Xavier Formosa

TL;DR: A novel series of donepezil-tacrine hybrids designed to simultaneously interact with the active, peripheral and midgorge binding sites of acetylcholinesterase have been synthesized and tested, exhibiting IC50 values in the subnanomolar or low nanomolar range in most cases.

TL;DR: Two isomeric series of dual binding site acetylcholinesterase (AChE) inhibitors that retain the potent and selective human AChE inhibitory activity of the parent 6-chlorotacrine while exhibiting a significant in vitro inhibitoryActivity toward the AChe-induced and self-induced Abeta aggregation and toward BACE-1, as well as ability to enter the central nervous system, which makes them promising anti-Alzheimer lead compounds.

TL;DR: Huprine-tacrine heterodimers take on added value in that they display a potent in vitro inhibitory activity toward human butyrylcholinesterase, self-induced Aβ aggregation, and β-secretase, and are able to cross the blood-brain barrier.

TL;DR: Two novel families of dual binding site acetylcholinesterase (AChE) inhibitors have been developed, able to interfere in vitro both formation and aggregation of the beta-amyloid peptide, the latter effects endowing these compounds with the potential to modify Alzheimer's disease progression.

TL;DR: A series of h uprine-tacrine heterodimers has been developed by connection of huprine Y with tacrine through a linker of appropriate length to allow simultaneous interaction with both binding sites of acetylcholinesterase.