(2S)-3-phenyl-2-[[(4E,8E)-5,9,13-trimethyl-2-phosphonotetradeca-4,8,12-trienoyl]amino]propanoic acid

• 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: (2S)-3-phenyl-2-[[(4E,8E)-5,9,13-trimethyl-2-phosphonotetradeca-4,8,12-trienoyl]amino]propanoic acid
• 化学式: C₂₆H₃₈NO₆P
• 分子量: 491.565
• InChiKey: SPVTYABZHGVPOA-TYDKRXPQSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5
• 重原子数：
  34
• 可旋转键数：
  14
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.46
• 拓扑面积：
  124
• 氢给体数：
  4
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  反,反-法呢基溴 在 2,3,5-三甲基吡啶 、 lithium hydroxide 、 正丁基锂 、 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 (2S)-3-phenyl-2-[[(4E,8E)-5,9,13-trimethyl-2-phosphonotetradeca-4,8,12-trienoyl]amino]propanoic 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

文献信息

• Inhibition of farnesyl protein transferase by new farnesyl phosphonate derivatives of phenylalanine
  作者：M. Lamothe、D. Perrin、D. Blotières、M. Leborgne、S. Gras、D. Bonnet、B.T. Hill、S. Halazy

  DOI：10.1016/0960-894x(96)00238-7

  日期：1996.6

  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