ArticleJournal of the American Chemical Society2024
A Method for Rigorously Selective Capture and Simultaneous Fluorescent Labeling of N-Terminal Glycine Peptides.
Article in Journal of the American Chemical Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Design, Synthesis, and Applications of Fluorescent Amino Acids in Bioimaging.Chemical & biomedical imaging · 2026Review
- Recent advances in site-specific modifications of peptides and proteins.Chemical science · 2026Review
- Intracellular Peptide N-Myristoylation for Cancer Cell Ferroptosis without Acquired Resistance.Journal of the American Chemical Society · 2025Article
- β-alkoxy enones for biocompatible primary amine conjugation.Innovation (Cambridge (Mass.)) · 2025Article
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Authors and funding
7 authors.
Funding
Abstract
Although chemical methods for the selective derivatization of amino acid (AA) side chains in peptides and proteins are available, selective N-terminal labeling is challenging, especially for glycine, which has no side chain at the α-carbon position. We report here a double activation at glycine's α-methylene group that allows this AA to be differentiated from the other 19 AAs. A condensation reaction of dibenzoylmethane with glycine results in the formation of an imine, and subsequent tautomerization is followed by intramolecular cyclization, leading to the formation of a fluorescent pyrrole ring. Additionally, the approach exhibits compatibility with AAs possessing reactive side chains. Further, the method allows for selective pull-down assays of N-terminal glycine peptides from mixtures without prior knowledge of the N-terminal peptide distribution.
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