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Updated: Dec 2, 2025

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
Published on: December 9, 2017
DNAzymes for amine and peptide lysine acylation
Tianjiong Yao1, Jack J Przybyla, Peter Yeh
1Department of Chemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, IL 61801, USA. sks@illinois.edu.
Researchers developed novel DNAzymes capable of acylating amines, specifically targeting lysine side chains on peptides. This breakthrough expands DNAzyme catalysis for potential sequence-selective peptide and protein modification.
Area of Science:
- Biochemistry
- Molecular Biology
- Catalysis
Background:
- DNAzymes, or catalytic DNA molecules, have been identified for various chemical reactions.
- Peptide modification, particularly lysine acylation, presents a significant challenge for DNAzyme catalysis.
Purpose of the Study:
- To identify DNAzymes capable of catalyzing peptide lysine acylation.
- To expand the catalytic capabilities of DNAzymes for acylating amine groups.
Main Methods:
- Utilized in vitro selection techniques to discover DNAzymes.
- Employed reactive aryl ester acyl donors as electrophiles for the acylation reaction.
Main Results:
- Successfully identified DNAzymes that can acylate amines, including lysine side chains on DNA-anchored peptides.
- Demonstrated that some identified DNAzymes can transfer a glutaryl group to an amino group.
Conclusions:
- The study expands the known scope of DNAzyme-catalyzed reactions.
- The findings suggest future applications of DNAzymes for sequence-selective lysine acylation in peptides and proteins.
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