OATAO - Open Archive Toulouse Archive Ouverte Open Access Week

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

[img] (Document in English)

PDF (Publisher's version) - Depositor and staff only - Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader
439kB

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

Abstract

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
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 - INPT (FRANCE)
Université de Toulouse > Université Toulouse III - Paul Sabatier - UPS (FRANCE)
Laboratory name:
Statistics:download
Deposited By: Nadia Kelmouss
Deposited On:14 Dec 2012 12:18

Repository Staff Only: item control page