Amphipols from a to Z*

J. L. Popot, T. Althoff, D. Bagnard, J. L. Banéres, P. Bazzacco, E. Billon-Denis, L. 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. KleinschmidtW. Kühlbrandt, C. Le Bon, K. L. Martinez, M. Picard, B. Pucci, J. N. Sachs, C. Tribet, C. Van Heijenoort, F. Wien, F. Zito, M. Zoonens

Research output: Contribution to journalArticlepeer-review

205 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)379-408
Number of pages30
JournalAnnual Review of Biophysics
Volume40
Issue number1
DOIs
StatePublished - Jun 9 2011

Keywords

  • amphipathic polymers
  • membrane biochemistry
  • membrane biophysics
  • membrane proteins

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