A series of huprine-tacrine heterodimers has been developed by connection of huprine Y, a compound with one of the highest affinities for the active site of acetylcholinesterase yet reported, with tacrine, a compound with known affinity for the peripheral site of the enzyme, through a linker of appropriate length to allow simultaneous interaction with both binding sites. These compounds exhibit human acetylcholinesterase and butyrylcholinesterase inhibitory activities with IC50 values in the subnanomolar and low nanomolar range, respectively. © 2005 American Chemical Society.
|Journal||Journal of Medicinal Chemistry|
|Publication status||Published - 24 Mar 2005|