Fluorinated interfaces drive self-association of transmembrane α helices in lipid bilayers

被引：40
|
作者：
Naarmann, N
Bilgiçer, B
Meng, H
Kumar, K [1 ]
Steinem, C
机构：
[1] Tufts New England Med Ctr, Ctr Canc, Boston, MA 02110 USA
[2] Univ Regensburg, Inst Analyt Chem Chemo & Biosensor, D-93040 Regensburg, Germany
[3] Tufts Univ, Dept Chem, Medford, MA 02155 USA
来源：
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2006年 / 45卷 / 16期
关键词：
FRET (fluorescence resonance energy transfer); membrane proteins; membranes; peptides; protein engineering;
D O I：
10.1002/anie.200503567
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
An increased tendency to self-assemble is exhibited by helical peptides with a highly fluorinated interface embedded in phospholipid membranes. A simultaneously hydrophobic and lipophobic surface obtained by replacing all interface leucine residues with hexafluoroleucine results in a significant increase in the ability of transmembrane helices to form higher-order ensembles. A = fluorescence acceptor; D = fluorescence donor. (Figure Presented) © 2006 Wiley-VCH Verlag GmbH & Co. KGaA.
引用
收藏
页码：2588 / 2591
页数：4
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