[1-(4-methylbenzyl)-1H-5-imidazolyl]methyl acetate | 854714-87-7

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: [1-(4-methylbenzyl)-1H-5-imidazolyl]methyl acetate
• 英文别名: [3-[(4-Methylphenyl)methyl]imidazol-4-yl]methyl acetate
• CAS: 854714-87-7
• 化学式: C₁₄H₁₆N₂O₂
• 分子量: 244.293
• InChiKey: OYJLORWSEVMAKX-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.7
• 重原子数：
  18
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.29
• 拓扑面积：
  44.1
• 氢给体数：
  0
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  [1-(4-methylbenzyl)-1H-5-imidazolyl]methyl acetate 在 manganese(IV) oxide 、 sodium hydroxide 、 3 A molecular sieve 、 三乙胺 作用下， 以 1,4-二氧六环 、 甲醇 为溶剂， 反应 25.0h， 生成 methyl (2S)-2-[benzoyl-[1-[[3-[(4-methylphenyl)methyl]imidazol-4-yl]methyl]piperidin-4-yl]amino]-4-methylsulfanylbutanoate
  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-甲基苄溴 、 4-(乙酰氧基甲基)-1-(三苯基甲基)咪唑 在 三氟乙酸 作用下， 以 乙酸乙酯 为溶剂， 反应 25.0h， 以38%的产率得到[1-(4-methylbenzyl)-1H-5-imidazolyl]methyl acetate
  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