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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]

PMID: 29301396

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