Synthesis, human monoamine oxidase inhibitory activity and molecular docking studies of 3-heteroarylcoumarin derivatives.
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Delogu G, Picciau C, Ferino G, Quezada E, Podda G, Uriarte E, Vina D
Synthesis, human monoamine oxidase inhibitory activity and molecular docking studies of 3-heteroarylcoumarin derivatives.
Eur J Med Chem. 2011 Apr;46(4):1147-52. doi: 10.1016/j.ejmech.2011.01.033. Epub 2011 Jan 28.
- PubMed ID
- 21316817 [ View in PubMed]
- Abstract
Monoamine oxidase (MAO) is an important drug target for the treatment of neurological disorders. Series of 3-indolyl and 3-thiophenylcoumarins were synthesized and evaluated as inhibitors of the two human MAO isoforms, hMAO-A and hMAO-B. In general, the derivatives were found to be selective hMAO-B inhibitors with IC(50) values in the nanoMolar (nM) to microMolar (muM) range. Docking experiments were carried out in order to compare the theoretical and experimental affinity of these compounds to the hMAO-B protein. According to our results, docking experiments could be an interesting approach to try to predict the activity of this class of coumarins against MAO-B receptors.
DrugBank Data that Cites this Article
- Binding Properties
Drug Target Property Measurement pH Temperature (°C) Iproniazid Amine oxidase [flavin-containing] B IC 50 (nM) 7540 N/A N/A Details Selegiline Amine oxidase [flavin-containing] A IC 50 (nM) 67250 N/A N/A Details Selegiline Amine oxidase [flavin-containing] B IC 50 (nM) 14.8 N/A N/A Details