Dimethyl 2-[[methoxy-[4-methoxy-1-[(2-methylpropan-2-yl)oxycarbonylamino]-4-oxobutyl]phosphoryl]methyl]pentanedioate | 1446694-07-0

• 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: Dimethyl 2-[[methoxy-[4-methoxy-1-[(2-methylpropan-2-yl)oxycarbonylamino]-4-oxobutyl]phosphoryl]methyl]pentanedioate
• 英文别名: dimethyl 2-[[methoxy-[4-methoxy-1-[(2-methylpropan-2-yl)oxycarbonylamino]-4-oxobutyl]phosphoryl]methyl]pentanedioate
• CAS: 1446694-07-0
• 化学式: C₁₉H₃₄NO₁₀P
• 分子量: 467.453
• InChiKey: GDXAZNIVPQRLSI-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.5
• 重原子数：
  31
• 可旋转键数：
  17
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.79
• 拓扑面积：
  144
• 氢给体数：
  1
• 氢受体数：
  10

反应信息

• 作为反应物：
  描述：

  Dimethyl 2-[[methoxy-[4-methoxy-1-[(2-methylpropan-2-yl)oxycarbonylamino]-4-oxobutyl]phosphoryl]methyl]pentanedioate 在 三氟乙酸 作用下， 以 二氯甲烷 、 水 为溶剂， 反应 3.0h， 生成 dimethyl 2-(((1-amino-4-methoxy-4-oxobutyl)(methoxy)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：

  (1-(N-(tert-butyloxycarbonyl)amino)-3-phenylpropyl) 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 8.34h， 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

文献信息

• Phosphinic acid-based inhibitors of tubulin polyglutamylases
  作者：Yanjie Liu、Christopher P. Garnham、Antonina Roll-Mecak、Martin E. Tanner

  DOI：10.1016/j.bmcl.2013.05.069

  日期：2013.8

  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.