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ID: ALA1133484
Journal: Bioorg Med Chem Lett
Title: Highly potent and selective peptide-based inhibitors of the hepatitis C virus serine protease: towards smaller inhibitors.
Authors: Llinàs-Brunet M, Bailey M, Fazal G, Ghiro E, Gorys V, Goulet S, Halmos T, Maurice R, Poirier M, Poupart MA, Rancourt J, Thibeault D, Wernic D, Lamarre D.
Abstract: Structure-activity studies on a hexapeptide N-terminal cleavage product of a dodecamer substrate led to the identification of very potent and highly specific inhibitors of the HCV NS3 protease/NS4A cofactor peptide complex. The largest increase in potency was accomplished by the introduction of a (4R)-naphthalen-1-yl-4-methoxy substituent to the P2 proline. N-Terminal truncation resulted in tetrapeptides containing a C-terminal carboxylic acid, which exhibited low micromolar activity against the HCV serine protease.
CiteXplore: 11055335