Amphipols from A to Z

J-L Popot; T Althoff; D Bagnard; J-L Banères; P Bazzacco; E Billon-Denis; Laurent J.  Catoire; P Champeil; D Charvolin; M J Cocco; G Crémel; T Dahmane; L M de la Maza; C Ebel; F Gabel; F Giusti; Y Gohon; E Goormaghtigh; E Guittet; J. H.  Kleinschmidt; W Kühlbrandt; C Le Bon; Karen Laurence Martinez; M Picard; B Pucci; J N  Sachs; C Tribet; C Van Heijenoort; F Wien; F Zito; M Zoonens

doi:10.1146/annurev-biophys-042910-155219

Amphipols from A to Z

J-L Popot
, T Althoff
, D Bagnard
, J-L Banères
, P Bazzacco
, E Billon-Denis
, Laurent J. Catoire
, P Champeil
, D Charvolin
, M J Cocco
, G Crémel
, T Dahmane
, L M de la Maza
, C Ebel
, F Gabel
, F Giusti
, Y Gohon
, E Goormaghtigh
, E Guittet
, J. H. Kleinschmidt

W Kühlbrandt, C Le Bon, Karen Laurence Martinez, M Picard, B Pucci, J N Sachs, C Tribet, C Van Heijenoort, F Wien, F Zito, M Zoonens

Institut for Neurovidenskab

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

Abstract

Amphipols (APols) are short amphipathic polymers that can substitute for detergents to keep integral membrane proteins (MPs) water soluble. In this review, we discuss their structure and solution behavior; the way they associate with MPs; and the structure, dynamics, and solution properties of the resulting complexes. All MPs tested to date form water-soluble complexes with APols, and their biochemical stability is in general greatly improved compared with MPs in detergent solutions. The functionality and ligand-binding properties of APol-trapped MPs are reviewed, and the mechanisms by which APols stabilize MPs are discussed. Applications of APols include MP folding and cell-free synthesis, structural studies by NMR, electron microscopy and X-ray diffraction, APol-mediated immobilization of MPs onto solid supports, proteomics, delivery of MPs to preexisting membranes, and vaccine formulation.

Originalsprog	Engelsk
Tidsskrift	Annual Review of Biophysics
Vol/bind	40
Sider (fra-til)	379-408
Antal sider	30
ISSN	1936-122X
DOI	https://doi.org/10.1146/annurev-biophys-042910-155219
Status	Udgivet - jun. 2011

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10.1146/annurev-biophys-042910-155219

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Citationsformater

Popot, J.-L., Althoff, T., Bagnard, D., Banères, J.-L., Bazzacco, P., Billon-Denis, E., Catoire, L. J., Champeil, P., Charvolin, D., Cocco, M. J., Crémel, G., Dahmane, T., de la Maza, L. M., Ebel, C., Gabel, F., Giusti, F., Gohon, Y., Goormaghtigh, E., Guittet, E., ... Zoonens, M. (2011). Amphipols from A to Z. Annual Review of Biophysics, 40, 379-408. https://doi.org/10.1146/annurev-biophys-042910-155219

Popot, J-L, Althoff, T, Bagnard, D, Banères, J-L, Bazzacco, P, Billon-Denis, E, Catoire, LJ, Champeil, P, Charvolin, D, Cocco, MJ, Crémel, G, Dahmane, T, de la Maza, LM, Ebel, C, Gabel, F, Giusti, F, Gohon, Y, Goormaghtigh, E, Guittet, E, Kleinschmidt, JH, Kühlbrandt, W, Le Bon, C, Martinez, KL, Picard, M, Pucci, B, Sachs, JN, Tribet, C, Van Heijenoort, C, Wien, F, Zito, F & Zoonens, M 2011, 'Amphipols from A to Z', Annual Review of Biophysics, bind 40, s. 379-408. https://doi.org/10.1146/annurev-biophys-042910-155219

