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 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, 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.
Kuca
Kamil
K
Faculty of Military Health Sciences, University of Defence, Hradec Kralove, Czech Republic. kucakam@pmfhk.cz
Musilova
Lucie
L
Palecek
Jiri
J
Cirkva
Vladimir
V
Paar
Martin
M
Musilek
Kamil
K
Hrabinova
Martina
M
Pohanka
Miroslav
M
Karasova
Jana Zdarova
JZ
Jun
Daniel
D
D000110:Acetylcholinesterase / Q000187:drug effects* / Q000378:metabolism; D002091:Butyrylcholinesterase / Q000187:drug effects* / Q000378:metabolism; D004793:Enzyme Reactivators / Q000494:pharmacology*; D009682:Magnetic Resonance Spectroscopy; D010091:Oximes / Q000737:chemistry*; D010261:Paraoxon / Q000494:pharmacology*
D004793:Enzyme Reactivators; D010091:Oximes; D000110:Acetylcholinesterase; D002091:Butyrylcholinesterase; D010261:Paraoxon