Structure-activity relationship for the reactivators of acetylcholinesterase inhibited by nerve agent VX
Jazyk angličtina Země Nizozemsko Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
22779796
DOI
10.2174/1573406411309050008
PII: MC-EPUB-20120710-9
Knihovny.cz E-zdroje
- MeSH
- acetylcholinesterasa metabolismus MeSH
- cholinesterasové inhibitory chemická syntéza chemie farmakologie MeSH
- krysa rodu Rattus MeSH
- molekulární struktura MeSH
- organothiofosforové sloučeniny chemická syntéza chemie farmakologie MeSH
- potkani Wistar MeSH
- vztah mezi dávkou a účinkem léčiva MeSH
- vztahy mezi strukturou a aktivitou MeSH
- zvířata MeSH
- Check Tag
- krysa rodu Rattus MeSH
- mužské pohlaví MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- acetylcholinesterasa MeSH
- cholinesterasové inhibitory MeSH
- organothiofosforové sloučeniny MeSH
- VX MeSH Prohlížeč
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.
Citace poskytuje Crossref.org
Two step synthesis of a non-symmetric acetylcholinesterase reactivator
