Abstract
The human immunodeficiency virus (HIV) contains an aspartic protease known to be essential for retroviral maturation and replication. On the basis of the substrate transition state, we have studied HIV-1 protease inhibitors containing an unnatural amino acid, (2S,3S)-3-amino-2-hydroxy-4-phenylbutyric acid, named allophenylnorstatine with a hydroxymethylcarbonyl (HMC) isostere. We reported small dipeptide-based HIV-1 protease inhibitors containing the HMC isostere [1], In order to enhance the anti-HIV activity and improve the physicochemical characteristics, we designed and synthesized prodrug forms of a peptidomimetic HIV protease inhibitor, KNI-727, conjugated with a nucleoside reverse transcriptase inhibitor, AZT [2,3].
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