ArticleAngewandte Chemie (International ed. in English)2016
DNA-Catalyzed Introduction of Azide at Tyrosine for Peptide Modification.
Article in Angewandte Chemie (International ed. in English), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 18 citations in OpenAlex.
- Linker-Engineered Tyrosine-Azide Coatings for Stable Strain-Promoted Azide-Alkyne Cycloaddition (SPAAC) Functionalization.Polymers · 2025Article
- Sequence-Dependent Acylation of Peptide Lysine Residues by DNAzymes.Chembiochem : a European journal of chemical biology · 2024Article
- DNAmoreDB, a database of DNAzymes.Nucleic acids research · 2021Article
- DNAzymes for amine and peptide lysine acylation.Organic & biomolecular chemistry · 2021Article
- Monoclonal Anti-AMP Antibodies Are Sensitive and Valuable Tools for Detecting Patterns of AMPylation.iScience · 2020Article
- Tyrosine bioconjugation - an emergent alternative.Organic & biomolecular chemistry · 2020Review
- DNA-Catalyzed Introduction of Azide at Tyrosine for Peptide Modification.Angewandte Chemie (International ed. in English) · 2016Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
We show that DNA enzymes (deoxyribozymes) can introduce azide functional groups at tyrosine residues in peptide substrates. Using in vitro selection, we identified deoxyribozymes that transfer the 2'-azido-2'-deoxyadenosine 5'-monophosphoryl group (2'-Az-dAMP) from the analogous 5'-triphosphate (2'-Az-dATP) onto the tyrosine hydroxyl group of a peptide, which is either tethered to a DNA anchor or free. Some of the new deoxyribozymes are general with regard to the amino acid residues surrounding the tyrosine, while other DNA enzymes are sequence-selective. We use one of the new deoxyribozymes to modify free peptide substrates by attaching PEG moieties and fluorescent labels.
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Registered trials
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