Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: molecular interactions vs. physical constraints.
The binding of a fluorescent agonist to the acetycholine receptor from Torpedo electric organ has been studied by time-resolved spectroscopy in three different environments: in native membrane fragments, in the detergent CHAPS, and after complexation by amphipathic polymers ('amphipols'). Binding kinetics was similar in the membrane and in amphipols, demonstrating that the receptor can display unaltered allosteric transitions outside its natural lipid environment. In contrast, allosteric equilibria were strongly shifted towards the desensitized state in CHAPS. Therefore, the effect of CHAPS likely results from molecular interactions rather than from the loss of bulk physical properties of the membrane environment.
Martinez
Karen L
KL
Unité de Neurobiologie Moléculaire, CNRS URA 2182, Institut Pasteur, 25 rue du Dr Roux, 75734 Paris, France.
Gohon
Yann
Y
Corringer
Pierre-Jean
PJ
Tribet
Christophe
C
Mérola
Fabienne
F
Changeux
Jean-Pierre
JP
Popot
Jean-Luc
JL
D000494:Allosteric Regulation; D000818:Animals; D001665:Binding Sites; D002793:Cholic Acids; D003902:Detergents; D004557:Electric Organ / Q000378:metabolism; D005456:Fluorescent Dyes; D066298:In Vitro Techniques; D008055:Lipids; D011487:Protein Conformation; D011978:Receptors, Nicotinic / Q000737:chemistry* / Q000378:metabolism*; D012995:Solubility; D013501:Surface-Active Agents; D014101:Torpedo / Q000378:metabolism*
D002793:Cholic Acids; D003902:Detergents; D005456:Fluorescent Dyes; D008055:Lipids; D011978:Receptors, Nicotinic; D013501:Surface-Active Agents; C028213:3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate