Faculty of Military Health Sciences, University of Defence, Hradec Kralove, Czech Republic.
Molecules. 2009 Dec 1;14(12):4915-21. doi: 10.3390/molecules14124915.
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.
合成了四种新型双季铵类醛肟类胆碱酯酶重激活剂，它们在化学结构上有所不同。随后，评估了它们的生物活性，以研究它们对被对氧磷抑制的乙酰胆碱酯酶（AChE；EC 3.1.1.7）和丁酰胆碱酯酶（BuChE；EC 3.1.1.8）的重激活能力。将它们的重激活活性与目前临床上使用的标准重激活剂——氯解磷定、碘解磷定和双复磷进行了比较。结果表明，没有一种合成的化合物超过了被认为是对氧磷抑制的 AChE 重激活最有效化合物的碘解磷定。在 BuChE 重激活方面，两种化合物（K053 和 K068）的效果与碘解磷定相似。
