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Palladium-Mediated Arylation of Lysine in Unprotected Peptides.

ABSTRACT: A mild method for the arylation of lysine in an unprotected peptide is presented. In the presence of a preformed biarylphosphine-supported palladium(II)-aryl complex and a weak base, lysine amino groups underwent C-N bond formation at room temperature. The process generally exhibited high selectivity for lysine over other amino acids containing nucleophilic side chains and was applicable to the conjugation of a variety of organic compounds, including complex drug molecules, with an array of peptides. Finally, this method was also successfully applied to the formation of cyclic peptides by macrocyclization.

SUBMITTER: Lee HG

PROVIDER: S-EPMC5741856 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature

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Palladium-Mediated Arylation of Lysine in Unprotected Peptides.

Lee Hong Geun HG Lautrette Guillaume G Pentelute Bradley L BL Buchwald Stephen L SL

Angewandte Chemie (International ed. in English) 20170216 12

A mild method for the arylation of lysine in an unprotected peptide is presented. In the presence of a preformed biarylphosphine-supported palladium(II)-aryl complex and a weak base, lysine amino groups underwent C-N bond formation at room temperature. The process generally exhibited high selectivity for lysine over other amino acids containing nucleophilic side chains and was applicable to the conjugation of a variety of organic compounds, including complex drug molecules, with an array of pept ...[more]

PMID: 28206688

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