抄録
The human immunodeficiency virus type-1 (HIV-1), the causative agent of acquired immunodeficiency syndrome (AIDS), codes for a virus-specific aspartic protease responsible for processing the gag and gag-pol polyproteins and for the proliferation of the retrovirus. The HIV-1 protease functions as a homodimer and can recognize Phe-Pro and Tyr-Pro sequences as the cleavage site, but mammalian aspartic proteases do not have such specificity. These features provided a basis for the rational design of selective HIV protease-targeted drugs for the treatment of AIDS and related complex.
Based on the substrate transition state, we designed and synthesized a novel class of HIV protease inhibitors containing allophenylnorstatine [Apns; (2 S, 3S) -3-amino-2-hydroxy-4-phenylbutyric acid].
