The Journal of Membrane Biology

, Volume 247, Issue 9–10, pp 853–860 | Cite as

Amphipols in G Protein-Coupled Receptor Pharmacology: What Are They Good For?

  • Sophie Mary
  • Marjorie Damian
  • Rita Rahmeh
  • Bernard Mouillac
  • Jacky Marie
  • Sébastien Granier
  • Jean-Louis BanèresEmail author


G protein-coupled receptors are at a central node of all cell communications. Investigating their molecular functioning is therefore crucial for both academic purposes and drug design. However, getting the receptors as isolated, stable and purified proteins for such studies still stumbles over their instability out of the membrane environment. Different membrane-mimicking environments have been developed so far to increase the stability of purified receptors. Among them are amphipols. These polymers not only preserve the native fold of receptors purified from membrane fractions but they also allow specific applications such as folding receptors purified from inclusion bodies back to their native state. Of importance, amphipol-trapped G protein-coupled receptors essentially maintain their pharmacological properties so that they are perfectly adapted to further investigate the molecular mechanisms underlying signaling processes. We review here how amphipols have been used to refold and stabilize detergent-solubilized purified receptors and what are the main subsequent molecular pharmacology analyses that were performed using this strategy.


GPCR Amphipol G Protein Arrestin Ligand 



5-Hydroxytryptamine receptor 4


12S-Hydroxyheptadeca-5Z, 8E,10E-trienoic acid


Polyacrylate-based amphipol A8-35




Leukotriene B4 receptor 1


Leukotriene B4 receptor 2


Cannabinoid receptor 1


Cross-correlated relaxation-enhanced polarization transfer


C-X-C chemokine receptor 1




Fluorescence resonance energy transfer


Outer membrane protein A from Fusobacterium nucleatum


Ghrelin receptor type 1


G protein-coupled receptor


Inclusion bodies


Luminescence resonance energy transfer


Leukotriene B4




Outer membrane protein A from Escherichia coli


Non-ionic amphipol


Nuclear magnetic resonance


Spodoptera frugiperda


Vasopressin receptor 2



We are particularly indebted to J.-L. Popot (IBPC, Paris) for his invaluable contribution to all this work. We also wish to thank L. Catoire and M. Zoonens (IBPC, Paris) for helpful discussions. This work was supported by CNRS and National Agency of Research Grants ANR 06-BLAN-0087, ANR-10-BLAN-1208 and PCV08_323163.


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Copyright information

© Springer Science+Business Media New York 2014

Authors and Affiliations

  • Sophie Mary
    • 1
  • Marjorie Damian
    • 1
  • Rita Rahmeh
    • 2
  • Bernard Mouillac
    • 2
  • Jacky Marie
    • 1
  • Sébastien Granier
    • 2
  • Jean-Louis Banères
    • 1
    Email author
  1. 1.Faculté de Pharmacie, Institut des Biomolécules Max Mousseron (IBMM), CNRS UMR 5247Université Montpellier 1 et 2Montpellier Cedex 5France
  2. 2.Institut de Génomique Fonctionnelle (IGF), CNRS UMR 5203, INSERM U661Université Montpellier 1 et 2Montpellier Cedex 05France

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