Slight difference in the isomeric oximes K206 and K203 makes huge difference for the reactivation of organophosphorus-inhibited AChE: Theoretical and experimental aspects
| Autor: | Teodorico C. Ramalho, Elaine F.F. da Cunha, Daniel A. Polisel, Alexandre A. de Castro, Daiana T. Mancini, Kamil Kuca, Tanos C. C. França |
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| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Cholinesterase Reactivators Aché Toxicology Medicinal chemistry Mice 03 medical and health sciences chemistry.chemical_compound Organophosphorus Compounds 0302 clinical medicine Oximes medicine Animals Nerve agent Binding Sites Organothiophosphorus Compounds General Medicine Oxime Acetylcholinesterase language.human_language Molecular Docking Simulation 030104 developmental biology chemistry Drug Design 030220 oncology & carcinogenesis language Quantum Theory Thermodynamics Nerve Agents medicine.drug |
| Zdroj: | Chemico-Biological Interactions. 309:108671 |
| ISSN: | 0009-2797 |
| DOI: | 10.1016/j.cbi.2019.05.037 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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