Biotin-tagged probes for MMP expression and activation: design, synthesis, and binding properties

Bioconjug Chem. 2009 Apr;20(4):719-27. doi: 10.1021/bc8003827.


The design and synthesis of biotin chain-terminated inhibitors (BTI) showing high affinity for matrix metalloproteinases (MMPs) on one side and high affinity for avidin through the biotinylated tag on the other are reported. The affinity of the designed BTI toward five different MMPs has been evaluated and the simultaneous formation of a highly stable ternary system Avidin-BTI-MMP clearly assessed. This system will permit the development of new approaches to detect, quantify, or collect MMPs in biological samples, with potential applications in vivo.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Avidin / metabolism
  • Biotin / metabolism*
  • Catalytic Domain
  • Crystallography, X-Ray
  • Drug Design*
  • Enzyme Activation
  • Enzyme Inhibitors / pharmacology
  • Gene Expression Regulation, Enzymologic*
  • Metalloproteases / antagonists & inhibitors
  • Metalloproteases / chemistry
  • Metalloproteases / isolation & purification
  • Metalloproteases / metabolism*
  • Models, Molecular
  • Molecular Probes / chemical synthesis*
  • Molecular Probes / metabolism*
  • Protein Binding


  • Enzyme Inhibitors
  • Molecular Probes
  • Avidin
  • Biotin
  • Metalloproteases