Hydroxyquinones are competitive non-peptide inhibitors of HIV-1 proteinase

Brinkworth R.I. and Fairlie D.P. (1995) Hydroxyquinones are competitive non-peptide inhibitors of HIV-1 proteinase. Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, 1253 1: 5-8. doi:10.1016/0167-4838(95)00183-U


Author Brinkworth R.I.
Fairlie D.P.
Title Hydroxyquinones are competitive non-peptide inhibitors of HIV-1 proteinase
Journal name Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
ISSN 0167-4838
Publication date 1995-11-15
Sub-type Article (original research)
DOI 10.1016/0167-4838(95)00183-U
Volume 1253
Issue 1
Start page 5
End page 8
Total pages 4
Language eng
Subject 1303 Specialist Studies in Education
1304 Biophysics
1312 Molecular Biology
1315 Structural Biology
Abstract Quinones with one, two and three aromatic rings are a new class of micomolar 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.
Keyword Alizarin
anti-AIDS drug
Competitive inhibition
HIV-1 proteinase
Hydroxyquinone
Q-Index Code C1
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import - Archived
 
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