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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Novel hepatitis C virus protease inhibitors: thiazolidine derivatives.

This study evaluated the inhibitory effects of thiazolidine derivatives on hepatitis C virus (HCV) protease and other human serine proteases. The inhibition efficacy was tested with a reversed-phase high-performance liquid chromatography (HPLC) assay system using a NS3-NS4A fusion protein as the HCV protease and a synthetic peptide substrate that mimics the NS5A-5B junction. Nine thiazolidine derivatives showed more than 50% inhibition at 50 microg/ml. The most potent derivative was RD4-6250, with 50% inhibition at a concentration of 2.3 microg/ml; this concentration was lower than those of other protease inhibitors reported previously. The most selective derivative was RD4-6205, with 50% inhibition at a concentration of 6.4 microg/ml, a lower concentration than those on other serine proteases (chymotrypsin, trypsin, plasmin, and elastase). These results suggest that the RD4-6205 skeleton is an important structure for inhibitory activity on the HCV protease NS3-NS4A.[1]

References

  1. Novel hepatitis C virus protease inhibitors: thiazolidine derivatives. Sudo, K., Matsumoto, Y., Matsushima, M., Fujiwara, M., Konno, K., Shimotohno, K., Shigeta, S., Yokota, T. Biochem. Biophys. Res. Commun. (1997) [Pubmed]
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