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Inhibition of acetylcholinesterase by O-(methylcarbamoyl)oximes. Structure-activity relationships

Merlina, Georges and Calmon, Jean-Pierre Inhibition of acetylcholinesterase by O-(methylcarbamoyl)oximes. Structure-activity relationships. (1980) Journal of Agricultural and Food Chemistry, 28 (3). 673-675. ISSN 0021-8561

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Official URL: http://dx.doi.org/10.1021/jf60229a015


Since the anticholnesterase activity and the mechanism of alcaline hydrolysis of O-(methyl-carbamoy)benzaldoximes and acetopheniximes are analogous to those of phenyl N-methylcarbamates, these two groups of derivatives were compared by means of structure activity relationships.The correlation with the electronic substituent parameter δ showed that the mechanism of inhibition of acetylcholinesterase by O-(methylcarbamoyl)oximes is the same as that observed for phenyl N-methylcarbamates bearing strongly electron-withdrawing substituents.The correlations with the bimolecular rate constant Koh suggest that the mechanism of the alkaline hydrolysis of oximes carbamates may closely parallel their mechanism of interaction with acetylcholinesterase at the seryl hydroxyl.

Item Type:Article
HAL Id:hal-03487574
Audience (journal):International peer-reviewed journal
Uncontrolled Keywords:
Institution:French research institutions > Centre National de la Recherche Scientifique - CNRS (FRANCE)
Université de Toulouse > Institut National Polytechnique de Toulouse - Toulouse INP (FRANCE)
Université de Toulouse > Université Toulouse III - Paul Sabatier - UT3 (FRANCE)
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Deposited On:14 Dec 2012 12:18

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