ArticleBiochemistry2011
DNA-catalyzed covalent modification of amino acid side chains in tethered and free peptide substrates.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 39 citations in OpenAlex.
- Solution NMR Spectroscopy as a Tool to Study DNAzyme Structure and Function.Methods in molecular biology (Clifton, N.J.) · 2022Article
- DNAmoreDB, a database of DNAzymes.Nucleic acids research · 2021Article
- Tyrosine bioconjugation - an emergent alternative.Organic & biomolecular chemistry · 2020Review
- Molecular Features and Metal Ions That Influence 10-23 DNAzyme Activity.Molecules (Basel, Switzerland) · 2020Review
- Catalytic Nucleic Acids: Biochemistry, Chemical Biology, Biosensors, and Nanotechnology.iScience · 2020Review
- Supramolecular biofunctional materials.Biomaterials · 2017Review
- Biochemical and Biophysical Understanding of Metal Ion Selectivity of DNAzymes.Inorganica chimica acta · 2016Article
- Catalytic DNA: Scope, Applications, and Biochemistry of Deoxyribozymes.Trends in biochemical sciences · 2016Review
- Assessing histidine tags for recruiting deoxyribozymes to catalyze peptide and protein modification reactions.Organic & biomolecular chemistry · 2016Article
- Pursuing DNA catalysts for protein modification.Accounts of chemical research · 2015Article
- A generalizable DNA-catalyzed approach to peptide-nucleic acid conjugation.Chembiochem : a European journal of chemical biology · 2014Article
- DNA-catalyzed lysine side chain modification.Angewandte Chemie (International ed. in English) · 2014Article
- Supramolecular hydrogels made of basic biological building blocks.Chemistry, an Asian journal · 2014Review
- DNA catalysts with tyrosine kinase activity.Journal of the American Chemical Society · 2013Article
- Enhanced deoxyribozyme-catalyzed RNA ligation in the presence of organic cosolvents.Biopolymers · 2013Article
- Catalytic DNA with phosphatase activity.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Systematic evaluation of the dependence of deoxyribozyme catalysis on random region length.ACS combinatorial science · 2012Article
- Covalent tagging of phosphorylated peptides by phosphate-specific deoxyribozymes.Chembiochem : a European journal of chemical biology · 2012Article
- DNA-catalyzed reactivity of a phosphoramidate functional group and formation of an unusual pyrophosphoramidate linkage.Organic & biomolecular chemistry · 2012Article
- DNA-catalyzed reductive amination.Angewandte Chemie (International ed. in English) · 2011Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
This study focuses on the development of DNA catalysts (deoxyribozymes) that modify side chains of peptide substrates, with the long-term goal of achieving DNA-catalyzed covalent protein modification. We recently described several deoxyribozymes that modify tyrosine (Tyr) or serine (Ser) side chains by catalyzing their reaction with 5'-triphosphorylated RNA, forming nucleopeptide linkages. In each previous case, the side chain was presented in a highly preorganized three-dimensional architecture such that the resulting deoxyribozymes inherently cannot function with free peptides or proteins, which do not maintain the preorganization. Here we describe in vitro selection of deoxyribozymes that catalyze Tyr side chain modification of tethered and free peptide substrates, where the approach can potentially be generalized for catalysis involving large proteins. Several new deoxyribozymes for Tyr modification (and several for Ser modification as well) were identified; progressively better catalytic activity was observed as the selection design was strategically changed. The best new deoxyribozyme, 15MZ36, catalyzes covalent Tyr modification of a free tripeptide substrate with a k(obs) of 0.50 h(-1) (t(1/2) of 83 min) and up to 65% yield. These findings represent an important advance by demonstrating, for the first time, DNA catalysis involving free peptide substrates. The new results suggest the feasibility of DNA-catalyzed covalent modification of side chains of large protein substrates and provide key insights into how to achieve this goal.
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