1610553-24-6Relevant articles and documents
Design, synthesis, and characterization of novel, nonquaternary reactivators of GF-inhibited human acetylcholinesterase
McHardy, Stanton F.,Bohmann, Jonathan A.,Corbett, Michael R.,Campos, Bismarck,Tidwell, Michael W.,Thompson, Paul Marty,Bemben, Chris J.,Menchaca, Tony A.,Reeves, Tony E.,Cantrell Jr., William R.,Bauta, William E.,Lopez, Ambrosio,Maxwell, Donald M.,Brecht, Karen M.,Sweeney, Richard E.,McDonough, John
, p. 1711 - 1714 (2014/04/17)
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.
