Expanding the chemical space of peptides <i>via</i> biocompatible tryptophan C7-arylation.

ABSTRACT: Late-stage functionalization of peptides and amino acids is a powerful strategy for modulating biological activity and enabling targeted molecular imaging, offering a promising route for expanding the chemical space of peptides. Here, we report a Rh-catalyzed, P(iii)-directed C7-selective arylation of tryptophan residues using a removable N-P ^t Bu₂ auxiliary. This method exhibits broad substrate scope, excellent regioselectivity, and high functional group tolerance, enabling efficient and modular derivatization of tryptophan-containing amino acids and peptides. The resulting C7-arylated Trp derivatives serve as fluorogenic probes with environment-sensitive, turn-on fluorescence suitable for wash-free imaging of bacterial cells. Moreover, incorporation of

SUBMITTER: Liu L 

PROVIDER: S-EPMC12817912 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature