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• W3200721863 endingPage "1655" @default.
• W3200721863 startingPage "1649" @default.
• W3200721863 abstract "HCV NS5A inhibitors are the backbone of directly acting antiviral treatments against the hepatitis C virus (HCV). While these therapies are generally highly curative, they are less effective in some specific HCV patient populations. In the search for broader-acting HCV NS5A inhibitors that address these needs, we explored conformational restrictions imposed by the [7,5]-azabicyclic lactam moiety incorporated into daclatasvir (1) and related HCV NS5A inhibitors. Unexpectedly, compound 5 was identified as a potent HCV genotype 1a and 1b inhibitor. Molecular modeling of 5 bound to HCV genotype 1a suggested that the use of the conformationally restricted lactam moiety might have resulted in reorientation of its N-terminal carbamate to expose a new interaction with the NS5A pocket located between amino acids P97 and Y93, which was not easily accessible to 1. The results also suggest new chemistry directions that exploit the interactions with the P97-Y93 site toward new and potentially improved HCV NS5A inhibitors." @default.
• W3200721863 created "2021-09-27" @default.
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• W3200721863 date "2021-09-15" @default.
• W3200721863 modified "2023-09-27" @default.
• W3200721863 title "The Discovery of Conformationally Constrained Bicyclic Peptidomimetics as Potent Hepatitis C NS5A Inhibitors" @default.
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• W3200721863 doi "https://doi.org/10.1021/acsmedchemlett.1c00391" @default.
• W3200721863 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8591741" @default.
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• W3200721863 hasPublicationYear "2021" @default.
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