A new role for old ligands: discerning chelators for zinc metalloproteinases

J Am Chem Soc. 2006 Mar 15;128(10):3156-7. doi: 10.1021/ja057957s.

Abstract

In an effort to identify promising non-hydroxamate inhibitors of matrix metalloproteinases (MMPs) several new zinc-binding groups (ZBGs) based on pyridine-derived or aza-macrocycle chelators have been examined. Fluorescence-based enzyme assays have been used to determine the IC50 values for these ZBGs against MMP-1, MMP-3, and anthrax lethal factor (LF). Many of these ligands were found to be remarkably potent, with IC50 values as much as 185-fold lower than that found for acetohydroxamic acid. These ligands are proposed to be more selective "warheads" for the inhibition of metalloenzymes that contain Zn2+ versus other metal ions at their active site.

Publication types

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

MeSH terms

  • Binding Sites
  • Cations, Divalent
  • Chelating Agents / chemistry
  • Chelating Agents / pharmacology*
  • Hydroxamic Acids / chemistry
  • Hydroxamic Acids / pharmacology
  • Kinetics
  • Ligands
  • Matrix Metalloproteinase Inhibitors*
  • Matrix Metalloproteinases / chemistry
  • Matrix Metalloproteinases / metabolism*
  • Models, Molecular
  • Protease Inhibitors / chemistry
  • Protease Inhibitors / pharmacology*
  • Zinc / chemistry
  • Zinc / metabolism*

Substances

  • Cations, Divalent
  • Chelating Agents
  • Hydroxamic Acids
  • Ligands
  • Matrix Metalloproteinase Inhibitors
  • Protease Inhibitors
  • acetohydroxamic acid
  • Matrix Metalloproteinases
  • Zinc