4-amino-2-N-ethylthieno[3,2-c]pyridine-2,7-dicarboxamide | 1529795-99-0

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 噻吩并吡啶类
• 英文名称: 4-amino-2-N-ethylthieno[3,2-c]pyridine-2,7-dicarboxamide
• 英文别名: 4-amino-N2-ethylthieno[3,2-c]pyridine-2,7-dicarboxamide
• CAS: 1529795-99-0
• 化学式: C₁₁H₁₂N₄O₂S
• 分子量: 264.308
• InChiKey: JGOCMINENPDGCP-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.73
• 重原子数：
  18.0
• 可旋转键数：
  3.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.18
• 拓扑面积：
  111.1
• 氢给体数：
  3.0
• 氢受体数：
  5.0

反应信息

• 作为产物：
  描述：

  ethyl 7-cyano-4-(4-methoxybenzylamino)thieno[3,2-c]pyridine-2-carboxylate 在 钯 、 N,N-二异丙基乙胺 、 Methanaminium,N-[(dimethylamino)(3H-1,2,3-triazolo[4,5-b]pyridin-3-yloxy)methylene]-N-methyl-, hexafluorophosphate(1-) 、 三氟乙酸 、 sodium hydroxide 作用下， 以 四氢呋喃 、 N,N-二甲基甲酰胺 为溶剂， 反应 30.0h， 生成 4-amino-2-N-ethylthieno[3,2-c]pyridine-2,7-dicarboxamide
  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

文献信息

• Identification through structure-based methods of a bacterial NAD+-dependent DNA ligase inhibitor that avoids known resistance mutations
  作者：Kerry Murphy-Benenato、Hongming Wang、Helen M. McGuire、Hajnalka E. Davis、Ning Gao、D. Bryan Prince、Haris Jahic、Suzanne S. Stokes、P. Ann Boriack-Sjodin

  DOI：10.1016/j.bmcl.2013.11.007

  日期：2014.1

  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.