ArticleAngewandte Chemie (International ed. in English)2022
The Protein-Templated Synthesis of Enzyme-Generated Aptamers.
Article in Angewandte Chemie (International ed. in English), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 7 citations in OpenAlex.
- Template-independent enzymatic functionalization of DNA oligonucleotides with environment-sensitive nucleotide probes using terminal deoxynucleotidyl transferase.Nucleic acids research · 2025Article
- Design, Expression, and Purification of a Fusion Enzyme Containing Terminal Deoxynucleotidyl Transferase fromProtein and peptide letters · 2025Article
- A toolbox for enzymatic modification of nucleic acids with photosensitizers for photodynamic therapy.RSC chemical biology · 2024Article
- The Protein-Templated Synthesis of Enzyme-Generated Aptamers.Angewandte Chemie (International ed. in English) · 2022Article
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7 authors at 2 institutions in 3 countries.
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Abstract
Inspired by the chemical synthesis of molecularly imprinted polymers, we demonstrated for the first time, the protein-target mediated synthesis of enzyme-generated aptamers (EGAs). We prepared pre-polymerisation mixtures containing different ratios of nucleotides, an initiator sequence and protein template and incubated each mixture with terminal deoxynucleotidyl transferase (TdT). Upon purification and rebinding of the EGAs against the target, we observed an enhancement in binding of templated-EGAs towards the target compared to a non-templated control. These results demonstrate the presence of two primary mechanisms for the formation of EGAs, namely, the binding of random sequences to the target as observed in systematic evolution of ligands by exponential enrichment (SELEX) and the dynamic competition between TdT enzyme and the target protein for binding of EGAs during synthesis. The latter mechanism serves to increase the stringency of EGA-based screening and represents a new way to develop aptamers that relies on rational design.
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