| 1057750-79-4

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - 嘌呤核苷
• CAS: 1057750-79-4
• 化学式: C₁₀H₁₅FN₅O₁₂P₃S
• 分子量: 541.241
• InChiKey: DQSRKMYJJHTLDX-AESZWTTRSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.37
• 重原子数：
  32.0
• 可旋转键数：
  8.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  262.06
• 氢给体数：
  7.0
• 氢受体数：
  14.0

反应信息

• 作为产物：
  描述：

  2-氟腺苷 在 三氯硫磷 、 三辛胺 、 磷酸三乙酯 、 三丁基焦磷酸铵 作用下， 反应 2.0h， 生成
  参考文献：
  名称：

  Fluorine Substituted Adenosines As Probes of Nucleobase Protonation in Functional RNAs

  摘要：

  Ionized nucleobases are required for folding, conformational switching, or catalysis in a number of functional RNAs. A common strategy to study these sites employs nucleoside analogues with perturbed pK(a), but the interpretation of these studies is often complicated by the chemical modification introduced, in particular modifications that add, remove, or translocate hydrogen bonding groups in addition to perturbing pKa values. In the present study we present a series of fluorine substituted adenosine analogues that produce large changes in N1 pK(a) values with minimal structural perturbation. These analogues include fluorine for hydrogen substitutions in the adenine ring of adenosine and 7-deaza-adenosine with resulting N1 pK(a) values spanning more than 4 pKa units. To demonstrate the utility of these analogues we have conducted a nucleotide analogue interference mapping (NAIM) study on a self-ligating construct of the Varkud Satellite (VS) ribozyme. We find that each of the analogues is readily incorporated by T7 RNA polymerase and produces fully active transcripts when substituted at the majority of sites. Strong interferences are observed for three sites known to be critical for VS ribozyme function, most notably A756. Substitutions at A756 lead to slight enhancements in activity for elevated pK(a) analogues and dramatic interferences in activity for reduced pK(a) analogues, supporting the proposed catalytic role for this base. The structural similarity of these analogues, combined with their even incorporation and selective interference, provides an improved method for identifying sites of adenosine protonation in a variety of systems.

  DOI：

  10.1021/ja803336y