Peptide-Compatible Photoredox-Catalyzed Mutagenesis of Dehydroalanine to Aspartic Acid
A photoredox approach is described for converting dehydroalanine (Dha) residues in peptides to aspartic acid (Asp). Using ammonium formate as a CO<sub>2</sub><sup>•-</sup> 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 <sup>13</sup>C-labeled formate affords <sup>13</sup>C-Asp, facilitating direct isotopic labeling of the modified peptides.
Authors
- Tianyun Guo
- Penggang Zhao
- Xiaolei Wang (ORCID: https://orcid.org/0000-0002-8867-6528)
- Hong Wang (ORCID: https://orcid.org/0009-0001-1895-326X)
- Jian Liu (ORCID: https://orcid.org/0000-0002-6879-0614)
- Na Wang (ORCID: https://orcid.org/0000-0001-9179-4130)
- Jun Han
Institutions
- State Key Laboratory of Chemical Engineering (CN)
- Lanzhou University (CN)
Publication Details
- Journal
- Organic Letters
- Published
- 2025-08-25
- DOI
- https://doi.org/10.1021/acs.orglett.5c03204
- Citations
- 1
- Primary Topic
- Chemical Synthesis and Analysis
- Type
- article
- Field-Weighted Citation Impact
- 0.81
Funders
- National Natural Science Foundation of China
- Science and Technology Program of Gansu Province