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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)
Author(s) -
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.
Publication year - 2017
Publication title -
chemmedchem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.201700490
Subject(s) - front cover , ns5b , hepatitis c virus , chemistry , stereochemistry , benzofuran , computational biology , virology , biology , virus , hepacivirus , cover (algebra) , mechanical engineering , engineering
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).