Fluorinated Interfaces Drive Self-Association of Transmembrane α Helices in Lipid Bilayers

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 inc...

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Veröffentlicht in:	Angewandte Chemie International Edition 2006-04, Vol.45 (16), p.2588-2591
Hauptverfasser:	Naarmann, Natascha, Bilgiçer, Başar, Meng, He, Kumar, Krishna, Steinem, Claudia
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Circular Dichroism Fluorine - chemistry FRET (fluorescence resonance energy transfer) Lipid Bilayers - chemistry membrane proteins Membrane Proteins - chemistry membranes Molecular Sequence Data peptides protein engineering Protein Structure, Secondary
Online-Zugang:	Volltext
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