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The first HIV protease inhibitor, saquinavir, is a peptidomimetic hydroxyethylamine [6] and was marketed in 1995. [18] It is a transition state analogue of a native substrate of the protease. [6] The observation that HIV-1 protease cleaves the sequences containing the dipeptides Tyr-Pro or Phe-Pro was the basic design criterion. [19]
HIV-1 protease or PR is a retroviral aspartyl protease (retropepsin), an enzyme involved with peptide bond hydrolysis in retroviruses, that is essential for the life-cycle of HIV, the retrovirus that causes AIDS.
Some of the most well known are antiviral drugs widely used to treat HIV/AIDS, hepatitis C and COVID-19. These protease inhibitors prevent viral replication by selectively binding to viral proteases (e.g. HIV-1 protease) and blocking proteolytic cleavage of protein precursors that are necessary for the production of infectious viral particles.
The genome and proteins of HIV (human immunodeficiency virus) have been the subject of extensive research since the discovery of the virus in 1983. [1] [2] "In the search for the causative agent, it was initially believed that the virus was a form of the Human T-cell leukemia virus (HTLV), which was known at the time to affect the human immune system and cause certain leukemias.
Gp41 also known as glycoprotein 41 is a subunit of the envelope protein complex of retroviruses, including human immunodeficiency virus (HIV). Gp41 is a transmembrane protein that contains several sites within its ectodomain that are required for infection of host cells.
The HIV-1 p24 capsid protein plays crucial roles throughout the replication cycle, making it an attractive therapeutic target. Unlike the viral enzymes ( protease , reverse transcriptase and integrase ) that are currently targeted by small-molecule antiretroviral drugs, p24 capsid proteins operate through protein-protein interactions.
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