Structural analysis and molecular docking of trypanocidal aryloxy-quinones in trypanothione and glutathione reductases: a comparison with biochemical data
作者： Brenda Vera , Karina Vázquez , Carolina Mascayano , Ricardo A. Tapia , Victoria Espinosa
DOI: 10.1080/07391102.2016.1195283
关键词:
摘要: A set of aryloxy-quinones, previously synthesized and evaluated against Trypanosoma cruzi epimastigotes cultures, were found more potent selective than nifurtimox. One the possible mechanisms trypanocidal activity these quinones could be inhibition trypanothione reductase (TR). Considering that glutathione (GR) is equivalent TR in humans, biochemical, kinetic, molecular docking studies GR envisaged compared with cytotoxic data a aryloxy-quinones. Biochemical assays indicated three naphthoquinones (Nq-h, Nq-g, Nq-d) selectively inhibit kinetic analyses Nq-h noncompetitive mechanism. Molecular dockings performed following putative binding sites: catalytic site, dimer interface, nicotinamide adenine dinucleotide phosphate-binding site. In GR, aryloxy-quinones to exhibit high affinity for site nea...
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