Triflic Acid-Mediated Chemoselective Indole C2-Heteroarylation of Peptide Tryptophan Residues by Triazine.

Abstract

Peptide modification provides opportunities to afford peptides with designed functions. Among the proteogenic amino acids, tryptophan represents an ideal and attractive target for peptide modification because of the exclusive chemical reactivity of its unique indole structure. Herein, we reported an indole C2 position-selective and transition-metal-free modification approach for indole derivatives and tryptophan-containing peptides by triazine derivatives via triflic acid activation and that the incorporated functional group could act as an orthogonal handle for further bioconjugation via an inverse electron demand Diels-Alder reaction.