Abstract
Several different membrane-active peptides were labeled with a variety of fluorinated amino acids for structure analysis by solid state 19 F NMR. Namely, 4-F-Phg/4-CF 3 -Phg, 3,3,3-F 3 -Ala/3-F-Ala, and 2-CF 3 -Ala were used to replace a single amino acid such as Ile/Leu, Ala, and Aib, respectively, without significantly perturbing the peptide conformation or function. These NMR reporter groups can be analyzed to calculate the structure and mobility of the peptide in the lipid bilayer. This review focuses on synthetic challenges with 19 F-labeled amino acids, such as racemization and fluorine elimination, and recent results on various antimicrobial and fusogenic peptides in model membranes will be summarized.
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