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In AIDS therapy, attempts have been made to inhibitthe virus-encoded enzymes, e.g. HIV-1 protease, using active site-directedinhibitors. This approach is questionable, however, due to virus mutations andthe high toxicity of the drugs. An alternative method to inhibit the dimericHIV protease is the targeting of the interface region of the protease subunitsin order to prevent subunit dimerization and enzyme activity. This approachshould be less prone to inactivation by mutation. A list of improved‘dimerization inhibitors’ of HIV-1 protease is presented. The main structuralfeatures are a short ‘interface’ peptide segment, including non-natural aminoacids, and an aliphatic N-terminal blocking group. The high inhibitory power ofsome of the lipopeptides [e.g. palmitoyl-Tyr-Glu-Leu-OH, palmitoyl-Tyr-Glu-(L-thyronine)-OH, palmitoyl-Tyr-Glu-(L-biphenyl-alanine)-OH] with lownanomolar  Ki  valuesin the enzyme test suggests that mimetics with goodbio-availability can be derived for AIDS therapy.

Lipopeptides as Dimerization Inhibitors of HIV-1 Protease