Amphipols
Amphipols (a portmanteau of amphiphilic polymers) are a class of amphiphilic polymers designed to keep membrane proteins soluble in water without the need for detergents, which are traditionally used to this end but tend to be denaturing. Amphipols adsorb onto the hydrophobic transmembrane surface of membrane proteins thanks to their hydrophobic moieties and keep the complexes thus formed water-soluble thanks to the hydrophilic ones. Amphipol-trapped membrane proteins are, as a rule, much more stable than detergent-solubilized ones, which facilitates their study by most biochemical and biophysical approaches. Amphipols can be used to fold denatured membrane proteins to their native form and have proven particularly precious in the field of single-particle electron cryo-microscopy (cryo-EM; see e.g. ).The properties and uses of amphipols and other non-conventional surfactants are the subject of a book by Jean-Luc Popot.
See also
- Peptitergents - synthetic peptide sequences which can substitute to detergents to keep membrane proteins water-soluble.
- Nanodisc - water-soluble protein-stabilized lipid discs that can trap and stabilize membrane proteins.
References
- ↑ Bowie, J (2001). "Stabilizing membrane proteins". Current Opinion in Structural Biology. 11 (4): 397–402. doi:10.1016/S0959-440X(00)00223-2. ISSN 0959-440X. PMID 11495729.
- ↑ Tribet, C; Audebert, R; Popot, JL (24 December 1996). "Amphipols: polymers that keep membrane proteins soluble in aqueous solutions". Proceedings of the National Academy of Sciences of the United States of America. 93 (26): 15047–50. Bibcode:1996PNAS...9315047T. doi:10.1073/pnas.93.26.15047. PMC 26353. PMID 8986761.
- ↑ Popot, J.-L., et al. (2011) Amphipols from A to Z. Annu. Rev. Biophys. 40:379-408.
- ↑ Zoonens, M., Popot, J.-L. (2014) Amphipols for each season. J. Membr. Biol. 247:759-796.
- ↑ Popot, J.-L. (2018) Membrane proteins in aqueous solutions: From detergents to amphipols. Springer, New York, in the press.
- ↑ Pocanschi, C.L., Dahmane, T., Gohon, Y., Rappaport, F., Apell, H.-J., Kleinschmidt, J.H., Popot, J.-L. (2006) Amphipathic polymers: tools to fold integral membrane proteins to their active form. Biochemistry 45:13954-13961.
- ↑ Dahmane, T., Damian, M., Mary, S., Popot, J.-L., Banères, J.-L. (2009) Amphipol-assisted in vitro folding of G protein-coupled receptors. Biochemistry 48:6516-6521.
- ↑ Althoff, T., Mills, D.J., Popot, J.-L., Kühlbrandt, W. (2011) Assembly of electron transport chain components in bovine mitochondrial supercomplex I1III2IV1. EMBO J. 30:4652-4664.
- ↑ Liao, M., Cao, E., Julius, D., Cheng, Y. (2013) Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature 504:107-112.
- ↑ Popot, J.-L. (2018) Membrane proteins in aqueous solutions. From detergents to amphipols. Springer, New York, xxv + 708 p.
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