ArticleChembiochem : a European journal of chemical biology2025
Versatile Enzymatic Approach for Truncation, Labeling, and Mutation of Nucleobase-Modified Aptamers Demonstrated on Indole-Modified β-Conglutin Aptamer.
Article in Chembiochem : a European journal of chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Expedient single-round selection of hyper-modified aptamer targeting insulin receptor from over-represented dually nucleobase-modified DNA libraries.Nature communications · 2026Article
- Article
- Versatile Enzymatic Approach for Truncation, Labeling, and Mutation of Nucleobase-Modified Aptamers Demonstrated on Indole-Modified β-Conglutin Aptamer.Chembiochem : a European journal of chemical biology · 2025Article
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7 authors.
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Abstract
A new enzymatic method for truncation of aptamers from 5'-end has been developed and demonstrated on a newly selected indole-modified β-conglutin aptamer. This method relies on extension of a primer containing ribonucleotides, which can be specifically hydrolyzed by RNase, thereby removing the whole or 5'-part of the primer. This approach enables flexible synthesis of modified aptamers truncated from the 5' end, 3' end, or both ends-a capability previously achievable only through chemical oligonucleotide synthesis. Furthermore, by employing doubly labeled primers, diverse labeled or modified nucleotides are introduced to prepare 5'-labeled aptamers suitable for fluorescence- or immobilization-based assays. The different variations of this method also enable the synthesis of mutated sequences to study the effect of modifications and their positions. Overall, this enzymatic method provides a valuable alternative for the truncation or labeling of (hyper)modified and functional oligonucleotides avoiding the need for chemical synthesis.
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