ArticleChemical science2020
Site-selective aqueous C-H acylation of tyrosine-containing oligopeptides with aldehydes.
Article in Chemical science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Recent developments in the cleavage, functionalization, and conjugation of proteins and peptides at tyrosine residues.Chemical science · 2023Review
- Site-Selective C-H Amination of Phenol-Containing Biomolecules.Organic letters · 2023Article
- The thiol-sulfoxonium ylide photo-click reaction for bioconjugation.Chemical science · 2023Article
- Ruthenaelectro-catalyzed C-H acyloxylation for late-stage tyrosine and oligopeptide diversification.Chemical science · 2022Article
- Late-Stage C-H Acylation of Tyrosine-Containing Oligopeptides with Alcohols.Organic letters · 2021Article
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Authors and funding
2 authors.
Funding
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Abstract
The development of useful synthetic tools to label amino acids within a peptide framework for the ultimate modification of proteins in a late-stage fashion is a challenging task of utmost importance within chemical biology. Herein, we report the first Pd-catalyzed C-H acylation of a collection of Tyr-containing peptides with aldehydes. This water-compatible tagging technique is distinguished by its site-specificity, scalability and full tolerance of sensitive functional groups. Remarkably, it provides straightforward access to a high number of oligopeptides with altered side-chain topology including mimetics of endomorphin-2 and neuromedin N, thus illustrating its promising perspectives toward the diversification of structurally complex peptides and chemical ligation.
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