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Design, Synthesis, and Application of an Optimized Monofluorinated Aliphatic Label for Peptide Studies by Solid‐State 19 F NMR Spectroscopy
Author(s) -
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.
Publication year - 2016
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201608116
Subject(s) - lipophilicity , chemistry , peptide , fluorine 19 nmr , nuclear magnetic resonance spectroscopy , glycine , lipid bilayer , amino acid , spectroscopy , stereochemistry , solid state nuclear magnetic resonance , combinatorial chemistry , nuclear magnetic resonance spectroscopy of nucleic acids , membrane , biochemistry , nuclear magnetic resonance , transverse relaxation optimized spectroscopy , physics , quantum mechanics
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.