Front Cover: Development of a New Structural Class of Broadly Acting HCV Non‐Nucleoside Inhibitors Leading to the Discovery of MK‐8876 (ChemMedChem 17/2017)

The front cover picture shows the crystal structure of MK‐8876 bound to the hepatitis C virus (HCV) NS5B protein. The biaryl linkage at the 5‐position of the benzofuran acts as a bridge between the Palm I and Palm II binding sites, enabling MK‐8876 to interact with both sites simultaneously. MK‐8876...

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Bibliographic Details
Published in:ChemMedChem 2017-09, Vol.12 (17), p.1418-1418
Main Authors: McComas, Casey C., Palani, Anandan, Chang, Wei, Holloway, M. Katharine, Lesburg, Charles A., Li, Peng, Liverton, Nigel, Meinke, Peter T., Olsen, David B., Peng, Xuanjia, Soll, Richard M., Ummat, Ajay, Wu, Jie, Wu, Jin, Zorn, Nicolas, Ludmerer, Steven W.
Format: Article
Language:English
Subjects:
Benzofuran
Binding sites
Crystal structure
Genotypes
hepatitis C
inhibitors
MK-8876
Mutants
non-nucleoside
NS5B
NS5B protein
Viruses
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Summary:The front cover picture shows the crystal structure of MK‐8876 bound to the hepatitis C virus (HCV) NS5B protein. The biaryl linkage at the 5‐position of the benzofuran acts as a bridge between the Palm I and Palm II binding sites, enabling MK‐8876 to interact with both sites simultaneously. MK‐8876 shows broad potency against a wide range of HCV genotypes and maintains that potency against clinically relevant mutants. More information can be found in the Full Paper by Casey C. McComas et al. on page 1436 in Issue 17, 2017 (DOI: 10.1002/cmdc.201700228).
ISSN:1860-7179
1860-7187
DOI:10.1002/cmdc.201700490