N-methyl-N-(1-methylpiperidin-4-yl)-3-(3-(trifluoromethyl)phenyl)-[1,2,4]triazolo[4,3-b]pyridazin-6-amine | 1166855-02-2

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 唑类
• 英文名称: N-methyl-N-(1-methylpiperidin-4-yl)-3-(3-(trifluoromethyl)phenyl)-[1,2,4]triazolo[4,3-b]pyridazin-6-amine
• 英文别名: N-methyl-N-(1-methylpiperidin-4-yl)-3-[3-(trifluoromethyl)phenyl]-[1,2,4]triazolo[4,3-b]pyridazin-6-amine
• CAS: 1166855-02-2
• 化学式: C₁₉H₂₁F₃N₆
• 分子量: 390.411
• InChiKey: FLOQWWLPIRCNAE-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.3
• 重原子数：
  28
• 可旋转键数：
  3
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.42
• 拓扑面积：
  49.6
• 氢给体数：
  0
• 氢受体数：
  8

反应信息

• 作为产物：
  描述：

  1-甲基-4-(甲氨基)哌啶 、 6-chloro-3-(3-trifluoromethylphenyl)-1,2,4-triazolo<4,3-b>pyridazine 反应 4.0h， 生成 N-methyl-N-(1-methylpiperidin-4-yl)-3-(3-(trifluoromethyl)phenyl)-[1,2,4]triazolo[4,3-b]pyridazin-6-amine
  参考文献：
  名称：

  Structure-based design of 3-aryl-6-amino-triazolo[4,3-b]pyridazine inhibitors of Pim-1 kinase

  摘要：

  A series of substituted 3-aryl-6-amino-triazolo[4,3-b]pyridazines were identified as highly selective inhibitors of Pim-1 kinase. Initial exploration identified compound 24 as a potent, selective inhibitor, limited in its utility by poor solubility and permeability. Understanding the unusual ATP-binding site of the Pim kinases and X-ray crystallographic data on compound 24 led to design improvements in this class of inhibitor. This resulted in compound 29, a selective, soluble and permeable inhibitor of Pim-1. (C) 2009 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2009.04.061

文献信息

• Structure-based design of 3-aryl-6-amino-triazolo[4,3-b]pyridazine inhibitors of Pim-1 kinase
  作者：Ron Grey、Albert C. Pierce、Guy W. Bemis、Marc D. Jacobs、Cameron Stuver Moody、Rahul Jajoo、Narinder Mohal、Jeremy Green

  DOI：10.1016/j.bmcl.2009.04.061

  日期：2009.6

  A series of substituted 3-aryl-6-amino-triazolo[4,3-b]pyridazines were identified as highly selective inhibitors of Pim-1 kinase. Initial exploration identified compound 24 as a potent, selective inhibitor, limited in its utility by poor solubility and permeability. Understanding the unusual ATP-binding site of the Pim kinases and X-ray crystallographic data on compound 24 led to design improvements in this class of inhibitor. This resulted in compound 29, a selective, soluble and permeable inhibitor of Pim-1. (C) 2009 Elsevier Ltd. All rights reserved.