Postsynthetic modifications of peptides have proven to be important tools in a wide array of applications. Current peptide N-arylation requires high temperature and is limited to single amino acids. A new method for direct arylation at the unprotected N-terminus of peptides has been studied in the Ball Lab. The reaction uses an ortho-substituted aryl boronic acid as the coupling partner for peptide α-amine mediated by copper acetate in aqueous buffer. Herein the optimization of this arylation method through pH, buffer, and co-solvent screening in addition to copper(II) and boronic acid concentration screens is described. Ortho-substituted aryl boronic acids and various peptide sequences were also screened to determine the boronic acid scope and peptide tolerance of this reaction. Reaction yields determined through HPLC analysis show modification with aryl boronic acids bearing ortho-electron withdrawing groups and a high tolerability to peptide sequeces.

Copper(II) mediated <i>N</i>-arylation of the peptide N-terminus

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

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Copper(II) mediated N-arylation of the peptide N-terminus