A fast and robust 19F NMR-based method for finding new HIV-1 protease inhibitors.
The human immunodeficiency virus (HIV) which encodes, among other indispensable enzymes, an aspartic protease that is essential for viral maturation and replication. Numerous inhibitors of the protease have been developed. However, the eventual resistance of HIV-1 to these drugs implies a continuous battle to develop new inhibitors. Proposed herein is a robust, fast, and reliable method employing (19)F NMR for the evaluation of the inhibitory activity of new compounds against HIV-1 protease.
Frutos
Silvia
S
Institut de Recerca Biomèdica (IRB-PCB), Parc Científic de Barcelona, Josep Samitier, 1-5. E-08028 Barcelona, Spain.
Tarrago
Teresa
T
Giralt
Ernest
E
D001665:Binding Sites; D002851:Chromatography, High Pressure Liquid; D016333:HIV Protease / Q000187:drug effects; D017320:HIV Protease Inhibitors / Q000737:chemistry / Q000494:pharmacology*; D015497:HIV-1 / Q000201:enzymology*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D013058:Mass Spectrometry
D017320:HIV Protease Inhibitors; D016333:HIV Protease