[3-benzyloxy-4-(2-hydroxy-1,1-dimethylethyl)benzyl]carbamic acid tert-butyl ester | 871309-06-7

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯酚醚
• 英文名称: [3-benzyloxy-4-(2-hydroxy-1,1-dimethylethyl)benzyl]carbamic acid tert-butyl ester
• CAS: 871309-06-7
• 化学式: C₂₃H₃₁NO₄
• 分子量: 385.503
• InChiKey: NVZIQAAZAPDSJV-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.56
• 重原子数：
  28.0
• 可旋转键数：
  7.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.43
• 拓扑面积：
  67.79
• 氢给体数：
  2.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  [3-benzyloxy-4-(2-hydroxy-1,1-dimethylethyl)benzyl]carbamic acid tert-butyl ester 在 盐酸 、 三氟二甲基硫醚络合物 、 1-羟基苯并三唑 、 2-乙氧基-1-乙氧碳酰基-1,2-二氢喹啉 作用下， 以 1,4-二氧六环 、 乙醚 、 二氯甲烷 为溶剂， 反应 0.5h， 生成 N-(3-hydroxy-4-(1-hydroxy-2-methylpropan-2-yl)benzyl)-4-phenoxybenzamide
  参考文献：
  名称：

  Two classes of p38α MAP kinase inhibitors having a common diphenylether core but exhibiting divergent binding modes

  摘要：

  Two new classes of diphenylether inhibitors of p38alpha MAP kinase are described. Both chemical classes are based on a common diphenylether core that is identified by simulated fragment annealing as one of the most favored chemotypes within a prominent hydrophobic pocket of the p38alpha ATP-binding site. In the fully elaborated molecules, the diphenylether moiety acts as an anchor occupying the deep pocket, while polar extensions make specific interactions with either the adenine binding site or the phosphate binding site of ATP. The synthesis, crystallographic analysis, and biological activity of these p38alpha inhibitors are discussed.

  DOI：

  10.1016/j.bmcl.2005.08.038
• 作为产物：
  描述：

  [3-benzyloxy-4-(1,1-dimethyl-2-triisopropylsilanyloxyethyl)phenyl]acetic acid ethyl ester 在 lithium hydroxide 、 叠氮磷酸二苯酯 、 四丁基氟化铵 、 三乙胺 作用下， 以 四氢呋喃 、 二氯甲烷 、 甲苯 为溶剂， 反应 18.5h， 生成 [3-benzyloxy-4-(2-hydroxy-1,1-dimethylethyl)benzyl]carbamic acid tert-butyl ester
  参考文献：
  名称：

  Two classes of p38α MAP kinase inhibitors having a common diphenylether core but exhibiting divergent binding modes

  摘要：

  Two new classes of diphenylether inhibitors of p38alpha MAP kinase are described. Both chemical classes are based on a common diphenylether core that is identified by simulated fragment annealing as one of the most favored chemotypes within a prominent hydrophobic pocket of the p38alpha ATP-binding site. In the fully elaborated molecules, the diphenylether moiety acts as an anchor occupying the deep pocket, while polar extensions make specific interactions with either the adenine binding site or the phosphate binding site of ATP. The synthesis, crystallographic analysis, and biological activity of these p38alpha inhibitors are discussed.

  DOI：

  10.1016/j.bmcl.2005.08.038