期刊
CHEMCATCHEM
卷 13, 期 21, 页码 4618-4624出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cctc.202101070
关键词
bioorganic chemistry; conjugation; DNA; G-Quadruplexes; peptides
资金
- ECHO grant from the Dutch Organization for Scientific research (NWO) [711.017.004]
The aptamer-functionalized hGQ DNAzymes enhance the bioconjugation of N-methyl luminol to tyrosine-containing residues and peptides, with a 12-fold increase in the catalytic rate constant. When applied for modifying Tyr-containing peptides, the nucleoapzymes not only recognize the ligand structure embedded in a larger peptide structure, but also show that distant residues in the peptide substrate can influence the conversion.
Hemin/G-quadruplex (hGQ) DNAzymes are horseradish peroxidase-mimicking catalysts capable of the oxidation of a variety of substrates. We now implement aptamer-functionalized hGQ DNAzymes, also known as nucleoapzymes, to achieve increased bioconjugation of N-methyl luminol to tyrosine-containing residues and peptides. We found that the presence of a tyrosinamide-binding aptamer leads to a 12-fold increase in the catalytic rate constant (k(cat)), and the saturation kinetics curves that were obtained provide evidence for the involvement of the substrate binding site in the reaction. The application of the best performing nucleoapzymes for the modification of Tyr-containing peptides reveals that (i) the aptamer also recognizes the ligand structure when this is embedded in a larger peptide structure, and (ii) distant residues in the peptide substrate can influence the conversion. As such, we show that nucleoapzymes display enzyme-like features and provide an additional tool in the toolbox of bioconjugation chemistry.
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