1-deaza-5'-O-(4.4’-dimethoxytrityl)-N⁶-(N,N-dimethylaminomethylene)-2’-deoxyadenosine | 1414781-82-0

• 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: 1-deaza-5'-O-(4.4’-dimethoxytrityl)-N⁶-(N,N-dimethylaminomethylene)-2’-deoxyadenosine
• CAS: 1414781-82-0
• 化学式: C₃₅H₃₇N₅O₅
• 分子量: 607.709
• InChiKey: WCDMAOABCFASOD-DCMFLLSESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.33
• 重原子数：
  45.0
• 可旋转键数：
  11.0
• 环数：
  6.0
• sp3杂化的碳原子比例：
  0.29
• 拓扑面积：
  103.46
• 氢给体数：
  1.0
• 氢受体数：
  9.0

反应信息

• 作为反应物：
  描述：

  1-deaza-5'-O-(4.4’-dimethoxytrityl)-N⁶-(N,N-dimethylaminomethylene)-2’-deoxyadenosine 、 2-氰乙基N,N-二异丙基氯亚磷酰胺 在 N,N-二异丙基乙胺 作用下， 以 四氢呋喃 为溶剂， 反应 12.0h， 以63%的产率得到1-deaza-5’-O-(4.4’-dimethoxytrityl)-N⁶-(N,N-dimethylaminomethylene)-2’-deoxyadenosine-3’-O-[(2-cyanoethyl)-N,N-diisopropylphosphoramidite]
  参考文献：
  名称：

  Gas-Phase Studies of Substrates for the DNA Mismatch Repair Enzyme MutY

  摘要：

  The gas-phase thermochernical properties (tautomeric energies, acidity, and proton affinity) have been measured and calculated for adenine and six adenine analogues that were designed to test features of the catalytic mechanism used by the adenine glycosylase MutY. The gas-phase intrinsic properties are correlated to possible excision mechanisms and MutY excision rates to gain insight into the MutY mechanism. The data support a mechanism involving protonation at N7 and hydrogen bonding to N3 of adenine. We also explored the acid-catalyzed (non-enzymatic) depurination of these substrates, which appears to follow a different mechanism than that employed by MutY,) 3 which we elucidate using calculations.

  DOI：

  10.1021/ja309082k
• 作为产物：
  描述：

  7-amino-3-(2'-deoxy-β-D-ribofuranosyl)imidazo[4,5-b]pyridine 在 吡啶 作用下， 以 四氢呋喃 、 甲醇 为溶剂， 反应 28.05h， 生成 1-deaza-5'-O-(4.4’-dimethoxytrityl)-N⁶-(N,N-dimethylaminomethylene)-2’-deoxyadenosine
  参考文献：
  名称：

  Gas-Phase Studies of Substrates for the DNA Mismatch Repair Enzyme MutY

  摘要：

  The gas-phase thermochernical properties (tautomeric energies, acidity, and proton affinity) have been measured and calculated for adenine and six adenine analogues that were designed to test features of the catalytic mechanism used by the adenine glycosylase MutY. The gas-phase intrinsic properties are correlated to possible excision mechanisms and MutY excision rates to gain insight into the MutY mechanism. The data support a mechanism involving protonation at N7 and hydrogen bonding to N3 of adenine. We also explored the acid-catalyzed (non-enzymatic) depurination of these substrates, which appears to follow a different mechanism than that employed by MutY,) 3 which we elucidate using calculations.

  DOI：

  10.1021/ja309082k