4-(4-methoxybenzylamino)thieno[3,2-c]pyridine-2,7-dicarbonitrile | 1529795-93-4

• 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: 4-(4-methoxybenzylamino)thieno[3,2-c]pyridine-2,7-dicarbonitrile
• 英文别名: 4-[(4-Methoxyphenyl)methylamino]thieno[3,2-c]pyridine-2,7-dicarbonitrile；4-[(4-methoxyphenyl)methylamino]thieno[3,2-c]pyridine-2,7-dicarbonitrile
• CAS: 1529795-93-4
• 化学式: C₁₇H₁₂N₄OS
• 分子量: 320.374
• InChiKey: XIGQXWXQIMXSTF-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.66
• 重原子数：
  23.0
• 可旋转键数：
  4.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.12
• 拓扑面积：
  81.73
• 氢给体数：
  1.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  4-(4-methoxybenzylamino)thieno[3,2-c]pyridine-2,7-dicarbonitrile 在 硫酸 、 钯 作用下， 反应 2.0h， 以69%的产率得到4-aminothieno[3,2-c]pyridine-2,7-dicarboxamide sulfate
  参考文献：
  名称：

  Identification through structure-based methods of a bacterial NAD+-dependent DNA ligase inhibitor that avoids known resistance mutations

  摘要：

  In an attempt to identify novel inhibitors of NAD(+)-dependent DNA ligase (LigA) that are not affected by a known resistance mutation in the adenosine binding pocket, a detailed analysis of the binding sites of a variety of bacterial ligases was performed. This analysis revealed several similarities to the adenine binding region of kinases, which enabled a virtual screen of known kinase inhibitors. From this screen, a thienopyridine scaffold was identified that was shown to inhibit bacterial ligase. Further characterization through structure and enzymology revealed the compound was not affected by a previously disclosed resistance mutation in Streptococcus pneumoniae LigA, Leu75Phe. A subsequent medicinal chemistry program identified substitutions that resulted in an inhibitor with moderate activity across various Gram-positive bacterial LigA enzymes. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2013.11.007
• 作为产物：
  描述：

  4-甲氧基苄胺 在 potassium carbonate 作用下， 以 N-甲基吡咯烷酮 、 N,N-二甲基甲酰胺 为溶剂， 反应 16.5h， 生成 4-(4-methoxybenzylamino)thieno[3,2-c]pyridine-2,7-dicarbonitrile
  参考文献：
  名称：

  Identification through structure-based methods of a bacterial NAD+-dependent DNA ligase inhibitor that avoids known resistance mutations

  摘要：

  In an attempt to identify novel inhibitors of NAD(+)-dependent DNA ligase (LigA) that are not affected by a known resistance mutation in the adenosine binding pocket, a detailed analysis of the binding sites of a variety of bacterial ligases was performed. This analysis revealed several similarities to the adenine binding region of kinases, which enabled a virtual screen of known kinase inhibitors. From this screen, a thienopyridine scaffold was identified that was shown to inhibit bacterial ligase. Further characterization through structure and enzymology revealed the compound was not affected by a previously disclosed resistance mutation in Streptococcus pneumoniae LigA, Leu75Phe. A subsequent medicinal chemistry program identified substitutions that resulted in an inhibitor with moderate activity across various Gram-positive bacterial LigA enzymes. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2013.11.007