Acetylcholinesterase and Butyrylcholinesterase Inhibited by Paraoxon

0333208 - ÚCHP 2011 RIV CH eng J - Článek v odborném periodiku
Kuča, K. - Musilová, L. - Paleček, J. - Církva, Vladimír - Paar, M. - Musílek, K. - Hrabinová, M. - Pohanka, M. - Zdarová Karasová, J. - Jun, D.
Acetylcholinesterase and Butyrylcholinesterase Inhibited by Paraoxon.
Molecules. Roč. 14, č. 12 (2009), s. 4915-4921. E-ISSN 1420-3049
Grant ostatní: MO0(CZ) FZV0000604
Výzkumný záměr: CEZ:AV0Z40720504
Klíčová slova: acetylcholinesterase * reactivator * oxime
Kód oboru RIV: CC - Organická chemie
Impakt faktor: 1.738, rok: 2009

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 butyrylcholinesterase (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. In case of BuChE reactivation, two compounds (K053 and K068) achieved similar results as obidoxime.
Trvalý link: http://hdl.handle.net/11104/0178252