2-(4-(7-methoxyquinolin-4-yl)piperazin-1-yl)-N-(pyridin-2-ylmethyl)acetamide

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 二嗪烷类
• 英文名称: 2-(4-(7-methoxyquinolin-4-yl)piperazin-1-yl)-N-(pyridin-2-ylmethyl)acetamide
• 英文别名: 2-[4-(7-methoxyquinolin-4-yl)piperazin-1-yl]-N-(pyridin-2-ylmethyl)acetamide
• 化学式: C₂₂H₂₅N₅O₂
• 分子量: 391.473
• InChiKey: AZZWEYMIHUODDZ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.9
• 重原子数：
  29
• 可旋转键数：
  6
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.32
• 拓扑面积：
  70.6
• 氢给体数：
  1
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  4-氯-7-甲氧基喹啉 在 potassium carbonate 、 1-丙基磷酸酐 、 三乙胺 、 lithium hydroxide 作用下， 以 四氢呋喃 、 甲醇 、 二氯甲烷 、 水 、 乙腈 为溶剂， 反应 7.0h， 生成 2-(4-(7-methoxyquinolin-4-yl)piperazin-1-yl)-N-(pyridin-2-ylmethyl)acetamide
  参考文献：
  名称：

  Engineering another class of anti-tubercular lead: Hit to lead optimization of an intriguing class of gyrase ATPase inhibitors

  摘要：

  A structure based medium throughput virtual screening campaign of BITS-Pilani in house chemical library to identify novel binders of Mycobacterium tuberculosis gyrase ATPase domain led to the discovery of a quinoline scaffold. Further medicinal chemistry explorations on the right hand core of the early hit, engendered a potent lead demonstrating superior efficacy both in the enzyme and whole cell screening assay. The binding affinity shown at the enzyme level was further corroborated by biophysical characterization techniques. Early pharmacokinetic evaluation of the optimized analogue was encouraging and provides interesting potential for further optimization. (C) 2016 Elsevier Masson SAS. All rights reserved.

  DOI：

  10.1016/j.ejmech.2016.06.042

文献信息

• Engineering another class of anti-tubercular lead: Hit to lead optimization of an intriguing class of gyrase ATPase inhibitors
  作者：Variam Ullas Jeankumar、Rudraraju Srilakshmi Reshma、Rahul Vats、Renuka Janupally、Shalini Saxena、Perumal Yogeeswari、Dharmarajan Sriram

  DOI：10.1016/j.ejmech.2016.06.042

  日期：2016.10

  A structure based medium throughput virtual screening campaign of BITS-Pilani in house chemical library to identify novel binders of Mycobacterium tuberculosis gyrase ATPase domain led to the discovery of a quinoline scaffold. Further medicinal chemistry explorations on the right hand core of the early hit, engendered a potent lead demonstrating superior efficacy both in the enzyme and whole cell screening assay. The binding affinity shown at the enzyme level was further corroborated by biophysical characterization techniques. Early pharmacokinetic evaluation of the optimized analogue was encouraging and provides interesting potential for further optimization. (C) 2016 Elsevier Masson SAS. All rights reserved.