Methods for modifying intact peptides are useful but can be unselective with regard to amino acid position and sequence context. In this work, we used in vitro selection to identify DNAzymes that acylate a Lys residue of a short peptide in sequence‐dependent fashion. The DNAzymes do not acylate Lys when placed at other residues in the peptide, and the acylation activity depends on the Lys sequence context. A high acylation yield is observed on the preparative nanomole scale. These findings are promising for further development of DNAzymes for broader application to top‐down Lys acylation of peptide and protein substrates.
Sequence‐Dependent Acylation of Peptide Lysine Residues by DNAzymes
Prakriti K Das,Scott K Silverman
Published 2024 in ChemBioChem
ABSTRACT
PUBLICATION RECORD
- Publication year
2024
- Venue
ChemBioChem
- Publication date
2024-09-06
- Fields of study
Biology, Medicine, Chemistry
- Identifiers
- External record
- Source metadata
Semantic Scholar, PubMed
CITATION MAP
EXTRACTION MAP
CLAIMS
- No claims are published for this paper.
CONCEPTS
- No concepts are published for this paper.
REFERENCES
Showing 1-79 of 79 references · Page 1 of 1
CITED BY
Showing 1-1 of 1 citing papers · Page 1 of 1