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The Use of Amphipols for Solution NMR Studies of Membrane Proteins: Advantages and Constraints as Compared to Other Solubilizing Media

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Abstract

Solution-state nuclear magnetic resonance studies of membrane proteins are facilitated by the increased stability that trapping with amphipols confers to most of them as compared to detergent solutions. They have yielded information on the state of folding of the proteins, their areas of contact with the polymer, their dynamics, water accessibility, and the structure of protein-bound ligands. They benefit from the diversification of amphipol chemical structures and the availability of deuterated amphipols. The advantages and constraints of working with amphipols are discussed and compared to those associated with other non-conventional environments, such as bicelles and nanodiscs.

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Abbreviations

APol:

Amphipol

A8-35:

Polyacrylate-based amphipol A8-35

BLT2:

Low-affinity leukotriene receptor

BR:

Bacteriorhodopsin

C8E4 :

Octyltetraoxyethylene

CFE:

Cell-free expression

CRINEPT:

Cross-correlated relaxation-enhanced polarization transfer

DHPC:

Dihexanoylphosphatidylcholine

DAPol:

A8-35 with perdeuterated octyl and isopropyl chains and a hydrogenated polyacrylate backbone

DPC:

n-Dodecylphosphocholine

DDM:

n-Dodecyl-β-d-maltopyranoside

GPCR:

G protein-coupled receptor

12-HHT:

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

HOESY:

Hetero-nuclear Overhauser spectroscopy

12-HETE:

12S-Hydroxy-5Z,8Z,10E,14Z-eicosatetraenoic acid

HSQC:

Hetero-single quantum correlation experiment

KpOmpA:

Outer membrane protein A from Klebsiella pneumoniae

LTB4 :

Leukotriene B4

MD:

Molecular dynamics

MP:

Membrane protein

MW:

Molecular weight

NAPol:

Non-ionic amphipol

MNG:

Maltose neopentyl glycol

NMR:

Nuclear magnetic resonance

NOE:

Nuclear Overhauser effect

ND:

Nanodisc

OmpA:

Outer membrane protein A from Escherichia coli

OmpX:

Outer membrane protein X from Escherichia coli

perDAPol:

Perdeuterated A8-35

PC-APol:

Phosphocholine amphipol

R S :

Stokes radius

SAPol:

Sulfonated amphipol

SDS:

Sodium dodecylsulfate

ssNMR:

Solid-state NMR

SEC:

Size exclusion chromatography

tOmpA:

Transmembrane domain of OmpA

TROSY:

Transverse relaxation optimized spectroscopy

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Acknowledgments

We are extremely grateful to Sophie Walmé and Marie-Noëlle Rager (ChimieParisTech, Paris), and Carine van Heijenoort (ICSN, Gif/Yvette) for assistance with NMR experiments. We express our gratitude to B. Pucci (Université d’Avignon et des Pays de Vaucluse) for his long-term involvement in the development of non-ionic amphipols. This work was supported by the Centre National de la Recherche Scientifique (CNRS), Paris-7 University (Sorbonne Paris Cité), the “Initiative d’Excellence” program from the French State (Grant “DYNAMO,” ANR-11-LABX-0011-01), Human Frontier Science Program Organization Grant RG00223/2000-M, from the Agence Nationale pour la Recherche ANR-07-BLAN-0092 “Amphipol-assisted folding of GPCRs,” and E.U. Specific Targeted Research Project “Innovative tools for membrane protein structural proteomics.” LJC is a recipient of Projects Exploratoires/Premier Soutien (PEPS, LeukomotiVe project) from the CNRS.

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Author notes

  1. Noelya Planchard

    Present address: Centre de Versailles-Grignon, Institut Jean-Pierre Bourgin, UMR 1318 INRA-AgroParisTech, Bâtiment 7, INRA, Route de St-Cyr, 78026, Versailles Cedex, France

  2. Tassadite Dahmane

    Present address: Department of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168th Street, 202 BB, New York, NY, 10032, USA

Authors and Affiliations

  1. Laboratoire de Biologie Physico-Chimique des Protéines Membranaires, Institut de Biologie Physico-Chimique (FRC 550), UMR 7099, CNRS, Université Paris 7, 13 rue Pierre et Marie Curie, 75005, Paris, France

    Noelya Planchard, Élodie Point, Tassadite Dahmane, Fabrice Giusti, Christel Le Bon, Manuela Zoonens, Jean-Luc Popot & Laurent J. Catoire

  2. Laboratoire de RMN et des interactions protéines/membranes, CNRS, Institut de Pharmacologie et de Biologie Structurale, 205 route de Narbonne, BP64182, 31077, Toulouse, France

    Marie Renault & Alain Milon

  3. Equipe Chimie Bioorganique et Systèmes Amphiphiles, Université d’Avignon et des Pays de Vaucluse, 33 rue Louis Pasteur, 84000, Avignon, France

    Grégory Durand

  4. Institut des Biomolécules Max Mousseron (UMR 5247), 15 avenue Charles Flahault, 34093, Montpellier Cedex 05, France

    Grégory Durand

  5. Centre de Recherche de Gif, Laboratoire de Chimie et Biologie Structurales, UPR 2301 CNRS, ICSN, 91198, Gif-sur-Yvette, France

    Éric Guittet

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  1. Noelya Planchard
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Planchard, N., Point, É., Dahmane, T. et al. The Use of Amphipols for Solution NMR Studies of Membrane Proteins: Advantages and Constraints as Compared to Other Solubilizing Media. J Membrane Biol 247, 827–842 (2014). https://doi.org/10.1007/s00232-014-9654-z

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