Design, Synthesis, and Application of an Optimized Monofluorinated Aliphatic Label for Peptide Studies by Solid‐State 19F NMR Spectroscopy. Issue 47 (5th October 2016)

• Record Type: Journal Article
• Authors: Kokhan, Serhii O.; Tymtsunik, Andriy V.; Grage, Stephan L.; Afonin, Sergii; Babii, Oleg; Berditsch, Marina; Strizhak, Alexander V.; Bandak, Dmytro; Platonov, Maxim O.; Komarov, Igor V.; Ulrich, Anne S.; Mykhailiuk, Pavel K.
• Is Part Of: Angewandte Chemie international edition. Volume 55:Issue 47(2016)
• Page Start: 14788
• Page End: 14792
• Publication Date: 2016-10-05
• Subjects: amino acids -- fluorine -- peptides -- propellanes -- solid-state NMR spectroscopy; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201608116
• Languages: English
• ISSNs: 1433-7851

Abstract

Abstract: A conformationally restricted monofluorinated α‐amino acid, (3‐fluorobicyclo[1.1.1]pentyl)glycine (F‐Bpg), was designed as a label for the structural analysis of membrane‐bound peptides by solid‐state 19 F NMR spectroscopy. The compound was synthesized and validated as a 19 F label for replacing natural aliphatic α‐amino acids. Calculations suggested that F‐Bpg is similar to Leu/Ile in terms of size and lipophilicity. The 19 F NMR label was incorporated into the membrane‐active antimicrobial peptide PGLa and provided information on the structure of the peptide in a lipid bilayer. Abstract : A conformationally restricted monofluorinated α‐amino acid was synthesized and used as a 19 F label to replace aliphatic amino acids in peptides. Its incorporation into the membrane‐active antimicrobial peptide PGLa demonstrated its applicability for peptide structure analysis and distance measurements by 19 F NMR spectroscopy.