Design, Synthesis, and Application of an Optimized Monofluorinated Aliphatic Label for Peptide Studies by Solid-State 19FNMR Spectroscopy

A conformationally restricted monofluorinated [alpha]-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 19F NMR spectroscopy. The compound was synthesized and validated as a 19F label for replacing...

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Bibliographic Details
Published inAngewandte Chemie International Edition Vol. 55; no. 47; p. 14788
Main 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
Format Journal Article
LanguageEnglish
Published Weinheim Wiley Subscription Services, Inc 14.11.2016
EditionInternational ed. in English
Subjects
Aliphatic compounds
Amino acids
Antiinfectives and antibacterials
Design
Design analysis
Design optimization
Glycine
Information dissemination
Lipophilicity
Magnetic resonance spectroscopy
Mathematical analysis
NMR spectroscopy
Peptides
Spectroscopic analysis
Spectrum analysis
Structural analysis
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Summary:A conformationally restricted monofluorinated [alpha]-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 19F NMR spectroscopy. The compound was synthesized and validated as a 19F label for replacing natural aliphatic [alpha]-amino acids. Calculations suggested that F-Bpg is similar to Leu/Ile in terms of size and lipophilicity. The 19F NMR label was incorporated into the membrane-active antimicrobial peptide PGLa and provided information on the structure of the peptide in a lipid bilayer.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201608116