Detecting drug-target binding in cells using fluorescence-activated cell sorting coupled with mass spectrometry analysis

Methods Appl Fluoresc. 2017 Dec 15;6(1):015002. doi: 10.1088/2050-6120/aa8c60.

Abstract

The assessment of drug-target engagement for determining the efficacy of a compound inside cells remains challenging, particularly for difficult target proteins. Existing techniques are more suited to soluble protein targets. Difficult target proteins include those with challenging in vitro solubility, stability or purification properties that preclude target isolation. Here, we report a novel technique that measures intracellular compound-target complex formation, as well as cellular permeability, specificity and cytotoxicity-the toxicity-affinity-permeability-selectivity (TAPS) technique. The TAPS assay is exemplified here using human kynurenine 3-monooxygenase (KMO), a challenging intracellular membrane protein target of significant current interest. TAPS confirmed target binding of known KMO inhibitors inside cells. We conclude that the TAPS assay can be used to facilitate intracellular hit validation on most, if not all intracellular drug targets.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biological Assay / methods*
  • Enzyme Inhibitors / pharmacology*
  • Flow Cytometry
  • Fluorescence
  • HEK293 Cells
  • Humans
  • Kynurenine 3-Monooxygenase* / antagonists & inhibitors
  • Kynurenine 3-Monooxygenase* / genetics
  • Kynurenine 3-Monooxygenase* / metabolism
  • Mass Spectrometry

Substances

  • Enzyme Inhibitors
  • Kynurenine 3-Monooxygenase