2-bromo-4-[(2-hydroxyethyl)amino]thieno[3,2-c]pyridine-7-carboxamide | 1529796-35-7

• 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: 2-bromo-4-[(2-hydroxyethyl)amino]thieno[3,2-c]pyridine-7-carboxamide
• 英文别名: 2-Bromo-4-(2-hydroxyethylamino)thieno[3,2-c]pyridine-7-carboxamide；2-bromo-4-(2-hydroxyethylamino)thieno[3,2-c]pyridine-7-carboxamide
• CAS: 1529796-35-7
• 化学式: C₁₀H₁₀BrN₃O₂S
• 分子量: 316.178
• InChiKey: NURIRNPCILKLBH-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.4
• 重原子数：
  17
• 可旋转键数：
  4
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.2
• 拓扑面积：
  117
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  2-溴-4-氯噻吩并[3,2-c]吡啶-7-甲腈 在 硫酸 作用下， 反应 2.0h， 生成 2-bromo-4-[(2-hydroxyethyl)amino]thieno[3,2-c]pyridine-7-carboxamide
  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.