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 language | English (US) |
---|---|
Pages (from-to) | 379-408 |
Number of pages | 30 |
Journal | Annual Review of Biophysics |
Volume | 40 |
Issue number | 1 |
DOIs | |
State | Published - Jun 9 2011 |
Keywords
- amphipathic polymers
- membrane biochemistry
- membrane biophysics
- membrane proteins