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title = "Amphipols from A to Z",

abstract = "Amphipols (APols) are short amphipathic polymers that can substitute for detergents to keep integral membrane proteins (MPs) water soluble. In this review, we discuss their structure and solution behavior; the way they associate with MPs; and the structure, dynamics, and solution properties of the resulting complexes. All MPs tested to date form water-soluble complexes with APols, and their biochemical stability is in general greatly improved compared with MPs in detergent solutions. The functionality and ligand-binding properties of APol-trapped MPs are reviewed, and the mechanisms by which APols stabilize MPs are discussed. Applications of APols include MP folding and cell-free synthesis, structural studies by NMR, electron microscopy and X-ray diffraction, APol-mediated immobilization of MPs onto solid supports, proteomics, delivery of MPs to preexisting membranes, and vaccine formulation.",

author = "J-L Popot and T Althoff and D Bagnard and J-L Ban{\`e}res and P Bazzacco and E Billon-Denis and Catoire, \{Laurent J.\} and P Champeil and D Charvolin and Cocco, \{M J\} and G Cr{\'e}mel and T Dahmane and \{de la Maza\}, \{L M\} and C Ebel and F Gabel and F Giusti and Y Gohon and E Goormaghtigh and E Guittet and Kleinschmidt, \{J. H.\} and W K{\"u}hlbrandt and \{Le Bon\}, C and Martinez, \{Karen Laurence\} and M Picard and B Pucci and Sachs, \{J N\} and C Tribet and \{Van Heijenoort\}, C and F Wien and F Zito and M Zoonens",

year = "2011",

month = jun,

doi = "10.1146/annurev-biophys-042910-155219",

language = "English",

volume = "40",

pages = "379--408",

journal = "Annual Review of Biophysics",

issn = "1936-122X",

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T1 - Amphipols from A to Z

AU - Popot, J-L

AU - Althoff, T

AU - Bagnard, D

AU - Banères, J-L

AU - Bazzacco, P

AU - Billon-Denis, E

AU - Catoire, Laurent J.

AU - Champeil, P

AU - Charvolin, D

AU - Cocco, M J

AU - Crémel, G

AU - Dahmane, T

AU - de la Maza, L M

AU - Ebel, C

AU - Gabel, F

AU - Giusti, F

AU - Gohon, Y

AU - Goormaghtigh, E

AU - Guittet, E

AU - Kleinschmidt, J. H.

AU - Kühlbrandt, W

AU - Le Bon, C

AU - Martinez, Karen Laurence

AU - Picard, M

AU - Pucci, B

AU - Sachs, J N

AU - Tribet, C

AU - Van Heijenoort, C

AU - Wien, F

AU - Zito, F

AU - Zoonens, M

PY - 2011/6

Y1 - 2011/6

N2 - Amphipols (APols) are short amphipathic polymers that can substitute for detergents to keep integral membrane proteins (MPs) water soluble. In this review, we discuss their structure and solution behavior; the way they associate with MPs; and the structure, dynamics, and solution properties of the resulting complexes. All MPs tested to date form water-soluble complexes with APols, and their biochemical stability is in general greatly improved compared with MPs in detergent solutions. The functionality and ligand-binding properties of APol-trapped MPs are reviewed, and the mechanisms by which APols stabilize MPs are discussed. Applications of APols include MP folding and cell-free synthesis, structural studies by NMR, electron microscopy and X-ray diffraction, APol-mediated immobilization of MPs onto solid supports, proteomics, delivery of MPs to preexisting membranes, and vaccine formulation.

AB - Amphipols (APols) are short amphipathic polymers that can substitute for detergents to keep integral membrane proteins (MPs) water soluble. In this review, we discuss their structure and solution behavior; the way they associate with MPs; and the structure, dynamics, and solution properties of the resulting complexes. All MPs tested to date form water-soluble complexes with APols, and their biochemical stability is in general greatly improved compared with MPs in detergent solutions. The functionality and ligand-binding properties of APol-trapped MPs are reviewed, and the mechanisms by which APols stabilize MPs are discussed. Applications of APols include MP folding and cell-free synthesis, structural studies by NMR, electron microscopy and X-ray diffraction, APol-mediated immobilization of MPs onto solid supports, proteomics, delivery of MPs to preexisting membranes, and vaccine formulation.

U2 - 10.1146/annurev-biophys-042910-155219

DO - 10.1146/annurev-biophys-042910-155219

M3 - Journal article

C2 - 21545287

SN - 1936-122X

VL - 40

SP - 379

EP - 408

JO - Annual Review of Biophysics

JF - Annual Review of Biophysics

ER -