Decarboxylative diversification of amino acids and peptides through metallaphotocatalytic editing of acidic residues.

Authors

Zhong-Wei Zhang, Zhe Feng, Jing Nie, Chi Wai Cheung, Jun-An Ma

Published in

Proceedings of the National Academy of Sciences of the United States of America. Volume 123. Issue 26. Pages e2600258123. Jun 30, 2026. Epub Jun 22, 2026.

Abstract

Lysine with a characteristic amino group on its side chain is one of the most abundant amino acids in protein structures, making libraries of lysine-based noncanonical amino acids (ncAAs) a valuable resource for expanding the functional and structural diversity of amino acids and peptides, unlocking new opportunities in peptide design and chemical modification. In this study, we report the development of a metallaphotocatalytic decarboxylation strategy that can smoothly transform aspartic acid, glutamic acid, homoglutamic acid, and higher homologs into various N-aryl lysines and analogs, a highly versatile yet underexploited class of functionalized ncAAs. The resulting ncAAs feature a wide array of aromatic and heteroaromatic substituents, as well as structurally tunable aliphatic side chains. Furthermore, this strategy can also be applied to the construction of arylamine-modified peptides, providing modular access to functionalized amino acid and peptide building blocks.

PMID:
42330272
Bibliographic data and abstract were imported from PubMed on 23 Jun 2026.

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