Theoretical Models of Aspartic Proteases: Active Site Properties, Dimer Stability and Interactions with Model Inhibitors

  • Anwar Rayan
  • Amit Fliess
  • Moshe Kotler
  • Michael Chorev
  • Amiram Goldblum
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 306)


HIV-1 PR, an aspartic proteinase (AP), is recognized now as an important target for designing effective and selective drugs which could arrest the late stages in replication of HIV-1, the causative agent of AIDS.1 Selectivity of such enzyme inhibitors is required in addition to high affinity. The most spectacular difference between HIV-1 PR, a retroviral enzyme, and the cellular AP, is the smaller size and dimeric structure of the former. The conservation of active site residues, Asp-Thr/Ser-Gly, seems to eliminate the ability to design selective active-site inhibitors for AP.2 This is, however, achieved by accumulated experience with the construction of novel renin inhibitors.


Active Site Residue Aspartic Proteinase Model Inhibitor Renin Inhibitor Dime Stability 
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Copyright information

© Plenum Press, New York 1991

Authors and Affiliations

  • Anwar Rayan
    • 1
  • Amit Fliess
    • 1
  • Moshe Kotler
    • 2
  • Michael Chorev
    • 1
  • Amiram Goldblum
    • 1
  1. 1.Department of Pharmaceutical Chemistry, School of PharmacyHebrew University of JerusalemJerusalemIsrael
  2. 2.Department of Molecular Genetics, School of MedicineHebrew University of JerusalemJerusalemIsrael

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