Identification of Sanguinarine as a Novel HIV Protease Inhibitor from High-Throughput Screening of 2,000 Drugs and Natural Products with a Cell-Based Assay

Ting-Jen      Cheng; David   S.   Goodsell; Chen-Chen      Kan

doi:10.2174/1570180054405811

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

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Letters in Drug Design & Discovery

Title: Identification of Sanguinarine as a Novel HIV Protease Inhibitor from High-Throughput Screening of 2,000 Drugs and Natural Products with a Cell-Based Assay

Volume: 2 Issue: 5

Author(s): Ting-Jen Cheng, David S. Goodsell and Chen-Chen Kan

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Keywords: high-throughput screening, e. coli-based system, sanguinarine, hiv protease, hiv protease inhibitors, hiv protease precursor

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.

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Cheng Ting-Jen, Goodsell S. David and Kan Chen-Chen, Identification of Sanguinarine as a Novel HIV Protease Inhibitor from High-Throughput Screening of 2,000 Drugs and Natural Products with a Cell-Based Assay, Letters in Drug Design & Discovery 2005; 2 (5) . https://dx.doi.org/10.2174/1570180054405811