studies and Computational Analysis on Kojic Acid Analogs as Tyrosinase Inhibitors.
- Authors
Ribeiro Lima, Carlyle; Silva, José Rogério A.; de Tássia Carvalho Cardoso, Érica; Silva, Edilene O.; Lameira, Jerônimo; Martins do Nascimento, José Luiz; do Socorro Barros Brasil, Davi; Alves, Cláudio N.
- 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 analogs 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.
- Subjects
PHENOL oxidase; CATIONS; MOLECULAR docking; FREE energy (Thermodynamics); MOLECULAR dynamics
- Publication
Molecules, 2014, Vol 19, Issue 7, p9591
- ISSN
1420-3049
- Publication type
Article
- DOI
10.3390/molecules19079591