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New methods in synthesis of acetylcholinesterase reactivators and evaluation of their potency to reactivate cyclosarin-inhibited AChE

✍ Scribed by K. Musílek; L. Lipka; V. Račáková; K. Kuča; D. Jun; V. Dohnal; M. Doležal

Book ID
111490935
Publisher
Versita
Year
2006
Tongue
English
Weight
194 KB
Volume
60
Category
Article
ISSN
0366-6352

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✦ Synopsis

Abstract

Nine potential AChE reactivators were synthesized using modification of currently known synthetic pathways. Their potency to reactivate AChE inhibited by cyclosarin nerve agent was tested in vitro. According to the previous results, 1,4-bis(2-hydroxyiminomethylpyridinium)butane dibromide seems to be the most potent AChE reactivator. The reactivation potency of these compounds depends on structural factors such as presence of quaternary nitrogens, length of the linking chain between both pyridinium rings, and position of the oxime moiety at the pyridinium ring.

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In vitro reactivation potency of some acetylcholinesterase reactivators against sarin- and cyclosarin-induced inhibitions
✍ Kamil Kuca; Jiri Cabal; Daniel Jun; Jiri Kassa; Lucie Bartosová; Gabriela Kuneso 📂 Article 📅 2005 🏛 John Wiley and Sons 🌐 English ⚖ 136 KB

In our study, we have tested six acetylcholinesterase (AChE) reactivators (pralidoxime, obidoxime, HI-6, trimedoxime, BI-6 and Hlö-7) for reactivation of sarin-and cyclosarin-inhibited AChE using an in vitro reactivation test. We have used rat brain homogenate as the suitable source of enzyme. All o