Alteração - Atendimento do Repositório Institucionalclique aqui para acessar a portaria
Please use this identifier to cite or link to this item:
|metadata.artigo.dc.title:||Asymmetric biocatalysis of the nerve agent VX by human serum paraoxonase 1: molecular docking and reaction mechanism calculations|
Castro, Alexandre A. de
Ramalho, Teodorico C.
Giacoppo, Juliana O. S.
Mancini, Daiana T.
Caetano, Melissa S.
Cunha, Elaine F. F. da
Modelagem de homologia
|metadata.artigo.dc.identifier.citation:||SARTORELLI, 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.|
|metadata.artigo.dc.description.abstract:||Organophosphorus 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.|
|Appears in Collections:||DQI - Artigos publicados em periódicos|
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.