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Selective Radical Trifluoromethylation of Native Residues in Proteins.


ABSTRACT: The incorporation of fluorine can not only significantly facilitate the study of proteins but also potentially modulate their function. Though some biosynthetic methods allow global residue-replacement, post-translational fluorine incorporation would constitute a fast and efficient alternative. Here, we reveal a mild method for direct protein radical trifluoromethylation at native residues as a strategy for symmetric-multifluorine incorporation on mg scales with high recoveries. High selectivity toward tryptophan residues enhanced the utility of this direct trifluoromethylation technique allowing ready study of fluorinated protein constructs using 19F-NMR.

SUBMITTER: Imiolek M 

PROVIDER: S-EPMC5806083 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature

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Selective Radical Trifluoromethylation of Native Residues in Proteins.

Imiołek Mateusz M   Karunanithy Gogulan G   Ng Wai-Lung WL   Baldwin Andrew J AJ   Gouverneur Véronique V   Davis Benjamin G BG  

Journal of the American Chemical Society 20180122 5


The incorporation of fluorine can not only significantly facilitate the study of proteins but also potentially modulate their function. Though some biosynthetic methods allow global residue-replacement, post-translational fluorine incorporation would constitute a fast and efficient alternative. Here, we reveal a mild method for direct protein radical trifluoromethylation at native residues as a strategy for symmetric-multifluorine incorporation on mg scales with high recoveries. High selectivity  ...[more]

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