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Merck
  • Conformational antibody binding to a native, cell-free expressed GPCR in block copolymer membranes.

Conformational antibody binding to a native, cell-free expressed GPCR in block copolymer membranes.

PloS one (2014-10-21)
Hans-Peter M de Hoog, Esther M Lin JieRong, Sourabh Banerjee, Fabien M Décaillot, Madhavan Nallani
초록

G-protein coupled receptors (GPCRs) play a key role in physiological processes and are attractive drug targets. Their biophysical characterization is, however, highly challenging because of their innate instability outside a stabilizing membrane and the difficulty of finding a suitable expression system. We here show the cell-free expression of a GPCR, CXCR4, and its direct embedding in diblock copolymer membranes. The polymer-stabilized CXCR4 is readily immobilized onto biosensor chips for label-free binding analysis. Kinetic characterization using a conformationally sensitive antibody shows the receptor to exist in the correctly folded conformation, showing binding behaviour that is commensurate with heterologously expressed CXCR4.

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Sigma-Aldrich
Ethanolamine, ≥98%
Sigma-Aldrich
Ethanolamine, liquid, BioReagent, suitable for cell culture, ≥98%
Sigma-Aldrich
Ethanolamine, ≥99%
Supelco
Aucubin, analytical standard
Supelco
Ethanolamine, analytical standard
Sigma-Aldrich
Ethanolamine, puriss. p.a., ACS reagent, ≥99.0% (GC/NT)
Sigma-Aldrich
Ethanolamine, ACS reagent, ≥99.0%
Sigma-Aldrich
Ethanolamine, purified by redistillation, ≥99.5%
Aucubin, primary reference standard
Trolamine impurity A, European Pharmacopoeia (EP) Reference Standard