Differential binding of phenothiazine urea derivatives to wild-type human cholinesterases and butyrylcholinesterase mutants

Add time:09/06/2019    Source:sciencedirect.com

A series of N-10 urea derivatives of phenothiazine was synthesized and each compound was evaluated for its ability to inhibit human cholinesterases. Most were specific inhibitors of BuChE. However, the potent inhibitory effects on both cholinesterases of one sub-class, the cationic aminoureas, provide an additional binding mechanism to cholinesterases for these compounds. The comparative effects of aminoureas on wild-type BuChE and several BuChE mutants indicate a binding process involving salt linkage with the aspartate of the cholinesterase peripheral anionic site. The effect of such compounds on cholinesterase activity at high substrate concentration supports ionic interaction of aminoureas at the peripheral anionic site.

We also recommend Trading Suppliers and Manufacturers of 1-(1-Ethyl-3-pyrrolidinyl)-3-(p-methoxyphenyl)urea (cas 18471-30-2). Pls Click Website Link as below: cas 18471-30-2 suppliers

Prev:Original articleDevelopment of benzimidazole derivatives to inhibit HIV-1 replication through protecting APOBEC3G protein
Next:Discovery of aryl ureas and aryl amides as potent and selective histamine H3 receptor antagonists for the treatment of obesity (Part I))