Reactivationof Acetylcholinesterase Inhibited by Organophosphates in Peripheral Rat Tissues
Date of Degree
Original embargo terms
MSU Only Indefinitely
Graduate Thesis - Open Access
Master of Science
College of Veterinary Medicine
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.
Bennett, Joshua Peay, "Reactivationof Acetylcholinesterase Inhibited by Organophosphates in Peripheral Rat Tissues" (2015). Theses and Dissertations MSU. 3725.