Martinez Karen L, Gohon Yann, Corringer Pierre-Jean, Tribet Christophe, Mérola Fabienne, Changeux Jean-Pierre, Popot Jean-Luc
Unité de Neurobiologie Moléculaire, CNRS URA 2182, Institut Pasteur, 25 rue du Dr Roux, 75734 Paris, France.
FEBS Lett. 2002 Sep 25;528(1-3):251-6. doi: 10.1016/s0014-5793(02)03306-9.
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.
通过时间分辨光谱法，在三种不同环境下研究了荧光激动剂与电鳐电器官乙酰胆碱受体的结合：天然膜片段中、去污剂CHAPS中以及经两亲聚合物（“两亲分子”）络合后。膜中和两亲分子中的结合动力学相似，表明该受体在其天然脂质环境之外能展现未改变的变构转变。相比之下，在CHAPS中变构平衡强烈地向脱敏状态偏移。因此，CHAPS的作用可能源于分子间相互作用，而非膜环境整体物理性质的丧失。
