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PMID: 12437124 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Dimerization inhibitors of HIV-1 protease.

Biological chemistry ·Vol. 383 ·No. 9 ·2002-09-00 ·Pages 1321-4

Boggetto N, Reboud-Ravaux M

Abstract

By targeting the highly conserved antiparallel beta-sheet formed by the interdigitation of the N- and C-terminal strands of each monomer, dimerization inhibitors of HIV-1 protease may be useful to overcome the drug resistance observed with current active-site directed antiproteases. Sequestration of the monomer by the inhibitor (or disruption of the dimer interface) prevents the correct assembly of the inactive monomers to active enzyme. Strategies for the design of drugs targeting the dimer interface are described. Various dimerization inhibitors are reported including N- and C-terminal mimetics, lipopeptides and cross-linked interface peptides.

MeSH Terms
Dimerization Drug Design HIV Protease/metabolism HIV Protease Inhibitors/pharmacology Humans Models, Molecular Molecular Mimicry
Chemicals
HIV Protease Inhibitors HIV Protease
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Boggetto Nicole
Département de Biologie Cellulaire, Institut Jacques Monod, UMR 7592, CNRS-Université Paris 6, France.
Reboud-Ravaux Michèle
Article Info
Journal
Biological chemistry
Abbr.
Biol Chem
ISSN
1431-6730
Published
2002-09-00
Pages
1321-4
Language
English
Region
Germany
NLM ID
9700112
Subset
IM
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