Abstract
Abstract Corilagin was seperated from extract of Phyllanthus urinaria L. and used as the precursor of inhibitors of hepatitis C virus (HCV) NS3 serine protease. Six derivatives were obtained through the chemical modification of corilagin and their structures were elucidated by the spectra analysis. Bio assay of these compounds showed that two of them had improved inhibitory efficiency than the precursor, with IC50 values of 2.28 µmol/L and 1.52 µmol/L, respectively. The binding made of two active compounds with substrate binding site of HCV NS3 protease was also investigated by molecular docking method.
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