(p-Methoxy-phenyl)-glutarat | 37526-01-5

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯酚酯
• 英文名称: (p-Methoxy-phenyl)-glutarat
• 英文别名: 5-(4-methoxyphenoxy)-5-oxopentanoic acid
• CAS: 37526-01-5
• 化学式: C₁₂H₁₄O₅
• 分子量: 238.24
• InChiKey: AZRXJSPZJPFLDP-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.86
• 重原子数：
  17.0
• 可旋转键数：
  6.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.33
• 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：

  (p-Methoxy-phenyl)-glutarat 、 反-4-羟基-β-硝基苯乙烯 在 N,N'-二环己基碳二亚胺 作用下， 以 四氢呋喃 为溶剂， 以0.377 g的产率得到Pentanedioic acid 4-methoxy-phenyl ester 4-((E)-2-nitro-vinyl)-phenyl ester
  参考文献：
  名称：

  Inhibition of the her2 tyrosine kinase and characterization of a hydrophobic site near the nucleotide binding domain

  摘要：

  A series of compounds was prepared to investigate the hydrophobic character of the HER2 receptor tyrosine kinase active site. These bisubstrate analogs contained hydrophobic moieties in place of the polar triphosphate and nucleoside fragments of the natural ATP ligand. Despite these modifications, good affinity was observed as measured by inhibition of receptor autophosphorylation. (C) 1997 Elsevier Science Ltd.

  DOI：

  10.1016/s0960-894x(97)00369-7
• 作为产物：
  描述：

  戊二酸酐 、 4-甲氧基苯酚 在 N,N-二异丙基乙胺 作用下， 以 1,4-二氧六环 为溶剂， 反应 1.25h， 以94%的产率得到(p-Methoxy-phenyl)-glutarat
  参考文献：
  名称：

  Inhibition of the her2 tyrosine kinase and characterization of a hydrophobic site near the nucleotide binding domain

  摘要：

  A series of compounds was prepared to investigate the hydrophobic character of the HER2 receptor tyrosine kinase active site. These bisubstrate analogs contained hydrophobic moieties in place of the polar triphosphate and nucleoside fragments of the natural ATP ligand. Despite these modifications, good affinity was observed as measured by inhibition of receptor autophosphorylation. (C) 1997 Elsevier Science Ltd.

  DOI：

  10.1016/s0960-894x(97)00369-7

文献信息

• Inhibition of the her2 tyrosine kinase and characterization of a hydrophobic site near the nucleotide binding domain
  作者：Joseph A. Maddry、Conrad Kussner、Jackie W. Truss、Shri Niwas、E. Lucile White、Cecil D. Kwong

  DOI：10.1016/s0960-894x(97)00369-7

  日期：1997.8

  A series of compounds was prepared to investigate the hydrophobic character of the HER2 receptor tyrosine kinase active site. These bisubstrate analogs contained hydrophobic moieties in place of the polar triphosphate and nucleoside fragments of the natural ATP ligand. Despite these modifications, good affinity was observed as measured by inhibition of receptor autophosphorylation. (C) 1997 Elsevier Science Ltd.