Author/Authors :
Montse Llinàs-Brunet، نويسنده , , Murray Bailey، نويسنده , , Gulrez Fazal، نويسنده , , Elise Ghiro، نويسنده , , Vida Gorys، نويسنده , , Sylvie Goulet، نويسنده , , Ted Halmos، نويسنده , , Roger Maurice، نويسنده , , Martin Poirier، نويسنده , , Marc-André Poupart، نويسنده , , Jean Rancourt، نويسنده , , Diane Thibeault، نويسنده , , Dominik Wernic، نويسنده , , Daniel Lamarre، نويسنده ,
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.
