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1996-02-27
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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).