2-Methyladenosine-substituted 2′,5′-oligoadenylates: conformations, 2-5A binding and catalytic activities with human ribonuclease L

✍ Scribed by Yukio Kitade; Masaharu Wakana; Takayuki Tsuboi; Chizuko Yatome; Suzanne F Bayly; Mark R Player; Paul F Torrence

• Book ID: 104364985
• Publisher: Elsevier Science
• Year: 2000
• Tongue: English
• Weight: 119 KB
• Volume: 10
• Category: Article
• ISSN: 0960-894X
• DOI: 10.1016/s0960-894x(99)00703-9

✦ Synopsis

me 2 A), p5 H (me 2 A)2 H p5 H A2 H p5 H A, and p5 H (me 2 A) 2 H p5 H (me 2 A)2 H p5 H (me 2 A), were prepared via a modi®cation of a lead ion-catalyzed ligation reaction. These 5 H -monophosphates were subsequently converted into the corresponding 5 H -triphosphates. Both binding and activation of human recombinant RNase L by various 2-methyladenosine-substituted 2-5A analogues were examined. Among the 2-5A analogues, p5 H A2 H p5 H A2 H p5 H (me 2 A) showed the strongest binding anity and was as eective as 2-5A itself as an activator of RNase L. The CD spectra of both p5 H (me 2 A)2 H p5 H A2 H p5 H A and p5 H A2 H p5 H A2 H p5 H (me 2 A) were superimposable on that of p5 H A2 H p5 H A2 H p5 H A, indicative of an anti orientation about the base-glycoside bonds as in naturally occurring 2-5A.