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Reductant‐Induced Free Radical Fluoroalkylation of Nitrogen Heterocycles and Innate Aromatic Amino Acid Residues in Peptides and Proteins
Author(s) -
Rahimidashaghoul Kheironnesae,
Klimánková Iveta,
Hubálek Martin,
Korecký Michal,
Chvojka Matúš,
Pokorný Daniel,
Matoušek Václav,
Fojtík Lukáš,
Kavan Daniel,
Kukačka Zdeněk,
Novák Petr,
Beier Petr
Publication year - 2019
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201902944
Subject(s) - chemistry , tryptophan , amino acid , aromatic amino acids , hydrochloride , carbonic anhydrase , organic chemistry , aqueous solution , combinatorial chemistry , hydrolysis , cysteine , enzyme , biochemistry
A series of fluoroalkylated cyclic λ 3 ‐iodanes and their hydrochloride salts was prepared and used in a combination with sodium ascorbate in buffer or aqueous methanol mixtures for radical fluoroalkylation of a range of substituted indoles, pyrroles, tryptophan or its derivatives, and Trp residues in peptides. As demonstrated on several peptides, the aromatic amino acid residues of Trp, Tyr, Phe, and His are targeted with high selectivity to Trp. The functionalization method is biocompatible, mild, rapid, and transition‐metal‐free. The proteins myoglobin, ubiquitin, and human carbonic anhydrase I were also successfully functionalized.