Design and Synthesis of a Monofluoro-Substituted Aromatic Amino Acid as a Conformationally Restricted 19F NMR Label for Membrane-Bound Peptides

Мова статті: 
Англійська
Автор(и) статті: 
Anton N. Tkachenko, Pavel K. Mykhailiuk, Dmytro S. Radchenko, Oleg Babii, Sergii Afonin, Anne S. Ulrich, and Igor V. Komarov.
Вихідні данні статті: 
Eur. J. Org. Chem. 2014, 3584–3591.
Назва журналу: 
European Journal of Organic Chemistry
Рік публікації: 
2014
Issue: 
17
Ключові слова: 
Amino acids;Proteins;Membrane proteins;Protein modifications;Fluorine;Solid-state NMR spectroscopy
Ключове слово: 
Amino acids
Ключове слово: 
Proteins
Ключове слово: 
Membrane proteins
Ключове слово: 
Protein modifications
Ключове слово: 
Fluorine
Ключове слово: 
Solid-state NMR spectroscopy
Impact Factor: 
3,154
A monofluoro-substituted amino acid was designed to serve as a conformationally restricted label for solid-state 19F NMR distance measurements in membrane-bound peptides. The aromatic cis and trans isomers of 1-amino-3-(4-fluorophenyl)cyclobutanecarboxylic acid were synthesized in five steps from diethyl 2-(4-fluorophenyl)propanedioate. They were incorporated into the antimicrobial peptide gramicidin S to replace a native DPhenylalanine residue. Because the Cα-tetrasubstituted amino acid cannot racemize, it showed full compatibility with solid-phase peptide synthesis protocols. According to circular dichroism analysis and molecular modeling, the 19F-labeled analogues of the known helix-inducing amino acid (1-aminocyclobutane-1-carboxylic acid) do not disrupt the peptide conformation when substituted for Phe, neither in a β-turn nor in an α-helix.
Назва підрозділу: 
Кафедра супрамолекулярної хімії та біохімії
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Дизайн: Інститут високих технологій
Ivan Ivanov