Conformationally Constrained Mono-Fluorinated Arginine as a Cationic Label for Solid-State 19F NMR Analysis of Membrane-Bound Peptides

被引：10

作者：

Michurin, Oleg M. ^{[1
]}

Tolmachova, Kateryna ^{[1
,2
]}

Afonin, Sergii ^{[3
]}

Babii, Oleg ^{[4
]}

Grage, Stephan L. ^{[3
]}

Ulrich, Anne S. ^{[3
,4
]}

Komarov, Igor V. ^{[5
]}

Radchenko, Dmytro S. ^{[1
,5
]}

机构：

[1] Enamine Ltd, Vul Chervonotkatska 78, UA-02094 Kiev, Ukraine

[2] Natl Acad Sci Ukraine, Inst Bioorgan Chem & Petrochem, Vul Murmanska 1, UA-02660 Kiev, Ukraine

[3] Karlsruhe Inst Technol, Inst Biol Interfaces IBG 2, POB 3640, D-76021 Karlsruhe, Germany

[4] KIT, IOC, Fritz Haber Weg 6, D-76131 Karlsruhe, Germany

[5] Taras Shevchenko Natl Univ Kyiv, Vul Volodymyrska 60, UA-01601 Kiev, Ukraine

来源：

EUROPEAN JOURNAL OF ORGANIC CHEMISTRY | 2018年 / 2018卷 / 27-28期

关键词：

Amino acids; Arginine; Fluorinated compounds; Fluorine; Peptides; NMR spectroscopy; AMINO-ACIDS; DESIGN; OPTIMIZATION; SUBSTITUTE; ANALOGS;

D O I：

10.1002/ejoc.201800473

中图分类号：

O62 [有机化学];

学科分类号：

070303 ; 081704 ;

摘要：

A conformationally constrained mono-fluorinated analogue of arginine, (1S,3S)-1-amino-3-fluoro-3-(guanidinomethyl)cyclobutane-1-carboxylic acid (F-CbArg), has been designed as a label for solid-state F-19 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 F-19 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.

引用

页码：3826 / 3833

页数：8

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