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Lipopeptides as Dimerization Inhibitors of HIV-1 Protease by Schramm, H. J.; Rosny, E. De; Reboud-Ravaux, M.; Büttner, J.; Dick, A.; Schramm, W. is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Lipopeptides as Dimerization Inhibitors of HIV-1 Protease about?

## Abstract In AIDS therapy, attempts have been made to inhibit the virus-encoded enzymes, e.g. HIV-1 protease, using active site-directed inhibitors. This approach is questionable, however, due to virus mutations and the high toxicity of the drugs. An alternative method to inhibit the dimeric HIV protease is the targeting of the interface region of the protease subunits in order to prevent subunit dimerization and enzyme activity. This approach should be less prone to inactivation by mutation. A list of improved ‘dimerization inhibitors’ of HIV-1 protease is presented. The main structural features are a short ‘interface’ peptide segment, including non-natural amino acids, and an aliphatic N-terminal blocking group. The high inhibitory power of some of the lipopeptides [e.g. palmitoyl-Tyr-Glu-Leu-OH, palmitoyl-Tyr-Glu-(L-thyronine)-OH, palmitoyl-Tyr-Glu-(L-biphenyl-alanine)-OH] with low nanomolar__Ki__valuesin the enzyme test suggests that mimetics with good bio-availability can be derived for AIDS therapy.

Who reads Lipopeptides as Dimerization Inhibitors of HIV-1 Protease?

Author

Schramm, H. J.; Rosny, E. De; Reboud-Ravaux, M.; Büttner, J.; Dick, A.; Schramm, W.

Publisher

Walter de Gruyter GmbH & Co. KG; Walter de Gruyter GmbH (ISSN 1431-6730)

Published

1999

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)