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J Mol Model. 2012 Aug;18(8):3877-86. doi: 10.1007/s00894-012-1390-7. Epub 2012 Mar 17.

Targeting imidazoline site on monoamine oxidase B through molecular docking simulations.

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Faculdade de Biociências, Laboratório de Bioquímica Estrutural (LaBioQuest), Pontifícia Universidade Católica do Rio Grande do Sul, (PUCRS), Av. Ipiranga 6681, Porto Alegre, RS, 90619-900, Brazil.


Monoamine oxidase (MAO) is an enzyme of major importance in neurochemistry, because it catalyzes the inactivation pathway for the catecholamine neurotransmitters, noradrenaline, adrenaline and dopamine. In the last decade it was demonstrated that imidazoline derivatives were able to inhibit MAO activity. Furthermore, crystallographic studies identified the imidazoline-binding domain on monoamine oxidase B (MAO-B), which opens the possibility of molecular docking studies focused on this binding site. The goal of the present study is to identify new potential inhibitors for MAO-B. In addition, we are also interested in establishing a fast and reliable computation methodology to pave the way for future molecular docking simulations focused on the imidazoline-binding site of this enzyme. We used the program 'molegro virtual docker' (MVD) in all simulations described here. All results indicate that simplex evolution algorithm is able to succesfully simulate the protein-ligand interactions for MAO-B. In addition, a scoring function implemented in the program MVD presents high correlation coefficient with experimental activity of MAO-B inhibitors. Taken together, our results identified a new family of potential MAO-B inhibitors and mapped important residues for intermolecular interactions between this enzyme and ligands.

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