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Sequence-Dependent Acylation of Peptide Lysine Residues by DNAzymes.
- Source :
-
Chembiochem : a European journal of chemical biology [Chembiochem] 2024 Nov 04; Vol. 25 (21), pp. e202400578. Date of Electronic Publication: 2024 Oct 27. - Publication Year :
- 2024
-
Abstract
- 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.<br /> (© 2024 The Author(s). ChemBioChem published by Wiley-VCH GmbH.)
Details
- Language :
- English
- ISSN :
- 1439-7633
- Volume :
- 25
- Issue :
- 21
- Database :
- MEDLINE
- Journal :
- Chembiochem : a European journal of chemical biology
- Publication Type :
- Academic Journal
- Accession number :
- 39239825
- Full Text :
- https://doi.org/10.1002/cbic.202400578