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Reactivation of Acetylcholinesterase Inhibited by Organophosphates in Peripheral Rat Tissues

The aim of this study was to determine the ability of twenty novel substituted phenoxyalkyl pyridinium oximes to reactivate phosphylated acetylcholinesterase (AChE) in peripheral rat tissues, in vitro, inhibited by organophosphate anticholinesterase nerve agent surrogates. A sarin surrogate, phthalimidyl isopropyl methylphosphonate (PIMP), and a VX surrogate, 4-nitrophenyl ethyl methylphosphonate (NEMP), were used to inhibit AChE in skeletal muscle and serum samples. Reactivation of the widely used oxime 2-PAM was tested for comparison with the novel oximes. The novel oximes displayed a range of 23-102% reactivation of AChE in vitro across both tissue types. Most of the novel oximes tested in the present study demonstrated a higher percent reactivation of AChE, than 2-PAM. Therefore, these novel oximes have the potential to be effective antidotes used during the treatment of OP toxicity.

Identiferoai:union.ndltd.org:MSSTATE/oai:scholarsjunction.msstate.edu:td-4724
Date09 May 2015
CreatorsBennett, Joshua Peay
PublisherScholars Junction
Source SetsMississippi State University
Detected LanguageEnglish
Typetext
Formatapplication/pdf
SourceTheses and Dissertations

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