Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1370828 | Bioorganic & Medicinal Chemistry Letters | 2011 | 4 Pages |
Abstract
A series of new HIV-1 protease inhibitors with the hydroxyethylamine core and different hydroxyprolinamide P2 ligands were designed and synthesized. Variation of substitutions at the P2 significantly affected the enzyme inhibitory potency of the inhibitors. Compounds 2a and 2d showed excellent enzyme inhibitory activity with IC50 values in the nanomolar range. An active site binding model for inhibitors 2a and 2d was suggested based upon the computational-docking results of the ligand with HIV-1 protease. This model offers molecular insights regarding ligand-binding site interactions of the hydroxyprolinamide-derived novel P2-ligand.
Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slide
Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Bing-Lei Gao, Cheng-Mei Zhang, Yi-Zhen Yin, Long-Qian Tang, Zhao-Peng Liu,