| 词条 | Amphipols |
| 释义 |
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
References1. ^{{cite journal|last1=Bowie|first1=J|title=Stabilizing membrane proteins|journal=Current Opinion in Structural Biology|volume=11|issue=4|year=2001|pages=397–402|issn=0959-440X|doi=10.1016/S0959-440X(00)00223-2}} {{protein-stub}}2. ^{{cite journal|last1=Tribet|first1=C|last2=Audebert|first2=R|last3=Popot|first3=JL|title=Amphipols: polymers that keep membrane proteins soluble in aqueous solutions.|journal=Proceedings of the National Academy of Sciences of the United States of America|date=24 December 1996|volume=93|issue=26|pages=15047–50|pmid=8986761|doi=10.1073/pnas.93.26.15047|pmc=26353|bibcode=1996PNAS...9315047T}} 3. ^ Popot, J.-L., et al. (2011) Amphipols from A to Z. Annu. Rev. Biophys. 40:379-408. 4. ^Zoonens, M., Popot, J.-L. (2014) Amphipols for each season. J. Membr. Biol. 247:759-796. 5. ^Popot, J.-L. (2018) Membrane proteins in aqueous solutions: From detergents to amphipols. Springer, New York, in the press. 6. ^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. 7. ^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. 8. ^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. 9. ^Liao, M., Cao, E., Julius, D., Cheng, Y. (2013) Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature 504:107-112. 10. ^Popot, J.-L. (2018) Membrane proteins in aqueous solutions. From detergents to amphipols. Springer, New York, xxv + 708 p. 1 : Surfactants |
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