[1-(4-甲氧基苄基)-1H-5-咪唑基]乙酸甲酯 | 833490-36-1

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯酚醚
• 中文名称: [1-(4-甲氧基苄基)-1H-5-咪唑基]乙酸甲酯
• 英文名称: [1-(4-methoxybenzyl)-1H-5-imidazolyl]methyl acetate
• CAS: 833490-36-1
• 化学式: C₁₄H₁₆N₂O₃
• 分子量: 260.293
• InChiKey: WKHDNISNTHIYQN-UHFFFAOYSA-N

物化性质

• 熔点：
  80-81 °C
• 沸点：
  425.8±30.0 °C(Predicted)
• 密度：
  1.15±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.0
• 重原子数：
  19.0
• 可旋转键数：
  5.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.29
• 拓扑面积：
  53.35
• 氢给体数：
  0.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  [1-(4-甲氧基苄基)-1H-5-咪唑基]乙酸甲酯 在 sodium hydroxide 作用下， 以 甲醇 为溶剂， 以84%的产率得到4-[1-(4-甲氧基苄基)-1H-咪唑-5-基]甲醇
  参考文献：
  名称：

  Potent and Selective Farnesyl Transferase Inhibitors

  摘要：

  We recently described a novel series of CA(1)A(2)X peptidomimetics as farnesyl transferase inhibitors (FTIs). These compounds possess an N-(4-piperidinyl)benzamide scaffold mimicking A(1)A(2) residue. Extensive exploration of structure-activity relationships revealed that replacement of cysteine by substituted benzylimidazoles provided nanomolar FTIs with in vitro activities (18e, IC50 = 4.60 nM on isolated enzyme, EC50 = 20.0 nM for growth inhibition on a tumor cell line). The molecular docking of 18e and 19e in the active site of the enzyme provided details of key interactions with the protein and showed that the methionine or phenylalanine residue fits into the aryl binding site.

  DOI：

  10.1021/jm030502y
• 作为产物：
  描述：

  4-甲氧基溴苄 、 4-(乙酰氧基甲基)-1-(三苯基甲基)咪唑 在 甲醇 作用下， 以 乙酸乙酯 为溶剂， 反应 42.0h， 以30%的产率得到[1-(4-甲氧基苄基)-1H-5-咪唑基]乙酸甲酯
  参考文献：
  名称：

  Potent and Selective Farnesyl Transferase Inhibitors

  摘要：

  We recently described a novel series of CA(1)A(2)X peptidomimetics as farnesyl transferase inhibitors (FTIs). These compounds possess an N-(4-piperidinyl)benzamide scaffold mimicking A(1)A(2) residue. Extensive exploration of structure-activity relationships revealed that replacement of cysteine by substituted benzylimidazoles provided nanomolar FTIs with in vitro activities (18e, IC50 = 4.60 nM on isolated enzyme, EC50 = 20.0 nM for growth inhibition on a tumor cell line). The molecular docking of 18e and 19e in the active site of the enzyme provided details of key interactions with the protein and showed that the methionine or phenylalanine residue fits into the aryl binding site.

  DOI：

  10.1021/jm030502y