Versatile Enzymatic Approach for Truncation, Labeling, and Mutation of Nucleobase-Modified Aptamers Demonstrated on Indole-Modified β-Conglutin Aptamer.

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 sequenc

SUBMITTER: Ondrus M 

PROVIDER: S-EPMC12582157 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature