Rapid Determination of the Specificity Constant of Irreversible Inhibitors (kinact/KI) by Means of an Endpoint Competition Assay

Angew Chem Int Ed Engl. 2015 Nov 16;54(47):14099-102. doi: 10.1002/anie.201505800. Epub 2015 Oct 1.

Abstract

Owing to their covalent target occupancy, irreversible inhibitors require low exposures and offer long duration, and their use thus represents a powerful strategy for achieving pharmacological efficacy. Importantly, the potency metric of irreversible inhibitors is kinact/KI not IC50. A simple approach to measuring kinact/KI was developed that makes use of an irreversible probe for competitive assays run to completion against test compounds. In this system, the kinact/KI value of the test compound is equal to (kinact/KI)probe ×[probe]/IC50. The advantages of this method include simplicity, high throughput, and application to all target classes, and it only requires an in-depth kinetic evaluation of the probe.

Keywords: covalent inhibitors; drug discovery; enzyme kinetics; irreversible inhibition.

MeSH terms

  • Endpoint Determination*
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / pharmacology*
  • ErbB Receptors / antagonists & inhibitors*
  • ErbB Receptors / metabolism
  • Humans
  • Kinetics
  • Molecular Structure
  • Morpholines / chemistry
  • Morpholines / pharmacology*
  • Structure-Activity Relationship
  • Time Factors

Substances

  • Enzyme Inhibitors
  • Morpholines
  • Canertinib
  • ErbB Receptors