Cordycepin Analogs of 2–5 a as Activators of RNase L: Study of the Structural Requirements for RNase L Activation

Abstract

Enzymatically and chemically synthesized cordycepin analogs of 2–5A^† trimer and tetramer were found to be biologically active as protein synthesis inhibitors in intact cultured human fibroblast and murine L929 cells ^1,2. In rabbit reticulocyte lysates, the cordycepin tetramer analog of 2–5A inhibits protein synthesis through binding to and activation of RNase L³. Our present results using L929 cell extracts provide direct evidence that the cordycepin analogs of 2–5A can bind to and activate RNase L.