Zawadzka_2013_J.Pineal.Res_54_435

Novel inhibitors of cholinesterases, especially butyrylcholinesterase (BCHE), were obtained by coupling melatonin-tacrine heterodimers via the carbamate bond. Compounds 14a-i possessed potent cholinesterase inhibitory activity (with IC50 values as low as 1.18 nm for acetylcholinesterase (AChE) and 0.24 nm for butyrylcholinesterase (BCHE)). These heterodimers exhibit selectivity toward BCHE, being from 4- to 256-fold more active toward BCHE than AChE, but still acting as better AChE inhibitors than tacrine 4.