Fluidizing the Membrane by a Local Anesthetic: Phenylethanol Affects Membrane Protein Oligomerization

被引:33
作者
Anbazhagan, Veerappan [1 ,2 ]
Munz, Carmen [2 ]
Tome, Lydia [1 ]
Schneider, Dirk [1 ]
机构
[1] Johannes Gutenberg Univ Mainz, Inst Pharm & Biochem, D-55128 Mainz, Germany
[2] Univ Freiburg, Inst Biochem & Mol Biol, ZBMZ, D-79104 Freiburg, Germany
关键词
anesthetic; glycophorin A; helix-helix interaction; membrane; TOXCAT; TRANSMEMBRANE HELIX DIMER; GENERAL-ANESTHESIA; DIMERIZATION; ACTIVATION;
D O I
10.1016/j.jmb.2010.10.026
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The exact mechanism of action of anesthetics is still an open question While some observations suggest specific anesthetic protein mterachons, nonspecific perturbation of the lipid bilayer has also been suggested Perturbations of bilayer properties could subsequently affect the structure and function of membrane proteins Addition of the local anesthetic phenylethanol (PEtOH) to model membranes and intact Escherichia colt cells not only affected membrane fluidity but also severely altered the defined helix helix interaction within the membrane This experimental observation suggests that certain anesthetics modulate membrane physical properties and thereby indirectly affect transmembrane (TM) helix helix interactions, which are not only involved in membrane protein folding and assembly but also important for TM signaling (C) 2010 Elsevier Ltd All rights reserved
引用
收藏
页码:773 / 777
页数:5
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