2-isobutoxy-4-nitrobenzoic acid | 766552-33-4

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: 2-isobutoxy-4-nitrobenzoic acid
• 英文别名: 2-Isobutoxy-4-nitro-benzoesaeure；2-(2-Methylpropoxy)-4-nitrobenzoic acid
• CAS: 766552-33-4
• 化学式: C₁₁H₁₃NO₅
• 分子量: 239.228
• InChiKey: NURJMVKPGGNXMH-UHFFFAOYSA-N

物化性质

• 熔点：
  158.6-159.6 °C
• 沸点：
  404.3±30.0 °C(Predicted)
• 密度：
  1.274±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.5
• 重原子数：
  17
• 可旋转键数：
  4
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.36
• 拓扑面积：
  92.4
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  2-isobutoxy-4-nitrobenzoic acid 在 草酰氯 、 N,N-二甲基苯胺 、 N,N-二甲基甲酰胺 作用下， 以 四氢呋喃 、 丙酮 为溶剂， 反应 2.0h， 生成 3-isobutoxy-4-(2-isobutoxy-4-nitrobenzamido)benzoic acid
  参考文献：
  名称：

  Perturbation of the c-Myc–Max Protein–Protein Interaction via Synthetic α-Helix Mimetics

  摘要：

  The rational design of inhibitors of the bHLH-ZIP oncoprotein c-Myc is hampered by a lack of structure in its monomeric state. We describe herein the design of novel, low-molecular-weight, synthetic a-helix mimetics that recognize helical c-Myc in its transcriptionally active coiled-coil structure in association with its obligate bHLH-ZIP partner Max. These compounds perturb the heterodimers binding to its canonical E-box DNA sequence without causing protein-protein dissociation, heralding a new mechanistic class of direct c-Myc inhibitors. In addition to electrophoretic mobility shift assays, this model was corroborated by further biophysical methods, including NMR spectroscopy and surface plasmon resonance. Several compounds demonstrated a 2-fold or greater selectivity for c-Myc-Max heterodimers over Max-Max homodimers with IC50 values as low as 5.6 mu M. Finally, these compounds inhibited the proliferation of c-Myc-expressing cell lines in a concentration-dependent manner that correlated with the loss of expression of a c-Myc-dependent reporter plasmid despite the fact that c-MycMax heterodimers remained intact.

  DOI：

  10.1021/jm501440q
• 作为产物：
  描述：

  2-羟基-4-硝基苯甲酸甲酯 在 potassium carbonate 、 sodium hydroxide 作用下， 以 四氢呋喃 、 甲醇 、 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 17.25h， 生成 2-isobutoxy-4-nitrobenzoic acid
  参考文献：
  名称：

  Perturbation of the c-Myc–Max Protein–Protein Interaction via Synthetic α-Helix Mimetics

  摘要：

  The rational design of inhibitors of the bHLH-ZIP oncoprotein c-Myc is hampered by a lack of structure in its monomeric state. We describe herein the design of novel, low-molecular-weight, synthetic a-helix mimetics that recognize helical c-Myc in its transcriptionally active coiled-coil structure in association with its obligate bHLH-ZIP partner Max. These compounds perturb the heterodimers binding to its canonical E-box DNA sequence without causing protein-protein dissociation, heralding a new mechanistic class of direct c-Myc inhibitors. In addition to electrophoretic mobility shift assays, this model was corroborated by further biophysical methods, including NMR spectroscopy and surface plasmon resonance. Several compounds demonstrated a 2-fold or greater selectivity for c-Myc-Max heterodimers over Max-Max homodimers with IC50 values as low as 5.6 mu M. Finally, these compounds inhibited the proliferation of c-Myc-expressing cell lines in a concentration-dependent manner that correlated with the loss of expression of a c-Myc-dependent reporter plasmid despite the fact that c-MycMax heterodimers remained intact.

  DOI：

  10.1021/jm501440q

文献信息

• Derivatives of 4-Amino-2-hydroxybenzoic Acid. II
  作者：R. O. Clinton、U. J. Salvador、S. C. Laskowski、Mary Wilson

  DOI：10.1021/ja01123a005

  日期：1952.2
• Derivatives of 4-Amino-2-hydroxybenzoic Acid. V. Basic Ethers
  作者：R. O. Clinton、S. C. Laskowski、U. J. Salvador、Patricia M. Carroll

  DOI：10.1021/ja01566a073

  日期：1957.5
• Perturbation of the c-Myc–Max Protein–Protein Interaction via Synthetic α-Helix Mimetics
  作者：Kwan-Young Jung、Huabo Wang、Peter Teriete、Jeremy L. Yap、Lijia Chen、Maryanna E. Lanning、Angela Hu、Lester J. Lambert、Toril Holien、Anders Sundan、Nicholas D. P. Cosford、Edward V. Prochownik、Steven Fletcher

  DOI：10.1021/jm501440q

  日期：2015.4.9

  The rational design of inhibitors of the bHLH-ZIP oncoprotein c-Myc is hampered by a lack of structure in its monomeric state. We describe herein the design of novel, low-molecular-weight, synthetic a-helix mimetics that recognize helical c-Myc in its transcriptionally active coiled-coil structure in association with its obligate bHLH-ZIP partner Max. These compounds perturb the heterodimers binding to its canonical E-box DNA sequence without causing protein-protein dissociation, heralding a new mechanistic class of direct c-Myc inhibitors. In addition to electrophoretic mobility shift assays, this model was corroborated by further biophysical methods, including NMR spectroscopy and surface plasmon resonance. Several compounds demonstrated a 2-fold or greater selectivity for c-Myc-Max heterodimers over Max-Max homodimers with IC50 values as low as 5.6 mu M. Finally, these compounds inhibited the proliferation of c-Myc-expressing cell lines in a concentration-dependent manner that correlated with the loss of expression of a c-Myc-dependent reporter plasmid despite the fact that c-MycMax heterodimers remained intact.