MCH-R1 antagonists based on an arginine scaffold: SAR studies on the amino-terminus.
We have identified a novel series of potent MCH-R1 antagonists based on l-arginine. As predicted by computational methods, there was an activity dependence on the pi-electronic character of the aromatic systems corresponding to the amino-terminus of these molecules. These results have enhanced our understanding of the MCH-R1 receptor and the potential for a predictive homology model.
Méndez-Andino
José
J
Procter & Gamble Pharmaceuticals, 8700 Mason-Montgomery Road, Mason, OH 45039, USA. mendezandino.jl@pg.com
Colson
Anny-Odile
AO
Denton
Daniel
D
Mitchell
Maria C
MC
Cross-Doersen
Doreen
D
Hu
X Eric
XE
D001120:Arginine / Q000494:pharmacology*; D002460:Cell Line; D002851:Chromatography, High Pressure Liquid; D006801:Humans; D008156:Luciferases / Q000235:genetics; D008958:Models, Molecular; D008968:Molecular Conformation; D017481:Receptors, Somatostatin / Q000037:antagonists & inhibitors*; D013329:Structure-Activity Relationship
C103263:MCHR1 protein, human; D017481:Receptors, Somatostatin; D001120:Arginine; D008156:Luciferases