NONPEPTIDE INHIBITORS OF HCV SERINE PROTEINASE

We screened a chemical Library of 2000 compounds for inhibitors of hep atitis C virus (HCV) serine proteinase using an in vitro screening met hod measuring the hydrolysis of the peptide substrate. Three compounds sere found to be the most potent inhibitors (IC50 < 10(-5) M). Two of them had a similar structure, that of halogenated benzanilide, and we re not inhibitory for common serine proteinases, They inhibited the en zyme non-competitively with the substrate, Together with the result of the analogous compounds in the chemical library, the presumed structu ral requirements of the inhibition are pointed out. (C) 1998 Federatio n of European Biochemical Societies.