Characterization of alpha-nitromethyl ketone as a new zinc-binding group based on structural analysis of its complex with carboxypeptidase A

Bioorg Med Chem Lett. 2009 Sep 1;19(17):5009-11. doi: 10.1016/j.bmcl.2009.07.060. Epub 2009 Jul 12.

Abstract

Zinc-binding groups (ZBGs) are exhaustively applied in the development of the new inhibitors against a wide variety of physiologically and pathologically important zinc proteases. Here the alpha-nitro ketone was presented as a new ZBG, which is a transition-state analog featured by the unique bifurcated hydrogen bonds at the active site of carboxypeptidase A based on the structural analysis. Introduction of a nitro group at the alpha-position of the ketone could provide more non-covalent interactions without loss of the abilities to form a tetrahedral transition-state analog.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Carboxypeptidases A / antagonists & inhibitors*
  • Carboxypeptidases A / metabolism
  • Catalytic Domain
  • Crystallography, X-Ray
  • Hydrogen Bonding
  • Ketones / chemical synthesis
  • Ketones / chemistry*
  • Ketones / pharmacology
  • Molecular Conformation
  • Protease Inhibitors / chemical synthesis
  • Protease Inhibitors / chemistry*
  • Protease Inhibitors / pharmacology
  • Protein Binding
  • Zinc / chemistry*

Substances

  • Ketones
  • Protease Inhibitors
  • Carboxypeptidases A
  • Zinc