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.[1] 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.[2] 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.[3][4][5] Amphipols can be used to fold denatured membrane proteins to their native form[6][7] and have proven particularly precious in the field of single-particle electron cryo-microscopy (cryo-EM; see e.g. [8][9]).The properties and uses of amphipols and other non-conventional surfactants are the subject of a book by Jean-Luc Popot.[10]
See also[edit]
- 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[edit]
- ^ 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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