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Sequence-Dependent Acylation of Peptide Lysine Residues by DNAzymes.

Authors :
Das PK
Silverman SK
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