(S)-2-{(4E,8E)-2-[2-(Diethoxy-phosphoryl)-ethyl]-5,9,13-trimethyl-tetradeca-4,8,12-trienoylamino}-3-phenyl-propionic acid | 848487-21-8

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: (S)-2-{(4E,8E)-2-[2-(Diethoxy-phosphoryl)-ethyl]-5,9,13-trimethyl-tetradeca-4,8,12-trienoylamino}-3-phenyl-propionic acid
• CAS: 848487-21-8
• 化学式: C₃₂H₅₀NO₆P
• 分子量: 575.726
• InChiKey: ZXTYEEGQSOWKSW-ZQBXBZJXSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  7.88
• 重原子数：
  40.0
• 可旋转键数：
  20.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.56
• 拓扑面积：
  101.93
• 氢给体数：
  2.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  (S)-2-{(4E,8E)-2-[2-(Diethoxy-phosphoryl)-ethyl]-5,9,13-trimethyl-tetradeca-4,8,12-trienoylamino}-3-phenyl-propionic acid 在 2,3,5-三甲基吡啶 、 三甲基溴硅烷 作用下， 以 二氯甲烷 为溶剂， 以45%的产率得到(S)-3-Phenyl-2-[(4E,8E)-5,9,13-trimethyl-2-(2-phosphono-ethyl)-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：

  4-(二乙基膦)丁酸 在 lithium hydroxide 、 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 、 lithium diisopropyl amide 作用下， 以 四氢呋喃 、 水 为溶剂， 生成 (S)-2-{(4E,8E)-2-[2-(Diethoxy-phosphoryl)-ethyl]-5,9,13-trimethyl-tetradeca-4,8,12-trienoylamino}-3-phenyl-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