cp-640186 and Obesity

cp-640186 has been researched along with Obesity* in 1 studies

Other Studies

1 other study(ies) available for cp-640186 and Obesity

Article	Year
Design of small molecule inhibitors of acetyl-CoA carboxylase 1 and 2 showing reduction of hepatic malonyl-CoA levels in vivo in obese Zucker rats. Bioorganic & medicinal chemistry, 2011, May-15, Volume: 19, Issue:10 Inhibition of acetyl-CoA carboxylases has the potential for modulating long chain fatty acid biosynthesis and mitochondrial fatty acid oxidation. Hybridization of weak inhibitors of ACC2 provided a novel, moderately potent but lipophilic series. Optimization led to compounds 33 and 37, which exhibit potent inhibition of human ACC2, 10-fold selectivity over inhibition of human ACC1, good physical and in vitro ADME properties and good bioavailability. X-ray crystallography has shown this series binding in the CT-domain of ACC2 and revealed two key hydrogen bonding interactions. Both 33 and 37 lower levels of hepatic malonyl-CoA in vivo in obese Zucker rats. Topics: Acetyl-CoA Carboxylase; Animals; Crystallography, X-Ray; Diabetes Mellitus, Type 2; Drug Design; Enzyme Inhibitors; Fatty Acids; Humans; Liver; Male; Malonyl Coenzyme A; Mice; Mice, Inbred C57BL; Models, Molecular; Obesity; Rats; Rats, Zucker; Small Molecule Libraries; Structure-Activity Relationship	2011

Article

Year

Design of small molecule inhibitors of acetyl-CoA carboxylase 1 and 2 showing reduction of hepatic malonyl-CoA levels in vivo in obese Zucker rats.

Bioorganic & medicinal chemistry, 2011, May-15, Volume: 19, Issue:10

Inhibition of acetyl-CoA carboxylases has the potential for modulating long chain fatty acid biosynthesis and mitochondrial fatty acid oxidation. Hybridization of weak inhibitors of ACC2 provided a novel, moderately potent but lipophilic series. Optimization led to compounds 33 and 37, which exhibit potent inhibition of human ACC2, 10-fold selectivity over inhibition of human ACC1, good physical and in vitro ADME properties and good bioavailability. X-ray crystallography has shown this series binding in the CT-domain of ACC2 and revealed two key hydrogen bonding interactions. Both 33 and 37 lower levels of hepatic malonyl-CoA in vivo in obese Zucker rats.

Topics: Acetyl-CoA Carboxylase; Animals; Crystallography, X-Ray; Diabetes Mellitus, Type 2; Drug Design; Enzyme Inhibitors; Fatty Acids; Humans; Liver; Male; Malonyl Coenzyme A; Mice; Mice, Inbred C57BL; Models, Molecular; Obesity; Rats; Rats, Zucker; Small Molecule Libraries; Structure-Activity Relationship

2011