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Detection of ligand-receptor binding using microfluidic frontal affinity chromatography on proteoliposomes derived directly from native cell membranes

Journal article
Authors K. Olesen
R. Karlsson
Ulrika Lind
M. Davidson
Anders Blomberg
A. Karlsson
Published in Journal of Chromatography B-Analytical Technologies in the Biomedical and Life Sciences
Volume 931
Pages 84-89
ISSN 1570-0232
Publication year 2013
Published at Department of Chemistry and Molecular Biology
Pages 84-89
Language en
Links dx.doi.org/10.1016/j.jchromb.2013.0...
Keywords Microfluidics, Frontal affinity chromatography, Ligand-receptor binding, GPCR, Mass spectrometry, mass spectrometry, identification, proteins
Subject categories Analytical Chemistry

Abstract

A method for characterization of ligand binding to membrane receptors in their native cell membrane is presented. The methodology is based on microfluidic frontal affinity chromatography coupled to mass spectrometry (FAC-MS). Proteoliposomes with receptor of interest are prepared directly from cell membranes and serve as a stationary phase in a microfluidic flow cell for frontal analysis. The G-Protein-Coupled Receptor (GPCR) Ste2 involved in the pheromone-induced yeast mating pathway is used as a model receptor for proof of principle characterization. The ligand affinity of the natural pheromone peptide, the alpha-factor, is compared to a set of pheromone analogs having different receptor affinities. With short preparation time, preserved lipid composition and the ability to immobilize proteoliposomes from any cell membrane, we propose that our methodology with immobilized proteoliposomes together with microfluidics FAC-MS can be an important improvement for ligand-receptor studies in native membranes.

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