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Slight difference in the isomeric oximes K206 and K203 makes huge difference for the reactivation of organophosphorus-inhibited AChE: Theoretical and experimental aspects
DA. Polisel, AA. de Castro, DT. Mancini, EFF. da Cunha, TCC. França, TC. Ramalho, K. Kuca,
Jazyk angličtina Země Irsko
Typ dokumentu časopisecké články
- MeSH
- acetylcholinesterasa chemie metabolismus MeSH
- kvantová teorie MeSH
- myši MeSH
- nervová bojová látka chemie metabolismus MeSH
- organofosforové sloučeniny chemie metabolismus MeSH
- organothiofosforové sloučeniny chemie metabolismus MeSH
- oximy chemie MeSH
- racionální návrh léčiv MeSH
- reaktivátory cholinesterasy chemie metabolismus MeSH
- simulace molekulového dockingu MeSH
- termodynamika MeSH
- vazebná místa MeSH
- zvířata MeSH
- Check Tag
- myši MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
Studies with oximes have been extensively developed to design new reactivators with better efficiency, and greater spectrum of action. In this study, we aimed to analyze the influence of the Carbamoyl group position change in two isomeric oximes, K203 and K206, on the reactivation percentage of Mus musculus Acetylcholinesterase (MmAChE), inhibited by different nerve agents. Theoretical calculations were performed to assess the difference for the oxime activity with inhibited AChE-complexes and the factors that govern this difference. Comparing theoretical and experimental data, it is possible to observe that this change between the oximes results in different reactivation percentage for the same nerve agent, due to the different interaction modes and activation energy for the studied systems.
Biomedical Research Center University Hospital Hradec Kralove Hradec Kralove Czech Republic
Department of Chemistry Federal University of Lavras Lavras Brazil
Citace poskytuje Crossref.org
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- $a Slight difference in the isomeric oximes K206 and K203 makes huge difference for the reactivation of organophosphorus-inhibited AChE: Theoretical and experimental aspects / $c DA. Polisel, AA. de Castro, DT. Mancini, EFF. da Cunha, TCC. França, TC. Ramalho, K. Kuca,
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- $a Studies with oximes have been extensively developed to design new reactivators with better efficiency, and greater spectrum of action. In this study, we aimed to analyze the influence of the Carbamoyl group position change in two isomeric oximes, K203 and K206, on the reactivation percentage of Mus musculus Acetylcholinesterase (MmAChE), inhibited by different nerve agents. Theoretical calculations were performed to assess the difference for the oxime activity with inhibited AChE-complexes and the factors that govern this difference. Comparing theoretical and experimental data, it is possible to observe that this change between the oximes results in different reactivation percentage for the same nerve agent, due to the different interaction modes and activation energy for the studied systems.
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