| Title : Specific targeting of acetylcholinesterase and butyrylcholinesterase recognition sites. Rational design of novel, selective, and highly potent cholinesterase inhibitors - Savini_2003_J.Med.Chem_46_1 |
| Author(s) : Savini L , Gaeta A , Fattorusso C , Catalanotti B , Campiani G , Chiasserini L , Pellerano C , Novellino E , McKissic D , Saxena A |
| Ref : Journal of Medicinal Chemistry , 46 :1 , 2003 |
|
Abstract :
Tacrine-based AChE and BCHE inhibitors were designed by investigating the topology of the active site gorge of the two enzymes. The homobivalent ligands characterized by a nitrogen-bridged atom at the tether level could be considered among the most potent and selective cholinesterase inhibitors described to date. The nitrogen-containing homobivalent ligands 3e,g and the sulfur-containing 3h validated the hypothesis of extra sites of interaction in the AChE and BCHE active site gorges. |
| PubMedSearch : Savini_2003_J.Med.Chem_46_1 |
| PubMedID: 12502352 |
Savini L, Gaeta A, Fattorusso C, Catalanotti B, Campiani G, Chiasserini L, Pellerano C, Novellino E, McKissic D, Saxena A (2003)
Specific targeting of acetylcholinesterase and butyrylcholinesterase recognition sites. Rational design of novel, selective, and highly potent cholinesterase inhibitors
Journal of Medicinal Chemistry
46 :1
Savini L, Gaeta A, Fattorusso C, Catalanotti B, Campiani G, Chiasserini L, Pellerano C, Novellino E, McKissic D, Saxena A (2003)
Journal of Medicinal Chemistry
46 :1