Chemoselective Peptide Modification via Photocatalytic Tryptophan β‑Position Conjugation

Targeting tryptophan is a promising strategy to achieve high levels of selectivity for peptide or protein modification. A chemoselective peptide modification method via photocatalytic tryptophan β-position conjugation has been discovered. This transformation has good substrate scope for both peptide...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2018-06, Vol.140 (22), p.6797-6800
Main Authors: Yu, Younong, Zhang, Li-Kang, Buevich, Alexei V, Li, Guoqing, Tang, Haiqun, Vachal, Petr, Colletti, Steven L, Shi, Zhi-Cai
Format: Article
Language:English
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Summary:Targeting tryptophan is a promising strategy to achieve high levels of selectivity for peptide or protein modification. A chemoselective peptide modification method via photocatalytic tryptophan β-position conjugation has been discovered. This transformation has good substrate scope for both peptide and Michael acceptor, and has good chemoselectivity versus other amino acid residues. The endogenous peptides, glucagon and GLP-1 amide, were both successfully conjugated at the tryptophan β-position. Insulin was studied as a nontryptophan control molecule, resulting in exclusive B-chain C-terminal-selective decarboxylative conjugation. This transformation provides a novel approach toward peptide modification to support the discovery of new therapeutic peptides, protein labeling and bioconjugation.
ISSN:0002-7863
1520-5126
DOI:10.1021/jacs.8b03973