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Fluorinated Interfaces Drive Self‐Association of Transmembrane α Helices in Lipid Bilayers
Author(s) -
Naarmann Natascha,
Bilgiçer Başar,
Meng He,
Kumar Krishna,
Steinem Claudia
Publication year - 2006
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200503567
Subject(s) - transmembrane protein , phospholipid , transmembrane domain , fluorescence , membrane , biophysics , chemistry , lipid bilayer , interface (matter) , crystallography , molecule , biochemistry , organic chemistry , biology , receptor , physics , quantum mechanics , gibbs isotherm
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.