Matrix Metalloproteinase Protocols

Volume 622 of the series Methods in Molecular Biology pp 435-450


Kinetic Analysis of the Inhibition of Matrix Metalloproteinases: Lessons from the Study of Tissue Inhibitors of Metalloproteinases

  • Frances WillenbrockAffiliated withOrpington
  • , Daniel A. ThomasAffiliated withGlaxoSmithKline
  • , Augustin AmourAffiliated withGlaxoSmithKline

* Final gross prices may vary according to local VAT.

Get Access


Tissue inhibitors of metalloproteinases (TIMPs) are a group of highly potent inhibitors of matrix metalloproteinases (MMPs) and disintegrin metalloproteinases (ADAMs). The high affinity and “tight-binding” nature of the inhibition of MMPs or ADAMs by TIMPs presents challenges for the determination of both equilibrium and dissociation rate constants of these inhibitory events. Methodologies that enable some of these challenges to be overcome are described in this chapter and represent valuable lessons for the in vitro assessment of MMP or ADAM inhibitors within a drug discovery context.

Key words

Matrix metalloproteinases tissue inhibitors of metalloproteinases enzyme kinetics fluorescence resonance energy transfer