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Human immunodeficiency virus (HIV) protease inhibitors block the viral enzyme that cleaves Gag and Gag-Pol polyproteins. Polyprotein cleavage is needed for the maturation of new virions. In 1988 an active HIV protease was shown to be required for viral infectivity. The three-dimensional structure solved in 1989 revealed a homodimeric aspartyl protease with one catalytic aspartate from each subunit. Saquinavir, ritonavir, lopinavir, atazanavir and nelfinavir are active-site inhibitors of the HIV-1 enzyme. Ritonavir also inhibits cytochrome P450 3A4 (CYP3A4) and is used in drug metabolism studies. The list also holds HIV-1 inhibitors with other mechanisms, such as the maturation inhibitor bevirimat and the attachment inhibitor fostemsavir.
HIV Protease Substrate IV is a specific substrate designed for HIV protease. It facilitates the quantitative assessment of HIV-1 protease activity, enabling researchers to study the enzyme's function and evaluate potential inhibitors. This substrate is particularly useful in the development of antiviral therapies targeting HIV protease, contributing to the understanding of HIV pathogenesis and treatment strategies.
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HIV-1, HIV-2 Protease Substrate is a specific substrate designed for the enzymatic activity of HIV-1 and HIV-2 proteases. This substrate contains four residues that allow for conservative substitutions, facilitating studies on substrate binding and protease activity. It is a valuable tool for research focused on HIV protease function and the development of antiviral therapies.
Out of stock
All 3 sizes
HIV Protease Substrate 1 is a fluorogenic substrate specifically designed for the study of HIV protease activity. This reagent allows for the quantitative assessment of enzymatic function, facilitating investigations into HIV protease inhibitors and their effects on viral replication. It is particularly useful in the development of antiviral therapies and for studying the proteolytic processing of HIV proteins.
