(4E,8E)-2-(Diethoxy-phosphorylmethyl)-5,9,13-trimethyl-tetradeca-4,8,12-trienoic acid | 180088-17-9

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 异戊烯醇脂质
• 英文名称: (4E,8E)-2-(Diethoxy-phosphorylmethyl)-5,9,13-trimethyl-tetradeca-4,8,12-trienoic acid
• CAS: 180088-17-9
• 化学式: C₂₂H₃₉O₅P
• 分子量: 414.522
• InChiKey: UZACYWVWPNMKIB-YLYRKCBPSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  6.76
• 重原子数：
  28.0
• 可旋转键数：
  15.0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.68
• 拓扑面积：
  72.83
• 氢给体数：
  1.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  (4E,8E)-2-(Diethoxy-phosphorylmethyl)-5,9,13-trimethyl-tetradeca-4,8,12-trienoic acid 在 2,3,5-三甲基吡啶 、 lithium hydroxide 、 三甲基溴硅烷 、 1-(3-二甲基氨基丙基)-3-乙基碳二亚胺 、 3-羟基-1,2,3-苯并三嗪-4(3H)-酮 作用下， 以 四氢呋喃 、 二氯甲烷 、 水 为溶剂， 生成 (S)-3-Phenyl-2-((4E,8E)-5,9,13-trimethyl-2-phosphonomethyl-tetradeca-4,8,12-trienoylamino)-propionic acid
  参考文献：
  名称：

  Inhibition of farnesyl protein transferase by new farnesyl phosphonate derivatives of phenylalanine

  摘要：

  New farnesyl phosphonate derivatives of phenylalanine have been prepared as inhibitors of farnesyl-protein transferase (FPT). Enzyme inhibition studies with bovine brain FPT and rat liver squalene synthase show that compound <(3a)under bar> is a new, potent and selective FPT inhibitor. Moreover, structural modifications from <(3a)under bar> have provided some useful information concerning the key structural subunits necessary for optimum and selective FPT inhibition. Copyright (C) 1996 Elsevier Science Ltd

  DOI：

  10.1016/0960-894x(96)00238-7
• 作为产物：
  描述：

  反,反-法呢基溴 、 3-(二乙基膦)丙酸 在 lithium diisopropyl amide 作用下， 生成 (4E,8E)-2-(Diethoxy-phosphorylmethyl)-5,9,13-trimethyl-tetradeca-4,8,12-trienoic acid
  参考文献：
  名称：

  Inhibition of farnesyl protein transferase by new farnesyl phosphonate derivatives of phenylalanine

  摘要：

  New farnesyl phosphonate derivatives of phenylalanine have been prepared as inhibitors of farnesyl-protein transferase (FPT). Enzyme inhibition studies with bovine brain FPT and rat liver squalene synthase show that compound <(3a)under bar> is a new, potent and selective FPT inhibitor. Moreover, structural modifications from <(3a)under bar> have provided some useful information concerning the key structural subunits necessary for optimum and selective FPT inhibition. Copyright (C) 1996 Elsevier Science Ltd

  DOI：

  10.1016/0960-894x(96)00238-7