Experimental hydrophilic reactivator: bisoxime with three positive charges

Abstract

Within this study, experimental hydrophilic acetylcholinesterase (AChE) reactivator was evaluated in vitro against selected nerve agents (cyclosarin, tabun, sarin, VX agent). High hydrophilicity of the reactivator is caused by the presence of three positive charges in its molecule. Quaternary moiety involved in the connecting chain can influence linker’s interaction with the inner of the AChE. For the detailed description of reactivator-AChE interaction, docking studies were performed on theoretical models constructed from the chrystallographic structure of Mus musculus AChE (MmAChE).