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dc.creatorCastro, Alexandre A. de-
dc.creatorSoares, Flávia Villela-
dc.creatorPereira, Ander Francisco-
dc.creatorSilva, Telles Cardoso-
dc.creatorSilva, Daniela Rodrigues-
dc.creatorMancini, Daiana Teixeira-
dc.creatorCaetano, Melissa Soares-
dc.creatorCunha, Elaine F. F. da-
dc.creatorRamalho, Teodorico C.-
dc.date.accessioned2020-04-08T17:24:15Z-
dc.date.available2020-04-08T17:24:15Z-
dc.date.issued2019-
dc.identifier.citationCASTRO, A. A. de et al. Asymmetric biodegradation of the nerve agents Sarin and VX by human dUTPase: chemometrics, molecular docking and hybrid QM/MM calculations. Journal of Biomolecular Structure and Dynamics, New York, v. 37, n. 8, p. 2154-2164, 2019.pt_BR
dc.identifier.urihttps://www.tandfonline.com/doi/abs/10.1080/07391102.2018.1478751?journalCode=tbsd20pt_BR
dc.identifier.urihttp://repositorio.ufla.br/jspui/handle/1/39892-
dc.description.abstractOrganophosphorus compounds (OP) nerve agents are among the most toxic chemical substances known. Their toxicity is due to their ability to bind to acetylcholinesterase. Currently, some enzymes, such as phosphotriesterase, human serum paraoxonase 1 and diisopropyl fluorophosphatase, capable of degrading OP, have been characterized. Regarding the importance of bioremediation methods for detoxication of OP, this work aims to study the interaction modes between the human human deoxyuridine triphosphate nucleotidohydrolase (dUTPase) and Sarin and VX, considering their Rp and Sp enantiomers, to evaluate the asymmetric catalysis of those compounds. In previous work, this enzyme has shown good potential to degrade phosphotriesters, and based on this characteristic, we have applied the human dUTPase to the OP degradation. Molecular docking, chemometrics and mixed quantum and molecular mechanics calculations have been employed, showing a good interaction between dUTPase and OP. Two possible reaction mechanisms were tested, and according to our theoretical results, the catalytic degradation of OP by dUTPase can take place via both mechanisms, beyond being stereoselective, that is, dUTPase cleaves one enantiomer preferentially in relation to other. Chemometric techniques provided excellent assistance for performing this theoretical investigation. The dUTPase study shows importance by the fact of it being a human enzyme.pt_BR
dc.languageen_USpt_BR
dc.publisherTaylor & Francispt_BR
dc.rightsrestrictAccesspt_BR
dc.sourceJournal of Biomolecular Structure and Dynamicspt_BR
dc.subjectOrganophosphorus compoundspt_BR
dc.subjectMolecular dockingpt_BR
dc.subjectChemometricspt_BR
dc.subjectCompostos organofosforadospt_BR
dc.subjectQuimiometriapt_BR
dc.titleAsymmetric biodegradation of the nerve agents Sarin and VX by human dUTPase: chemometrics, molecular docking and hybrid QM/MM calculationspt_BR
dc.typeArtigopt_BR
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