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Human immunodeficiency virus protease: A target for aids therapy
Author(s) -
Debouck Christine,
Metcalf Brian W.
Publication year - 1990
Publication title -
drug development research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.582
H-Index - 60
eISSN - 1098-2299
pISSN - 0272-4391
DOI - 10.1002/ddr.430210102
Subject(s) - protease , virus , virology , retrovirus , viral life cycle , in vitro , proteases , biology , enzyme , ns2 3 protease , proteolytic enzymes , protease inhibitor (pharmacology) , immune system , viral replication , immunology , biochemistry , viral load , antiretroviral therapy
Human immunodeficiency virus, also called HIV, is the etiologic agent of acquired immune deficiency syndrome (AIDS). This retrovirus produces a small, dimeric aspartyl protease which specifically cleaves the precursor forms of the structural proteins and enzymes of the virus. This proteolytic activity is absolutely required for the production of mature, infectious viral particles and is therefore an attractive target for therapeutic intervention. Peptide analogues containing transition‐state mimics were synthesized and shown to inhibit the activity of the purified HIV protease in vitro to various extents. Most interestingly, the most potent inhibitors were shown to effectively block the protease in HIV‐infected cells and to impair the viral life cycle. Other approaches to interfere with the viral protease activity or production are also discussed.