Leucine aminopeptidase as a target for inhibitor design

Mini Rev Med Chem. 2001 Jul;1(2):133-44. doi: 10.2174/1389557013406990.

Abstract

In this review we focus on the most effective and the most promising inhibitors of leucine aminopeptidase. Their binding modes to the enzyme, the attempt to explain the origin of the inhibitory activity, as well as the structure-activity relationship for some of these compounds are discussed. Besides, the structural and electronic requirements of the enzyme active site and the binding pockets, together with the specificity towards the ligands, based on the structural and kinetic data, are presented.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acids / chemical synthesis
  • Amino Acids / chemistry
  • Amino Acids / pharmacology
  • Animals
  • Binding Sites
  • Drug Design
  • Enzyme Inhibitors / chemical synthesis*
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / pharmacology
  • Humans
  • Hydrogen Bonding
  • Leucyl Aminopeptidase / antagonists & inhibitors*
  • Leucyl Aminopeptidase / chemistry*
  • Models, Molecular
  • Peptides / chemical synthesis
  • Peptides / chemistry
  • Peptides / pharmacology
  • Protein Conformation
  • Structure-Activity Relationship

Substances

  • Amino Acids
  • Enzyme Inhibitors
  • Peptides
  • Leucyl Aminopeptidase