Phosphorothioate Analogs of 2–5A: Elucidation of the Stereochemical Course of the Enzymes of the 2–5A Synthetase/RNase L System

Abstract

Enzymatically and chemically synthesized 2–5A phosphorothioates stereochemical altered in the 2′,5′-internucleotide linkages gave a series of metabolically stable chiral 2–5A derivatives that have been used to study the stereochemical requirements for binding to and activation of RNase L. The RpRp and SpRp, but not the RpSp or SpSp, trimer core isomers could bind to and activate RNase L