Position-Selective Modification of Cyclic Peptides by Histidine-Directed β-C(sp3)-H Arylation of Alanine.

Authors

Sunday A Akintelu, Bo Yao

Published in

Organic letters. Volume 28. Issue 44. Pages 13654-13658. Nov 06, 2026.

Abstract

Herein we report a histidine-directed β-C(sp3)-H arylation method for the site-selective modification of alanine residues in cyclic peptides. Cyclic penta- to decapeptides with various cyclization patterns delivered Ala C-H arylated products in moderate-to-good yields and high positional selectivity. Both canonical α-amino acids and noncanonical β-, γ-, δ-, and ε-amino acids are compatible. Its synthetic utility was demonstrated via peptide bioconjugation with fluorophore, short peptide, and oleanolic acid.

PMID:
42992763
Bibliographic data and abstract were imported from PubMed on 06 Nov 2026.

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