Highly selective inhibition of butyrylcholinesterase by a novel melatonin–tacrine heterodimers | Zendy

Zawadzka Anna | Zendy; Łozińska Iwona | Zendy; Molęda Zuzanna | Zendy; Panasiewicz Mirosława | Zendy; Czarnocki Zbigniew | Zendy

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Highly selective inhibition of butyrylcholinesterase by a novel melatonin–tacrine heterodimers

Author(s) -

Zawadzka Anna,

Łozińska Iwona,

Molęda Zuzanna,

Panasiewicz Mirosława,

Czarnocki Zbigniew

Publication year - 2013

Publication title -

journal of pineal research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.881

H-Index - 131

eISSN - 1600-079X

pISSN - 0742-3098

DOI - 10.1111/jpi.12006

Subject(s) - tacrine , butyrylcholinesterase , acetylcholinesterase , cholinesterase , chemistry , stereochemistry , carbamate , melatonin , pharmacology , enzyme , aché , biochemistry , biology , endocrinology

Novel inhibitors of cholinesterases, especially butyrylcholinesterase ( B u C h E ), were obtained by coupling melatonin–tacrine heterodimers via the carbamate bond. Compounds 14a‐i possessed potent cholinesterase inhibitory activity (with IC 50 values as low as 1.18 n m for acetylcholinesterase ( AC h E ) and 0.24 n m for butyrylcholinesterase ( B u C h E )). These heterodimers exhibit selectivity toward B u C h E , being from 4‐ to 256‐fold more active toward B u C h E than AC h E , but still acting as better AC h E inhibitors than tacrine 4 .

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