80861-22-9Relevant academic research and scientific papers
The synthesis and structure-activity relationship of substituted N-phenyl anthranilic acid analogs as amyloid aggregation inhibitors
Simons, Lloyd J.,Caprathe, Bradley W.,Callahan, Michael,Graham, James M.,Kimura, Takenori,Lai, Yingjie,LeVine III, Harry,Lipinski, William,Sakkab, Annette T.,Tasaki, Yoshikazu,Walker, Lary C.,Yasunaga, Tomoyuki,Ye, Yuyang,Zhuang, Nian,Augelli-Szafran, Corinne E.
scheme or table, p. 654 - 657 (2009/09/06)
It is believed that β-amyloid aggregation is an important event in the development of Alzheimer's disease. In the course of our studies to identify β-amyloid aggregation inhibitors, a series of N-phenyl anthranilic acid analogs were synthesized and studied for β-amyloid inhibition activity. The synthesis, structure-activity relationship, and in vivo activity of these analogs are discussed.
Affinity of 3-acyl substituted 4-quinolones at the benzodiazepine site of GABAA receptors
Lager, Erik,Nilsson, Jakob,stergaard Nielsen, Elsebet,Nielsen, Mogens,Liljefors, Tommy,Sterner, Olov
, p. 6936 - 6948 (2008/12/21)
The finding that alkyl 1,4-dihydro-4-oxoquinoline-3-carboxylate and N-alkyl-1,4-dihydro-4-oxoquinoline-3-carboxamide derivatives may be high-affinity ligands at the benzodiazepine binding site of the GABAA receptor, prompted a study of 3-acyl-1,4-dihydro-4-oxoquinoline (3-acyl-4-quinolones). In general, the affinity of the 3-acyl derivatives was found to be comparable with the 3-carboxylate and the 3-carboxamide derivatives, and certain substituents (e.g., benzyl) in position 6 were again shown to be important. As it is believed that the benzodiazepine binding site is situated between an α- and a γ-subunit in the GABAA receptor, selected compounds were tested on the α1β2γ2s, α2β2γ2s and α3β2γ2s GABAA receptor subtypes. The 3-acyl-4-quinolones display various degrees of selectivity for α1- versus α2- and α3-containing receptors, and high-affinity ligands essentially selective for α1 over α3 were developed.
