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Inside Cover: Irreversible Cysteine‐Selective Protein Labeling Employing Modular Electrophilic Tetrafluoroethylation Reagents (Chem. Eur. J. 27/2017)
Author(s) -
Václavík Jiří,
Zschoche Reinhard,
Klimánková Iveta,
Matoušek Václav,
Beier Petr,
Hilvert Donald,
Togni Antonio
Publication year - 2017
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201701036
Subject(s) - reagent , chemistry , maleimide , cysteine , electrophile , iodoacetamide , nucleophile , biomolecule , hypervalent molecule , combinatorial chemistry , derivatization , bioorthogonal chemistry , enzyme , organic chemistry , biochemistry , chromatography , click chemistry , mass spectrometry , catalysis
Selective and irreversible labeling of a cysteine present in artificial retro‐aldolase is achieved by employing modular tetrafluoroalkylation reagents based on hypervalent iodine. Unlike commonly used maleimide or iodoacetamide reagents, the fluoroalkyl‐transfer λ 3 ‐iodanes leave the enzyme's active center, a nucleophilic lysine, intact. Many different functional moieties or dyes can be fused to the reagents in one step, making the method an attractive and robust approach for the derivatization of biomolecules. More information can be found in the Communication by P. Beier, D. Hilvert, A. Togni, et al. on page 6490 ff.