Abstract
We identified a non-peptidomimetic HIV protease inhibitor sanguinarine through screening a small compound library with a high-throughput E. coli-based assay. In vitro, sanguinarine inhibits the HIV protease with an IC50 of around 13 μM. Based on docking results, binding modes of sanguinarine to the HIV protease are proposed.
Keywords: high-throughput screening, e. coli-based system, sanguinarine, hiv protease, hiv protease inhibitors, hiv protease precursor