biostudies-literatureUnknown1(9)Cheng CCPyridine carboxamide-based inhibitors of the hepatitis C virus (HCV) NS5B polymerase were diversified and optimized to a variety of topologically related scaffolds. In particular, the 2-methyl nicotinic acid scaffold was developed into inhibitors with improved biochemical (IC50-GT1b = 0.014 μM) and cell-based HCV replicon potency (EC50-GT1b = 0.7 μM). Biophysical and biochemical characterization identified this novel series of compounds as palm site binders to HCV polymerase.ACS medicinal chemistry letters466-71https://www.ebi.ac.uk/biostudies/studies/S-EPMC4007899biostudies-literaturePyridine Carboxamides: Potent Palm Site Inhibitors of HCV NS5B Polymerase.PMC4007899Agrawal SWyss DFSoucy KAJiang CKHe ZWang YSFerrari EHuang XShipps GWCheng CCHuang HCfalsePyridine Carboxamides: Potent Palm Site Inhibitors of HCV NS5B Polymerase.Pyridine carboxamide-based inhibitors of the hepatitis C virus (HCV) NS5B polymerase were diversified and optimized to a variety of topologically related scaffolds. In particular, the 2-methyl nicotinic acid scaffold was developed into inhibitors with improved biochemical (IC50-GT1b = 0.014 μM) and cell-based HCV replicon potency (EC50-GT1b = 0.7 μM). Biophysical and biochemical characterization identified this novel series of compounds as palm site binders to HCV polymerase.2010-01-01T00:00:00Z2010 Dec2025-04-05T10:37:29.912Z2019-03-27T01:27:30ZS-EPMC40078992490023210.1021/ml100128h