Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: Molecular interactions vs. physical constraints

Karen L. Martinez; Yann Gohon; Pierre Jean Corringer; Christophe Tribet; Fabienne Mérola; Jean Pierre Changeux; Jean Luc Popot

doi:10.1016/S0014-5793(02)03306-9

Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: Molecular interactions vs. physical constraints

Karen L. Martinez, Yann Gohon, Pierre Jean Corringer, Christophe Tribet, Fabienne Mérola, Jean Pierre Changeux, Jean Luc Popot^*

^*Corresponding author for this work

Department of Chemistry

53 Citations (Scopus)

Abstract

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.

Original language	English
Journal	FEBS Letters
Volume	528
Issue number	1-3
Pages (from-to)	251-256
Number of pages	6
ISSN	0014-5793
DOIs	https://doi.org/10.1016/S0014-5793(02)03306-9
Publication status	Published - 25 Sept 2002

Keywords

Amphipol
Conformational transition
Detergent
Membrane protein
Nicotinic acetylcholine receptor

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10.1016/S0014-5793(02)03306-9

http://www.scopus.com/inward/record.url?scp=0037174145&partnerID=8YFLogxK

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title = "Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: Molecular interactions vs. physical constraints",

abstract = "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.",

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T1 - Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols

T2 - Molecular interactions vs. physical constraints

AU - Martinez, Karen L.

AU - Gohon, Yann

AU - Corringer, Pierre Jean

AU - Tribet, Christophe

AU - Mérola, Fabienne

AU - Changeux, Jean Pierre

AU - Popot, Jean Luc

PY - 2002/9/25

Y1 - 2002/9/25

N2 - 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.

AB - 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.

KW - Amphipol

KW - Conformational transition

KW - Detergent

KW - Membrane protein

KW - Nicotinic acetylcholine receptor

U2 - 10.1016/S0014-5793(02)03306-9

DO - 10.1016/S0014-5793(02)03306-9

M3 - Journal article

C2 - 12297315

AN - SCOPUS:0037174145

SN - 0014-5793

VL - 528

SP - 251

EP - 256

JO - F E B S Letters

JF - F E B S Letters

IS - 1-3

ER -

Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: Molecular interactions vs. physical constraints

Abstract

Keywords

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