Interaction between 2',5'-A Core Analogues and 2',5'-Specific Phosphodiesterase.

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Abstract
Analogues of (2'',5''-)triadenylate (2'',5''-A core) were synthesized and their stabilities against 2''-phosphodiesterase (2''PDi) purified from Ehrlich ascites cells were determined. Replacement of the ribose group with an arabinose in different positions of the trimer resulted in dramatic changes in the rate of hydrolysis by 2''PDi. Analogues with an arabinose at the 2'' terminal or in the middle position or both were stable against 2''PDi. These stable analogues did not inhibit the degradation of 2'',5''-A core by 2''PDi indicating that they did not have the same affinity for the enzyme. Modifications at the 3'' hydroxyls also resulted in structures resistent to degradation by 2''PDi. Replacement of the 6-aminopurine moiety of adenosine by 2-aminopurine resulted in only small changes in stability against 2''PDi. These results show that the configuration of the sugar at 2'' and 3'' carbons are important for the recognition by 2''-phosphodiesterase.

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