Phenyltetrahydroisoquinoline-pyridinaldoxime conjugates as efficient uncharged reactivators for the dephosphylation of inhibited human acetylcholinesterase. - Archive ouverte HAL
Article Dans Une Revue Journal of Medicinal Chemistry Année : 2012

Phenyltetrahydroisoquinoline-pyridinaldoxime conjugates as efficient uncharged reactivators for the dephosphylation of inhibited human acetylcholinesterase.

Résumé

Pyridinium and bis-pyridinium aldoximes are used as antidotes to reactivate acetylcholinesterase (AChE) inhibited by organophosphorus nerve agents. Herein, we described a series of nine nonquaternary phenyltetrahydroisoquinoline-pyridinaldoxime conjugates more efficient than or as efficient as pyridinium oximes to reactivate VX-, tabun- and ethyl paraoxon-inhibited human AChE. This study explores the structure-activity relationships of this new family of reactivators and shows that 1b-d are uncharged hAChE reactivators with a broad spectrum.

Domaines

Chimie organique
Fichier non déposé

Dates et versions

hal-00996512 , version 1 (26-05-2014)

Identifiants

Citer

Guillaume Mercey, Julien Renou, Tristan Verdelet, Maria Kliachyna, Rachid Baati, et al.. Phenyltetrahydroisoquinoline-pyridinaldoxime conjugates as efficient uncharged reactivators for the dephosphylation of inhibited human acetylcholinesterase.. Journal of Medicinal Chemistry, 2012, 55 (23), pp.10791-10795. ⟨10.1021/jm3015519⟩. ⟨hal-00996512⟩
81 Consultations
0 Téléchargements

Altmetric

Partager

More