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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

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Dimerization Inhibitors of HIV-1 Protease

N. Boggetto / M. Reboud-Ravaux

Citation Information: Biological Chemistry. Volume 383, Issue 9, Pages 1321–1324, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2002.150, June 2005

Publication History

Published Online:
2005-06-01

Abstract

By targeting the highly conserved antiparallel βsheet formed by the interdigitation of the N and Cterminal strands of each monomer, dimerization inhibitors of HIV-1 protease may be useful to overcome the drug resistance observed with current activesite 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 Cterminal mimetics, lipopeptides and crosslinked interface peptides.

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