       Document 0578
 DOCN  M9630578
 TI    Hydroxyquinones are competitive non-peptide inhibitors of HIV-1
       proteinase.
 DT    9603
 AU    Brinkworth RI; Fairlie DP; Centre for Drug Design and Development,
       University of Queensland,; Brisbane, Australia.
 SO    Biochim Biophys Acta. 1995 Nov 15;1253(1):5-8. Unique Identifier :
       AIDSLINE MED/96085082
 AB    Quinones with one, two and three aromatic rings are a new class of
       micromolar non-peptidic inhibitors of HIV-1 proteinase, an enzyme
       essential for replication of Human Immunodeficiency Virus and an
       important drug target for AIDS. Substituted anthraquinones bearing
       hydroxyl substituents on one of their three rings were the most potent
       of these inhibitors. Comparisons with other small non-peptidic
       inhibitors that are now emerging, together with enzyme kinetic data
       indicating that alizarin is a competitive inhibitor, suggest that
       anthraquinones bind in the active-site groove of HIV-1 proteinase.
 DE    Anthraquinones/*PHARMACOLOGY  Binding Sites  Binding, Competitive  Human
       Hydrogen-Ion Concentration  HIV Protease/*METABOLISM  HIV Protease
       Inhibitors/*CHEMISTRY/*PHARMACOLOGY  HIV-1/DRUG EFFECTS/*ENZYMOLOGY
       Kinetics  Molecular Structure  Oxidation-Reduction
       Quinones/CHEMISTRY/*PHARMACOLOGY  Spectrometry, Fluorescence
       Structure-Activity Relationship  Support, Non-U.S. Gov't  JOURNAL
       ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).

