Living Reference Work Entry

Modern Magnetic Resonance

pp 1-18

Date: Latest Version

Solid-State 19F-NMR Analysis of Peptides in Oriented Biomembranes

  • Erik StrandbergAffiliated withInstitute of Biological Interfaces (IBG-2), Karlsruhe Institute of Technology (KIT) Email author 
  • , Anne S. UlrichAffiliated withInstitute of Biological Interfaces (IBG-2), Karlsruhe Institute of Technology (KIT)Institute of Organic Chemistry (IOC), Karlsruhe Institute of Technology (KIT)


Solid-state 19F-NMR is a powerful method used to study membrane-active peptides under quasi-native conditions in lipid bilayers. As shown in this chapter, it is possible to determine the conformation, orientation, dynamics, and aggregation behavior of peptides in membranes. Compared with other nuclei, 19F provides a stronger signal, thus making it possible to study peptides at low concentrations (at peptide-to-lipid molar ratios as low as 1:3000) and to determine long distances between two labels (up to 11 Å in fluid bilayers). The method is well established and has been applied to a number of antimicrobial, cell-penetrating, and fusogenic peptides that form α-helices, β-sheets, or more irregular structures, and the results are summarized here. Several new 19F-labeled amino acids that have been recently introduced are described. With these, it is now possible to replace not only hydrophobic but also polar or charged amino acids without significant perturbation, thus making solid-state 19F-NMR a highly versatile tool for characterizing peptide-lipid interactions.


Alpha-helical peptides Antimicrobial peptides Beta-sheet peptides Cell-penetrating peptides Distance measurements Fusogenic peptides Membrane-active peptides Oriented samples Peptide orientation, dynamics and aggregation Solid-state 19F-NMR 19F-labeled amino acids 19F-19F dipolar couplings