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Novel Bisquaternary Oximes—Reactivation of Acetylcholinesterase and Butyrylcholinesterase Inhibited by Paraoxon

Authors :
Daniel Jun
Jana Zdarova Karasova
Miroslav Pohanka
Martina Hrabinova
Kamil Musilek
Martin Paar
Vladimir Cirkva
Jiri Palecek
Kamil Kuca
Lucie Musilova
Source :
Molecules, Vol 14, Iss 12, Pp 4915-4921 (2009)
Publication Year :
2009
Publisher :
MDPI AG, 2009.

Abstract

Four novel bisquaternary aldoxime cholinesterase reactivators differing in their chemical structure were prepared. Afterwards, their biological activity was evaluated for their ability to reactivate acetylcholinesterase (AChE; EC 3.1.1.7) and butyrylcholinesterase (BuChE; EC 3.1.1.8) inhibited by paraoxon. Their reactivation activity was compared with standard reactivators—pralidoxime, obidoxime and HI-6—which are clinically used at present. As it resulted, none of the prepared compounds surpassed obidoxime, which is considered to be the most potent compound if used for reactivation of AChE inhibited by paraoxon. In case of BuChE reactivation, two compounds (K053 and K068) achieved similar results as obidoxime.

Details

Language :
English
ISSN :
14203049
Volume :
14
Issue :
12
Database :
Directory of Open Access Journals
Journal :
Molecules
Publication Type :
Academic Journal
Accession number :
edsdoj.2f2fa07940354b5097e604981538403b
Document Type :
article
Full Text :
https://doi.org/10.3390/molecules14124915