This method demonstrates effective conversion of dehydroalanine to aspartic acid in peptides, suggesting a novel utility of photoredox chemistry.
A photoredox approach is described for converting dehydroalanine (Dha) residues in peptides to aspartic acid (Asp). Using ammonium formate as a CO2•– radical source under mild conditions, Dha is functionalized in a traceless manner.The protocol is compatible with peptide substrates, including fully unprotected, the complex antimicrobial peptide nisin. Notably, employing 13C-labeled formate affords 13C-Asp, facilitating direct isotopic labeling of the modified peptides.
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Han et al. (2025) studied this question.
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