Site-selective and inducible acylation of thrombin using aptamer-catalyst conjugates

Two acyl-transfer catalysts were conjugated to thrombin-binding DNA aptamers to acylate thrombin. Modification occurred site-selectively on Lys (>Ser) residues proximal to the respective aptamer-thrombin interface, was selective for thrombin in the presence of other proteins, and the activity of...

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Bibliographic Details
Published inChemical communications (Cambridge, England) Vol. 57; no. 96; pp. 1296 - 12963
Main Authors Keijzer, Jordi F, Firet, Judith, Albada, Bauke
Format Journal Article
LanguageEnglish
Published England Royal Society of Chemistry 03.12.2021
Subjects
Acylation
Aptamers, Nucleotide - chemistry
Catalysis
Catalysts
Models, Molecular
Molecular Structure
Thrombin
Thrombin - chemical synthesis
Thrombin - chemistry
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Summary:Two acyl-transfer catalysts were conjugated to thrombin-binding DNA aptamers to acylate thrombin. Modification occurred site-selectively on Lys (>Ser) residues proximal to the respective aptamer-thrombin interface, was selective for thrombin in the presence of other proteins, and the activity of both DNA-catalysts could be controlled by an external trigger. Functionalizing a protein-binding aptamer with an acylation catalyst leads to site-selective modification of the target protein in proximity to the aptamer-protein interface. This protein modification can be switched ON or OFF by an external trigger.
Bibliography:10.1039/d1cc05446e
Electronic supplementary information (ESI) available: Synthesis and characterization of compounds, synthesis of DNA constructs, details of the protein modification studies. See DOI
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1359-7345
1364-548X
DOI:10.1039/d1cc05446e