Chemoselective Copper-Mediated Modification of Selenocysteines in Peptides and Proteins

Zhenguang Zhao, Daphna Shimon, Norman Metanis*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


Highly valuable bioconjugated molecules must be synthesized through efficient, chemoselective chemical modifications of peptides and proteins. Herein, we report the chemoselective modification of peptides and proteins via a reaction between selenocysteine residues and aryl/alkyl radicals. In situ radical generation from hydrazine substrates and copper ions proceeds rapidly in an aqueous buffer at near neutral pH (5-8), providing a variety of Se-modified linear and cyclic peptides and proteins conjugated to aryl and alkyl molecules, and to affinity label tag (biotin). This chemistry opens a new avenue for chemical protein modifications.

Original languageAmerican English
Pages (from-to)12817-12824
Number of pages8
JournalJournal of the American Chemical Society
Issue number32
StatePublished - 18 Aug 2021

Bibliographical note

Publisher Copyright:
© 2021 American Chemical Society.


Dive into the research topics of 'Chemoselective Copper-Mediated Modification of Selenocysteines in Peptides and Proteins'. Together they form a unique fingerprint.

Cite this