Structure-activity relationship for the reactivators of acetylcholinesterase inhibited by nerve agent VX
Language English Country Netherlands Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
22779796
DOI
10.2174/1573406411309050008
PII: MC-EPUB-20120710-9
Knihovny.cz E-resources
- MeSH
- Acetylcholinesterase metabolism MeSH
- Cholinesterase Inhibitors chemical synthesis chemistry pharmacology MeSH
- Rats MeSH
- Molecular Structure MeSH
- Organothiophosphorus Compounds chemical synthesis chemistry pharmacology MeSH
- Rats, Wistar MeSH
- Dose-Response Relationship, Drug MeSH
- Structure-Activity Relationship MeSH
- Animals MeSH
- Check Tag
- Rats MeSH
- Male MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Acetylcholinesterase MeSH
- Cholinesterase Inhibitors MeSH
- Organothiophosphorus Compounds MeSH
- VX MeSH Browser
Nerve agents such as sarin, VX and tabun are organophosphorus compounds able to inhibit an enzyme acetylcholinesterase (AChE). AChE reactivators and anticholinergics are generally used as antidotes in the case of intoxication with these agents. None from the known AChE reactivators is able to reactivate AChE inhibited by all kinds of nerve agents. In this work, reactivation potency of seventeen structurally different AChE reactivators was tested in vitro and subsequently, relationship between their chemical structure and biological activity was outlined. VX was chosen as appropriate member of the nerve agent family.
References provided by Crossref.org
Two step synthesis of a non-symmetric acetylcholinesterase reactivator
