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Related Experiment Videos

Aspartic proteinases in disease: a structural perspective.

J B Cooper1

  • 1Division of Biochemistry and Molecular Biology, School of Biological Sciences, University of Southampton, Bassett Crescent East, UK. J.B.Cooper@soton.ac.uk

Current Drug Targets
|April 18, 2002
PubMed
Summary

Aspartic proteinases are crucial enzymes in various diseases, including AIDS, cancer, and infections. This review focuses on structure-based drug design for developing novel inhibitors targeting these enzymes.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Drug Discovery

Background:

  • Aspartic proteinases are vital enzymes implicated in numerous biological processes and diseases.
  • Examples include renin (hypertension), HIV proteinase (AIDS), cathepsin D (tumorigenesis), and pepsin (peptic ulcer disease).
  • These enzymes are also involved in amyloid disease, malaria, and fungal infections, highlighting the need for inhibitors.

Purpose of the Study:

  • To review the application of structure-based drug design for aspartic proteinase inhibitors.
  • To explore the catalytic mechanism and inhibitor design strategies.

Main Methods:

  • Review of existing literature on aspartic proteinases and structure-based drug design.
  • Analysis of the catalytic mechanism involving active site water and tetrahedral intermediates.

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  • Discussion of inhibitor design using transition state analogues.

    • Main Results:

    • Aspartic proteinases share a conserved catalytic mechanism involving active site aspartate residues and a water molecule.
    • Transition state analogues mimicking the tetrahedral intermediate are key for inhibitor design.
    • Structure-based drug design offers a rational approach to developing potent and specific inhibitors.

    Conclusions:

    • Aspartic proteinases represent significant therapeutic targets across a range of diseases.
    • Structure-based drug design is a powerful strategy for developing novel inhibitors.
    • Further research in this area holds promise for new treatments.