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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Selective reversible inhibition of human butyrylcholinesterase by aryl amide derivatives of phenothiazine.

Evidence suggests that specific inhibition of butyrylcholinesterase may be an appropriate focus for the development of more effective drugs to treat dementias such as Alzheimer's disease. Butyrylcholinesterase is a co-regulator of cholinergic neurotransmission and its activity is increased in Alzheimer's disease, and is associated with all neuropathological lesions in this disease. Some selective butyrylcholinesterase inhibitors have already been reported to increase acetylcholine levels and to reduce the formation of abnormal amyloid found in Alzheimer's disease. Synthesized N-(10)-aryl and N-(10)-alkylaryl amides of phenothiazine are specific inhibitors of butyrylcholinesterase. In some cases, inhibition constants in the nanomolar range are achieved. Enzyme specificity and inhibitor potency of these molecules can be related to molecular volumes, steric and electronic factors. Computed logP values indicate high potential for these compounds to cross the blood-brain barrier. Use of such butyrylcholinesterase inhibitors could provide direct evidence for the importance of this enzyme in the normal nervous system and in Alzheimer's disease.[1]


  1. Selective reversible inhibition of human butyrylcholinesterase by aryl amide derivatives of phenothiazine. Darvesh, S., McDonald, R.S., Darvesh, K.V., Mataija, D., Conrad, S., Gomez, G., Walsh, R., Martin, E. Bioorg. Med. Chem. (2007) [Pubmed]
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