Nine novel mono-oxime reactivators bearing xylene linker were synthesized in an effort to
improve previously prepared xylene bisoximes and monocarbamoyl-monooximes. The novel compounds
were tested in vitro on the model of tabun-, paraoxon-, methylparaoxon- and DFP-inhibited
human erythrocyte AChE. Their reactivation ability was compared to pralidoxime, asoxime, obidoxime and two previously
prepared xylene linked bisoximes (K107, K108). All compounds showed minimal reactivation of tabun-inhibited
AChE at selected concentration scale. This finding was explained by molecular modelling study. Bisoximes obidoxime
and K108 resulted as the best reactivators for paraoxon-, methylparaoxon- and DFP-inhibited AChE. The loss of nonoxime
moiety lead to the loss of reactivation ability within the novel compounds. Though the novel reactivators did not
exceed previously known compounds, they confirmed former SAR findings for xylene-linked AChE reactivators.
Keywords: Acetylcholinesterase, tabun, DFP, pesticide, reactivator, oxime, xylene linker.
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