A new generation of Amphipols is here. They differ from the old Amphipols mainly by the replacement of linear octyl chains for hydrophobic, saturated cycles (Marconnet, Michon and Le Bon et al. 2020). Due to this change the polymer remarkably improves its ability to extract membrane proteins from a biological membrane, regardless to the membrane and the protein of interest, while maintaining the native structure of the target.
Copolymers provide a hydrophobic surface facing the lipids, and a hydrophilic surface at the outside. This setup makes nanodiscs highly soluble in aqueous solutions and allows for the solubilization of membrane proteins in the absence of detergents.
As a secondary possibility the products can be used to creat 100% artificial nanodiscs. Phospholipids such as dimyristoyl-glycero-phosphocholine (DMPC) or palmitoyl-oleoyl-phosphatidyl-choline (POPC) have been proven to work here in combination with sodium cholate.
|Name||Adsorbance (280 nm, 1% solution)||Molecular Weigth||COA/AA Ratio||Solubility||pH (dissolved)|
|Ultrasolute™ Amphipol 17 |
|below 0.1 ||7,300 Da ||1:1 ||10% (H2O) ||7.5 ± 0.3 |
|Ultrasolute™ Amphipol 18 ||below 0.1 ||7,300 Da ||1:1 ||10% (H2O) ||7.5 ± 0.3 |
The complex from UltrasoluteTM Amphipol and membrane protein can be used with many biophysical assays, such as SDS-PAGE, SEC, Western Blot, UV/Vis spectroscopy, and many chromatographic procedures.
Ultrasolute™ - The next generation of Amphipols
Figure 1: Comparison between the original Amphipols from 1996 and our Ultrasolute™ Amphipols
- Anaïs Marconnet, Baptiste Michon, Christel Le Bon, Fabrice Giusti, Christophe Tribet, and Manuela Zoonens* ; Solubilization and stzabilization of membrane proteins by cycloalkane-modified Amphiphilic polymers, Biomacromolecules 2020, 21, 8, 3459–3467
- Anna J. Higgins, Alex J. Flynn, Anaïs Marconnet, Laura J. Musgrove , Vincent L. G. Postis, Jonathan D. Lippiat , Chun-wa Chung, Tom Ceska, Manuela Zoonens, Frank Sobott, and Stephen P. Muench, Cycloalkane-modified amphiphilic polymers provide direct extraction of membrane proteins for CryoEM analysis, Communications Biology, volume 4, Article number: 1337, 2021