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Updated: Jun 17, 2026
Chemical Triphosphorylation of Oligonucleotides
Published on: June 2, 2022
5'-O-dephosphorylated 2',5'-oligoadenylate (2-5A) with 8-methyladenosine at the 2'-terminus activates human RNase L
Kumi Nagaoka1, Yoshiaki Kitamura, Yoshihito Ueno
1United Graduate School of Drug Discovery and Medical Information Science, Gifu University, 1-1 Yanagido, Gifu 501-1193, Japan.
Abstract:
Human ribonuclease L (RNase L), an interferon-induced endoribonuclease, becomes enzymatically active after binding to 2-5A. The 5'-phosphoryl group of 2-5A is reportedly necessary for the conformational change leading to RNase L activation. However, we found that 5'-O-dephosphorylated 2-5A tetramer analogs with 8-methyladenosine at the 2'-terminus were more effective as an activator of RNase L than the parent 2-5A tetramer. Introduction of 8-methyladenosine is thought to induce a dramatic shift of 2-5A in the binding site of RNase L.
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