Plasmon-waveguide resonance spectroscopy: A new tool for investigating signal transduction by G-protein coupled receptors

Gordon Tollin, Zdzislaw Salamon, Scott Cowell, Victor J. Hruby

Research output: Contribution to journalArticle

4 Scopus citations

Abstract

Plasmon-waveguide resonance (PWR) spectroscopy provides a highly sensitive method for characterizing the kinetics, affinities and conformational changes involved in ligand binding to G-protein coupled receptors, without the need for radioactive or other labeling strategies. In the case of the cloned δ-opioid receptor from human brain incorporated into a lipid bilayer, we have shown that affinities determined in this way are consistent with those measured by standard binding procedures using membranes or whole cells containing the receptors, and that the spectral and kinetic properties of the binding processes allow facile distinction between agonist, inverse agonist, and antagonist ligands. We have also shown by direct measurements that G-protein binding affinities and the ability to undergo GTP/GDP exchange are dependent upon the type of ligand pre-bound to the receptor. PWR spectroscopy thus provides a powerful new approach to investigating signal transduction in biological membrane systems.

Original languageEnglish (US)
Pages (from-to)3307-3311
Number of pages5
JournalLife Sciences
Volume73
Issue number26
DOIs
StatePublished - Nov 14 2003

Keywords

  • Human delta-opioid receptor
  • Ligand binding
  • Lipid bilayers
  • Plasmon-waveguide resonance spectroscopy
  • Receptor conformational states

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Pharmacology, Toxicology and Pharmaceutics(all)

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