Universality of Oxime K203 for Reactivation of Nerve Agent-Inhibited AChE
Language English Country Netherlands Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
25845909
DOI
10.2174/1573406411666150407154204
PII: MC-EPUB-66389
Knihovny.cz E-resources
- MeSH
- Acetylcholinesterase metabolism MeSH
- Cholinesterase Inhibitors pharmacology MeSH
- Rats MeSH
- Humans MeSH
- Nerve Agents pharmacology MeSH
- Oximes pharmacology MeSH
- Pyridinium Compounds pharmacology MeSH
- Cholinesterase Reactivators pharmacology MeSH
- Animals MeSH
- Check Tag
- Rats MeSH
- Humans MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- 1-(4-carbamoylpyridinium)-4-(4-hydroxyiminomethylpyridinium)but-2-ene MeSH Browser
- Acetylcholinesterase MeSH
- Cholinesterase Inhibitors MeSH
- Nerve Agents MeSH
- Oximes MeSH
- Pyridinium Compounds MeSH
- Cholinesterase Reactivators MeSH
Oxime K203 seems to be the most promising oxime in case of reactivation of tabun-inhibited acetylcholinesterase (AChE). Although it was originally developed for treatment of tabun intoxications, it is able to reactivate cholinesterases inhibited by other nerve agents. This study is aimed at the evaluation of its potency in vitro against other nerve agents. For this purpose, sarin, tabun, cyclosarin, soman, VX, Russian VX and DFP were selected as members of the nerve agent family to check its universality. At high concentrations (10(-3) M), oxime K203 reached promising reactivation activity. At low concentrations, relevant for human use (10(-5) M), promising reactivation potency was obtained only with tabun. In conclusion, oxime K203 reactivates other nerve agents-inhibited cholinesterases, however its broad-spectrum reactivation is limited at high, for human not attainable, concentrations only.
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