N-{5-[(6,7-dimethoxyquinolin-4-yl)oxy]-pyridin-2-yl}piperazine-1-carboxamide | 1042431-76-4

• 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: N-{5-[(6,7-dimethoxyquinolin-4-yl)oxy]-pyridin-2-yl}piperazine-1-carboxamide
• 英文别名: N-[5-(6,7-dimethoxyquinolin-4-yl)oxypyridin-2-yl]piperazine-1-carboxamide
• CAS: 1042431-76-4
• 化学式: C₂₁H₂₃N₅O₄
• 分子量: 409.445
• InChiKey: VRXHQWAJCSWOBJ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.5
• 重原子数：
  30
• 可旋转键数：
  5
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.29
• 拓扑面积：
  97.8
• 氢给体数：
  2
• 氢受体数：
  7

反应信息

• 作为产物：
  描述：

  4-({5-[(6,7-dimethoxyquinolin-4-yl)oxy]pyridin-2-yl}carbamoyl)piperazine-1-carboxylic acid tert-butyl ester 在 盐酸 作用下， 以 1,4-二氧六环 为溶剂， 反应 12.0h， 以17%的产率得到N-{5-[(6,7-dimethoxyquinolin-4-yl)oxy]-pyridin-2-yl}piperazine-1-carboxamide
  参考文献：
  名称：

  Structure activity relationships of quinoline-containing c-Met inhibitors

  摘要：

  A series of quinoline-containing c-Met inhibitors were prepared and studied. Chemistry was developed to introduce a pyridyl moiety onto the 2-aryl ring present in a lead molecule which mitigated the potential for quinone formation relative to the original compound. The study also assessed the importance of an acylthiourea moiety present in the lead structure for effective binding to the c-Met protein ATP site. (c) 2007 Elsevier Masson SAS. All rights reserved.

  DOI：

  10.1016/j.ejmech.2007.08.011

文献信息

• Structure activity relationships of quinoline-containing c-Met inhibitors
  作者：Pei-Pei Kung、Lee Funk、Jerry Meng、Gordon Alton、Ellen Padrique、Barbara Mroczkowski

  DOI：10.1016/j.ejmech.2007.08.011

  日期：2008.6

  A series of quinoline-containing c-Met inhibitors were prepared and studied. Chemistry was developed to introduce a pyridyl moiety onto the 2-aryl ring present in a lead molecule which mitigated the potential for quinone formation relative to the original compound. The study also assessed the importance of an acylthiourea moiety present in the lead structure for effective binding to the c-Met protein ATP site. (c) 2007 Elsevier Masson SAS. All rights reserved.