8-hydroxy-2-[2-(4-nitrophenyl)ethenyl]quinoline-7-carboxylic acid | 765304-45-8

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 喹啉及其衍生物
• 英文名称: 8-hydroxy-2-[2-(4-nitrophenyl)ethenyl]quinoline-7-carboxylic acid
• CAS: 765304-45-8
• 化学式: C₁₈H₁₂N₂O₅
• 分子量: 336.304
• InChiKey: KWRMAQBKSXXWNB-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.72
• 重原子数：
  25.0
• 可旋转键数：
  4.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  113.56
• 氢给体数：
  2.0
• 氢受体数：
  5.0

反应信息

• 作为产物：
  描述：

  8-羟基-2-甲基喹啉-7-羧酸 、 对硝基苯甲醛 在 乙酸酐 、 吡啶 作用下， 以 水 为溶剂， 生成 8-hydroxy-2-[2-(4-nitrophenyl)ethenyl]quinoline-7-carboxylic acid
  参考文献：
  名称：

  Identification and structure–activity relationship of 8-hydroxy-quinoline-7-carboxylic acid derivatives as inhibitors of Pim-1 kinase

  摘要：

  Pim-1 kinase is a cytoplasmic serine/threonine kinase that controls programmed cell death by phosphorylating substrates that regulate both apotosis and cellular metabolism. A series of 2-styrylquinolines and quinoline-2-carboxamides has been identified as potent inhibitors of the Pim-1 kinase. The 8-hydroxyquinoline 7-carboxylic acid moiety appeared to be a crucial pharmacophore for activity. Molecular modeling indicated that interaction of this scaffold with Asp186 and Lys67 residues within the ATP-binding pocket might be responsible for the kinase inhibitory potency. (C) 2010 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2010.03.061

文献信息

• Identification and structure–activity relationship of 8-hydroxy-quinoline-7-carboxylic acid derivatives as inhibitors of Pim-1 kinase
  作者：Faten Sliman、Mélina Blairvacq、Emilie Durieu、Laurent Meijer、Jordi Rodrigo、Didier Desmaële

  DOI：10.1016/j.bmcl.2010.03.061

  日期：2010.5

  Pim-1 kinase is a cytoplasmic serine/threonine kinase that controls programmed cell death by phosphorylating substrates that regulate both apotosis and cellular metabolism. A series of 2-styrylquinolines and quinoline-2-carboxamides has been identified as potent inhibitors of the Pim-1 kinase. The 8-hydroxyquinoline 7-carboxylic acid moiety appeared to be a crucial pharmacophore for activity. Molecular modeling indicated that interaction of this scaffold with Asp186 and Lys67 residues within the ATP-binding pocket might be responsible for the kinase inhibitory potency. (C) 2010 Elsevier Ltd. All rights reserved.