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Design, synthesis, and characterization of novel, nonquaternary reactivators of GF-inhibited human acetylcholinesterase. 2014
Stanton F McHardy, and
Jonathan A Bohmann, and
Michael R Corbett, and
Bismarck Campos, and
Michael W Tidwell, and
Paul Marty Thompson, and
Chris J Bemben, and
Tony A Menchaca, and
Tony E Reeves, and
William R Cantrell, and
William E Bauta, and
Ambrosio Lopez, and
Donald M Maxwell, and
Karen M Brecht, and
Richard E Sweeney, and
John McDonough
Southwest Research Institute, Chemistry and Chemical Engineering Division, Department of Medicinal and Process Chemistry, 6220 Culebra Road, San Antonio, TX 78266, USA. Electronic address: stanton.mchardy@utsa.edu.
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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