(1-((tert-butoxycarbonyl)amino)-3-phenylpropyl)(5-methoxy-2-(methoxycarbonyl)-5-oxopentyl)phosphinic acid | 1446694-15-0

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: (1-((tert-butoxycarbonyl)amino)-3-phenylpropyl)(5-methoxy-2-(methoxycarbonyl)-5-oxopentyl)phosphinic acid
• CAS: 1446694-15-0
• 化学式: C₂₂H₃₄NO₈P
• 分子量: 471.488
• InChiKey: PRTHBNIKUMONTE-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.48
• 重原子数：
  32.0
• 可旋转键数：
  11.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.59
• 拓扑面积：
  128.23
• 氢给体数：
  2.0
• 氢受体数：
  7.0

反应信息

• 作为反应物：
  描述：

  (1-((tert-butoxycarbonyl)amino)-3-phenylpropyl)(5-methoxy-2-(methoxycarbonyl)-5-oxopentyl)phosphinic acid 在 sodium periodate 、 ruthenium(III) trichloride hydrate 、 三甲基硅烷化重氮甲烷 作用下， 以 乙醚 、 水 、 乙酸乙酯 、 甲苯 为溶剂， 反应 4.34h， 生成 Dimethyl 2-[[methoxy-[4-methoxy-1-[(2-methylpropan-2-yl)oxycarbonylamino]-4-oxobutyl]phosphoryl]methyl]pentanedioate
  参考文献：
  名称：

  Phosphinic acid-based inhibitors of tubulin polyglutamylases

  摘要：

  Tubulin is subject to a reversible post-translational modification involving polyglutamylation and deglutamylation of glutamate residues in its C-terminal tail. This process plays key roles in regulating the function of microtubule associated proteins, neuronal development, and metastatic progression. This study describes the synthesis and testing of three phosphinic acid-based inhibitors that have been designed to inhibit both the glutamylating and deglutamylating enzymes. The compounds were tested against the polyglutamylase TTLL7 using tail peptides as substrates (100 mu M) and the most potent inhibitor displayed an IC50 value of 150 mu M. The incorporation of these compounds into tubulin C-terminal tail peptides may lead to more potent TTLL inhibitors. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2013.05.069
• 作为产物：
  描述：

  2-亚甲基戊二酸二甲酯 、 反应 3.0h， 生成 (1-((tert-butoxycarbonyl)amino)-3-phenylpropyl)(5-methoxy-2-(methoxycarbonyl)-5-oxopentyl)phosphinic acid
  参考文献：
  名称：

  Phosphinic acid-based inhibitors of tubulin polyglutamylases

  摘要：

  Tubulin is subject to a reversible post-translational modification involving polyglutamylation and deglutamylation of glutamate residues in its C-terminal tail. This process plays key roles in regulating the function of microtubule associated proteins, neuronal development, and metastatic progression. This study describes the synthesis and testing of three phosphinic acid-based inhibitors that have been designed to inhibit both the glutamylating and deglutamylating enzymes. The compounds were tested against the polyglutamylase TTLL7 using tail peptides as substrates (100 mu M) and the most potent inhibitor displayed an IC50 value of 150 mu M. The incorporation of these compounds into tubulin C-terminal tail peptides may lead to more potent TTLL inhibitors. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2013.05.069