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Updated: May 2, 2026

Preparation and In Vivo Use of an Activity-based Probe for N-acylethanolamine Acid Amidase
Published on: November 23, 2016
Design, synthesis, and characterization of novel, nonquaternary reactivators of GF-inhibited human
Stanton F McHardy1, Jonathan A Bohmann1, Michael R Corbett1
1Southwest Research Institute, Chemistry and Chemical Engineering Division, Department of Medicinal and Process Chemistry, 6220 Culebra Road, San Antonio, TX 78266, USA.
Abstract:
The goal of this research was to identify structurally novel, non-quaternarypyridinium reactivators of GF (cyclosarin)-inhibited hAChE that possess the capacity to mediate in vitro reactivation of GF-inhibited human acetylcholinesterase (hAChE). New compounds were designed, synthesized and assessed in GF-inhibited hAChE assays. Structure activity relationships for AChE binding and reactivation of GF-inhibited hAChE were developed. Lead compounds from two different chemical series, represented by compounds 17 and 38, displayed proficient in vitro reactivation of GF-inhibited hAChE, while also possessing low inhibition of native enzyme.
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