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 increase in the ability of transmembrane helices to form higher‐order ensembles. A=fluorescence acceptor; D=fluorescence donor.