Patent
Chiral intermediates for the preparation of peptidomimetic protease inhibitors
Babine Robert Edward,Shu-Hui Chen,Jason Eric Lamar,Snyder Nancy June,Sun Xicheng David,Mark Joseph Tebbe,Frantz Victor,Wang Q May,Yip Yvonne Yee Mai,Collado Ivan,Cristina Garcia-Paredes,Parker Raymond Samuel,Jin Ling,Deqi Duo,Glass John Irvin +14 more
- 31 Aug 2001
TL;DR: In this article, the peptidomimetic compounds useful as protease inhibitors, particularly as serine protease inhibitor and more particularly as hepatitis C NS3 protease inhibition; intermediates thereto; their preparation including novel steroselective processes to intermediates.
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Abstract: The present invention relates to peptidomimetic compounds useful as protease inhibitors (1), particularly as serine protease inhibitors and more particularly as hepatitis C NS3 protease inhibitors; intermediates thereto; their preparation including novel steroselective processes to intermediates. The invention is also directed to pharmaceutical compositions and to methods for using the compounds for inhibiting HCV protease or treating a patient suffering from an HCV infection or physiological condition related to the infection. Also provided are pharmaceutical combinations comprising, in addition to one or more HCV serine protease inhibitors, one or more interferons exhibiting anti-HCV activity and/or one or more compounds having anti HCV activity and a pharmaceutically acceptable carrier, and methods for treating or preventing a HCV infection in a patient using the compositions. The present invention is also directed to a kit or pharmaceutical pack for treating or preventing HCV infection in a patient.
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TL;DR: The nucleotide sequence of the RNA genome of the human hepatitis C virus has been determined and significant genome diversity is apparent within the putative 5' structural gene region of different HCV isolates, suggesting the presence of closely related but distinct viral genotypes.
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TL;DR: Deletion analyses suggest that the structural and NS2 regions of the polyprotein are not required for the HCV NS3 proteinase activity, and sequence comparison of the residues flanking these cleavage sites for all sequenced HCV strains reveals conserved residues which may play a role in determining HCV proteinase substrate specificity.
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