176092-23-2Relevant academic research and scientific papers
Differential binding of phenothiazine urea derivatives to wild-type human cholinesterases and butyrylcholinesterase mutants
Darvesh, Sultan,Pottie, Ian R.,Darvesh, Katherine V.,McDonald, Robert S.,Walsh, Ryan,Conrad, Sarah,Penwell, Andrea,Mataija, Diane,Martin, Earl
experimental part, p. 2232 - 2244 (2010/05/18)
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.
Use of N-substituted phenothiazines
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, (2008/06/13)
The invention relates to the use of N-substituted phenothiazines for the production of medicaments for the treatment of cerebral disorders. The invention likewise relates to novel active compounds which are prepared by reaction of phenothiazine with the appropriate acids, esters or amides or by reaction of the phenothiazinecarbonyl halides with amines. The active compounds are particularly suitable for the treatment of dementias and age-related leaning and memory disorders and depressions.
