Novel Bisquaternary Oximes—Reactivation of Acetylcholinesterase and Butyrylcholinesterase Inhibited by Paraoxon

Four novel bisquaternary aldoxime cholinesterase reactivators differing in their chemical structure were prepared. Afterwards, their biological activity was evaluated for their ability to reactivate acetylcholinesterase (AChE; EC 3.1.1.7) and butyryl-cholinesterase (BuChE; EC 3.1.1.8) inhibited by p...

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Detalles Bibliográficos
Autores principales: Kuca, Kamil, Musilova, Lucie, Palecek, Jiri, Cirkva, Vladimir, Paar, Martin, Musilek, Kamil, Hrabinova, Martina, Pohanka, Miroslav, Karasova, Jana Zdarova, Jun, Daniel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International 2009
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6255039/
https://www.ncbi.nlm.nih.gov/pubmed/20032868
http://dx.doi.org/10.3390/molecules14124915
Descripción
Sumario:Four novel bisquaternary aldoxime cholinesterase reactivators differing in their chemical structure were prepared. Afterwards, their biological activity was evaluated for their ability to reactivate acetylcholinesterase (AChE; EC 3.1.1.7) and butyryl-cholinesterase (BuChE; EC 3.1.1.8) inhibited by paraoxon. Their reactivation activity was compared with standard reactivators—pralidoxime, obidoxime and HI-6—which are clinically used at present. As it resulted, none of the prepared compounds surpassed obidoxime, which is considered to be the most potent compound if used for reactivation of AChE inhibited by paraoxon. In case of BuChE reactivation, two compounds (K053 and K068) achieved similar results as obidoxime.

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