Charles University, Faculty of Pharmacy, Department of Pharmaceutical Chemistry and Drug Control, Heyrovskeho 1203, 500 05 Hradec Kralove, Czech Republic.
Bioorg Med Chem Lett. 2011 Apr 15;21(8):2505-9. doi: 10.1016/j.bmcl.2011.02.047. Epub 2011 Feb 21.
This paper describes the preparation and in vitro evaluation of 18 newly prepared bis-quinolinium inhibitors on human recombinant acetylcholinesterase (AChE) and human plasmatic butyrylcholinesterase (BChE). Their inhibitory (IC(50)) and was compared to the chosen standards ambenonium dichloride, edrophonium chloride, BW284c51 and ethopropazine hydrochloride. One novel compound was found to be a promising inhibitor of hAChE (in nM range) and was better than edrophonium chloride or BW284c51, but was worse than ambenonium chloride. This compound also showed selectivity towards hAChE and it was confirmed as a non-competitive inhibitor of hAChE by kinetic analysis. A molecular modelling study further confirmed its binding to the peripheral active site of hAChE via apparent π-π or π-cationic interactions.
本文描述了 18 种新合成的双喹啉鎓抑制剂对人重组乙酰胆碱酯酶(AChE)和人血浆丁酰胆碱酯酶(BChE)的制备和体外评价。将它们的抑制作用(IC50)与选定的标准品氨甲酰胆碱二氯化物、依酚氯铵氯化物、BW284c51 和丙哌嗪盐酸盐进行了比较。发现一种新型化合物对 hAChE 具有很高的抑制作用(在纳摩尔范围内),优于依酚氯铵氯化物或 BW284c51,但劣于氨甲酰胆碱二氯化物。该化合物对 hAChE 也具有选择性,并通过动力学分析证实它是 hAChE 的非竞争性抑制剂。分子建模研究进一步证实了它通过明显的π-π 或π-阳离子相互作用与 hAChE 的外周活性位点结合。