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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. Bioassay of these compounds showed that two of them had improved inhibitory efficiency than the precursor, with IC50 values of 2.28μmol/L and 1.52μmol/L, respectively. The binding mode of two active compounds with substrate bind ing site of HCV NS3 protease was also investigated by molecular docking method.
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. Bioassay 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 mode of two active compounds with substrate binding site of HCV NS3 protease was also investigated by molecular docking method.