Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1372255 | Bioorganic & Medicinal Chemistry Letters | 2009 | 5 Pages |
The importance of internal hydrogen bonding in a series of benzothiadiazine and 1,4-benzothiazine NS5b inhibitors has been explored. Computational analysis has been used to compare the protonated vs. anionic forms of each series and we demonstrate that activity against HCV NS5b polymerase is best explained using the anionic forms. The syntheses and structure–activity relationships for a variety of new analogs are also discussed.
Graphical abstractThe importance of internal hydrogen bonding in a series of benzothiadiazine and 1,4-benzothiazine NS5b inhibitors has been explored. Computational analysis suggests HCV NS5b polymerase activity is best explained using the anionic forms.Figure optionsDownload full-size imageDownload as PowerPoint slide