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

页码：2588 / 2591

页数：4

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