3',5'-O-(1,1,3,3-tetraisopropyldisiloxane-1,3-diyl)-2'-deoxy-2'-(triphenylmethylthio)adenosine | 1174402-97-1

• 分子结构分类: 有机化合物 - 苯类化合物 - 三苯基化合物
• 英文名称: 3',5'-O-(1,1,3,3-tetraisopropyldisiloxane-1,3-diyl)-2'-deoxy-2'-(triphenylmethylthio)adenosine
• CAS: 1174402-97-1
• 化学式: C₄₁H₅₃N₅O₄SSi₂
• 分子量: 768.14
• InChiKey: ZIIRXUHBXJDNEX-KPASRLDTSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  9.36
• 重原子数：
  53.0
• 可旋转键数：
  10.0
• 环数：
  7.0
• sp3杂化的碳原子比例：
  0.44
• 拓扑面积：
  106.54
• 氢给体数：
  1.0
• 氢受体数：
  10.0

反应信息

• 作为反应物：
  描述：

  3',5'-O-(1,1,3,3-tetraisopropyldisiloxane-1,3-diyl)-2'-deoxy-2'-(triphenylmethylthio)adenosine 在 四丁基氟化铵 作用下， 以 四氢呋喃 为溶剂， 反应 3.0h， 以90%的产率得到2'-deoxy-2'-triphenylmethylthioadenosine
  参考文献：
  名称：

  Synthesis and Evaluation of an RNA Editing Substrate Bearing 2′-Deoxy-2′-Mercaptoadenosine

  摘要：

  The RNA-editing adenosine deaminases (ADARs) catalyze deamination of adenosine to inosine in double stranded structure found in various RNA substrates, including mRNAs. Here we describe the synthesis of a phosphoramidite of 2 '-deoxy-2 '-mercaptoadenosine and its incorporation into an ADAR substrate. Surprisingly, no deamination product was observed with this substrate indicating replacing the 2 '-OH with a 2 '-SH at the editing site is highly inhibitory. Modeling of nucleotide binding into the active site suggests the side chain of T375 of human ADAR2 to be in proximity of the 2 '-substituent. Mutation of this residue to cysteine caused a greater that 100-fold reduction in deamination rate with the 2 '-OH substrate.

  DOI：

  10.1080/15257770902736459
• 作为产物：
  描述：

  三苯甲硫醇 、 2'-O-triflyl-3',5'-O-(tetraisopropyldisiloxane-1,3-diyl)-ara-adenosine 在 sodium hydride 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 以1.87 g的产率得到3',5'-O-(1,1,3,3-tetraisopropyldisiloxane-1,3-diyl)-2'-deoxy-2'-(triphenylmethylthio)adenosine
  参考文献：
  名称：

  Synthesis and Evaluation of an RNA Editing Substrate Bearing 2′-Deoxy-2′-Mercaptoadenosine

  摘要：

  The RNA-editing adenosine deaminases (ADARs) catalyze deamination of adenosine to inosine in double stranded structure found in various RNA substrates, including mRNAs. Here we describe the synthesis of a phosphoramidite of 2 '-deoxy-2 '-mercaptoadenosine and its incorporation into an ADAR substrate. Surprisingly, no deamination product was observed with this substrate indicating replacing the 2 '-OH with a 2 '-SH at the editing site is highly inhibitory. Modeling of nucleotide binding into the active site suggests the side chain of T375 of human ADAR2 to be in proximity of the 2 '-substituent. Mutation of this residue to cysteine caused a greater that 100-fold reduction in deamination rate with the 2 '-OH substrate.

  DOI：

  10.1080/15257770902736459