Fluorinated Interfaces Drive Self‐Association of Transmembrane α Helices in Lipid Bilayers | Zendy

Naarmann Natascha | Zendy; Bilgiçer Başar | Zendy; Meng He | Zendy; Kumar Krishna | Zendy; Steinem Claudia | Zendy

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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.

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