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Conformationally Constrained Mono‐Fluorinated Arginine as a Cationic Label for Solid‐State 19 F NMR Analysis of Membrane‐Bound Peptides
Author(s) -
Michurin Oleg M.,
Tolmachova Kateryna,
Afonin Sergii,
Babii Oleg,
Grage Stephan L.,
Ulrich Anne S.,
Komarov Igor V.,
Radchenko Dmytro S.
Publication year - 2018
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/ejoc.201800473
Subject(s) - chemistry , cationic polymerization , nuclear magnetic resonance spectroscopy , amphiphile , peptide , context (archaeology) , stereochemistry , arginine , combinatorial chemistry , membrane , amino acid , crystallography , organic chemistry , biochemistry , copolymer , paleontology , polymer , biology
A conformationally constrained mono‐fluorinated analogue of arginine, (1 S ,3 S )‐1‐amino‐3‐fluoro‐3‐(guanidinomethyl)cyclobutane‐1‐carboxylic acid (F‐CbArg), has been designed as a label for solid‐state 19 F NMR spectroscopy. The compound was synthesized and its structural and functional similarity to arginine demonstrated in the context of a representative antimicrobial peptide. The cationic 19 F NMR label was incorporated into the amphiphilic helix of temporin A and provided information on water and phosphate contacts within the lipid environment, thereby demonstrating the utility of F‐CbArg in structural studies of membrane‐bound peptides.