Combined kinetic studies and computational analysis on kojic acid analogous as tyrosinase inhibitors. 2014

Carlyle Ribeiro Lima, and José Rogério A Silva, and Erica de Tássia Carvalho Cardoso, and Edilene O Silva, and Jerônimo Lameira, and José Luiz Martins do Nascimento, and Davi do Socorro Barros Brasil, and Cláudio N Alves
Laboratório de Planejamento e Desenvolvimento de Fármacos, Instituto de Ciências Exatas e Naturais, Universidade Federal do Pará, 66075-110 Belém, PA, Brazil. carlylelima@hotmail.com.

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.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D011753 Pyrones Keto-pyrans.
D014442 Monophenol Monooxygenase An enzyme of the oxidoreductase class that catalyzes the reaction between L-tyrosine, L-dopa, and oxygen to yield L-dopa, dopaquinone, and water. It is a copper protein that acts also on catechols, catalyzing some of the same reactions as CATECHOL OXIDASE. EC 1.14.18.1. Dopa Oxidase,Phenoloxidase,Tyrosinase,Cresolase,Phenol Oxidase,Phenoloxidase A,Phenoloxidase B,Monooxygenase, Monophenol,Oxidase, Dopa,Oxidase, Phenol
D056004 Molecular Dynamics Simulation A computer simulation developed to study the motion of molecules over a period of time. Molecular Dynamics Simulations,Molecular Dynamics,Dynamic, Molecular,Dynamics Simulation, Molecular,Dynamics Simulations, Molecular,Dynamics, Molecular,Molecular Dynamic,Simulation, Molecular Dynamics,Simulations, Molecular Dynamics
D062105 Molecular Docking Simulation A computer simulation technique that is used to model the interaction between two molecules. Typically the docking simulation measures the interactions of a small molecule or ligand with a part of a larger molecule such as a protein. Molecular Docking,Molecular Docking Simulations,Molecular Docking Analysis,Analysis, Molecular Docking,Docking Analysis, Molecular,Docking Simulation, Molecular,Docking, Molecular,Molecular Docking Analyses,Molecular Dockings,Simulation, Molecular Docking
D020134 Catalytic Domain The region of an enzyme that interacts with its substrate to cause the enzymatic reaction. Active Site,Catalytic Core,Catalytic Region,Catalytic Site,Catalytic Subunit,Reactive Site,Active Sites,Catalytic Cores,Catalytic Domains,Catalytic Regions,Catalytic Sites,Catalytic Subunits,Core, Catalytic,Cores, Catalytic,Domain, Catalytic,Domains, Catalytic,Reactive Sites,Region, Catalytic,Regions, Catalytic,Site, Active,Site, Catalytic,Site, Reactive,Sites, Active,Sites, Catalytic,Sites, Reactive,Subunit, Catalytic,Subunits, Catalytic

Related Publications

Carlyle Ribeiro Lima, and José Rogério A Silva, and Erica de Tássia Carvalho Cardoso, and Edilene O Silva, and Jerônimo Lameira, and José Luiz Martins do Nascimento, and Davi do Socorro Barros Brasil, and Cláudio N Alves
October 2015, Bioorganic & medicinal chemistry letters,
Carlyle Ribeiro Lima, and José Rogério A Silva, and Erica de Tássia Carvalho Cardoso, and Edilene O Silva, and Jerônimo Lameira, and José Luiz Martins do Nascimento, and Davi do Socorro Barros Brasil, and Cláudio N Alves
October 2009, Bioorganic & medicinal chemistry letters,
Carlyle Ribeiro Lima, and José Rogério A Silva, and Erica de Tássia Carvalho Cardoso, and Edilene O Silva, and Jerônimo Lameira, and José Luiz Martins do Nascimento, and Davi do Socorro Barros Brasil, and Cláudio N Alves
November 2022, Molecules (Basel, Switzerland),
Carlyle Ribeiro Lima, and José Rogério A Silva, and Erica de Tássia Carvalho Cardoso, and Edilene O Silva, and Jerônimo Lameira, and José Luiz Martins do Nascimento, and Davi do Socorro Barros Brasil, and Cláudio N Alves
September 2020, European journal of medicinal chemistry,
Carlyle Ribeiro Lima, and José Rogério A Silva, and Erica de Tássia Carvalho Cardoso, and Edilene O Silva, and Jerônimo Lameira, and José Luiz Martins do Nascimento, and Davi do Socorro Barros Brasil, and Cláudio N Alves
December 2019, Journal of enzyme inhibition and medicinal chemistry,
Carlyle Ribeiro Lima, and José Rogério A Silva, and Erica de Tássia Carvalho Cardoso, and Edilene O Silva, and Jerônimo Lameira, and José Luiz Martins do Nascimento, and Davi do Socorro Barros Brasil, and Cláudio N Alves
October 2015, IUBMB life,
Carlyle Ribeiro Lima, and José Rogério A Silva, and Erica de Tássia Carvalho Cardoso, and Edilene O Silva, and Jerônimo Lameira, and José Luiz Martins do Nascimento, and Davi do Socorro Barros Brasil, and Cláudio N Alves
July 2019, Bioorganic chemistry,
Carlyle Ribeiro Lima, and José Rogério A Silva, and Erica de Tássia Carvalho Cardoso, and Edilene O Silva, and Jerônimo Lameira, and José Luiz Martins do Nascimento, and Davi do Socorro Barros Brasil, and Cláudio N Alves
May 2021, Molecules (Basel, Switzerland),
Carlyle Ribeiro Lima, and José Rogério A Silva, and Erica de Tássia Carvalho Cardoso, and Edilene O Silva, and Jerônimo Lameira, and José Luiz Martins do Nascimento, and Davi do Socorro Barros Brasil, and Cláudio N Alves
November 2021, Molecular diversity,
Carlyle Ribeiro Lima, and José Rogério A Silva, and Erica de Tássia Carvalho Cardoso, and Edilene O Silva, and Jerônimo Lameira, and José Luiz Martins do Nascimento, and Davi do Socorro Barros Brasil, and Cláudio N Alves
July 2019, Chemistry & biodiversity,
Copied contents to your clipboard!