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dc.creatorSartorelli, Jaqueline-
dc.creatorCastro, Alexandre A. de-
dc.creatorRamalho, Teodorico C.-
dc.creatorGiacoppo, Juliana O. S.-
dc.creatorMancini, Daiana T.-
dc.creatorCaetano, Melissa S.-
dc.creatorCunha, Elaine F. F. da-
dc.date.accessioned2018-07-13T13:41:35Z-
dc.date.available2018-07-13T13:41:35Z-
dc.date.issued2016-11-
dc.identifier.citationSARTORELLI, J. et al. Asymmetric biocatalysis of the nerve agent VX by human serum paraoxonase 1: molecular docking and reaction mechanism calculations. Medicinal Chemistry Research, Cambridge, v. 25, n. 11, p. 2521-2533, Nov. 2016.pt_BR
dc.identifier.urihttps://link.springer.com/article/10.1007/s00044-016-1704-xpt_BR
dc.identifier.urihttp://repositorio.ufla.br/jspui/handle/1/29636-
dc.description.abstractOrganophosphorus compounds have been employed in agricultural activity for a long time, causing serious public health problems. Due to their toxic properties, these compounds have also been used as chemical weapons. In view of this scenario, the catalytic degradation and the development of bioremediation processes of organophosphorus compounds have been of wide interest. Among several enzymes capable of degrading organophosphorus compounds, the human serum paraoxonase 1 has shown good potential for this purpose. To evaluate the interaction mode between the human serum paraoxonase 1 (wild-type and mutants) enzymes and the VX compound, one of the most toxic organophosphorus compounds known, molecular docking calculations were conducted. In addition, seeking to analyze the reaction pathway and the stereochemistry preference by human serum paraoxonase 1 and the R p and S p enantiomers of VX, quantum mechanical/molecular mechanics calculations were performed. Our theoretical findings put in evidence that the wild-type and mutant human serum paraoxonase 1 enzymes strongly interact with VX. Moreover, with the quantum mechanical/molecular mechanics study, we observed that the human serum paraoxonase 1 preferentially degrades one enantiomer in relation to the other. The current results indicate key points for designing new, more efficient mutant human serum paraoxonase 1 enzymes for VX degradation.pt_BR
dc.languageen_USpt_BR
dc.publisherSpringerpt_BR
dc.rightsrestrictAccesspt_BR
dc.sourceMedicinal Chemistry Researchpt_BR
dc.subjectOrganophosphorus compoundspt_BR
dc.subjectHomology modelingpt_BR
dc.subjectMolecular dockingpt_BR
dc.subjectCompostos organofosforadospt_BR
dc.subjectModelagem de homologiapt_BR
dc.subjectDocagem molecularpt_BR
dc.titleAsymmetric biocatalysis of the nerve agent VX by human serum paraoxonase 1: molecular docking and reaction mechanism calculationspt_BR
dc.typeArtigopt_BR
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