2-((3-(3-chlorophenyl)-7-methyl-4-oxo-3,4-dihydroquinazolin-2-yl)thio)hexanoic acid | 1146625-21-9

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 二氮杂萘
• 英文名称: 2-((3-(3-chlorophenyl)-7-methyl-4-oxo-3,4-dihydroquinazolin-2-yl)thio)hexanoic acid
• CAS: 1146625-21-9
• 化学式: C₂₁H₂₁ClN₂O₃S
• 分子量: 416.928
• InChiKey: VUUQTBHCIGGIST-UHFFFAOYSA-N

物化性质

• 沸点：
  614.0±65.0 °C(predicted)
• 密度：
  1.32±0.1 g/cm3(Temp: 20 °C; Press: 760 Torr)(predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  5.08
• 重原子数：
  28.0
• 可旋转键数：
  7.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.29
• 拓扑面积：
  72.19
• 氢给体数：
  1.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  哌啶-4-甲酰胺 、 2-((3-(3-chlorophenyl)-7-methyl-4-oxo-3,4-dihydroquinazolin-2-yl)thio)hexanoic acid 在 benzotriazol-1-yloxyl-tris-(pyrrolidino)-phosphonium hexafluorophosphate 、 三乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 生成 1-(2-(3-(3-Chlorophenyl)-7-methyl-4-oxo-3,4-dihydroquinazolin-2-ylthio)hexanoyl)piperidine-4-carboxamide
  参考文献：
  名称：

  Development of thioquinazolinones, allosteric Chk1 kinase inhibitors

  摘要：

  A high throughput screening campaign was designed to identify allosteric inhibitors of Chk1 kinase by testing compounds at high concentration. Activity was then observed at K(m) for ATP and at near-physiological concentrations of ATP. This strategy led to the discovery of a non-ATP competitive thioquinazolinone series which was optimized for potency and stability. An X-ray crystal structure for the complex of our best inhibitor bound to Chk1 was solved, indicating that it binds to an allosteric site approximately 13A from the ATP binding site. Preliminary data is presented for several of these compounds.

  DOI：

  10.1016/j.bmcl.2008.12.076
• 作为产物：
  描述：

  2-溴己酸 、 3-(3-chlorophenyl)-2-mercapto-7-methylquinazolin-4(3H)-one 在 三乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 生成 2-((3-(3-chlorophenyl)-7-methyl-4-oxo-3,4-dihydroquinazolin-2-yl)thio)hexanoic acid
  参考文献：
  名称：

  Development of thioquinazolinones, allosteric Chk1 kinase inhibitors

  摘要：

  A high throughput screening campaign was designed to identify allosteric inhibitors of Chk1 kinase by testing compounds at high concentration. Activity was then observed at K(m) for ATP and at near-physiological concentrations of ATP. This strategy led to the discovery of a non-ATP competitive thioquinazolinone series which was optimized for potency and stability. An X-ray crystal structure for the complex of our best inhibitor bound to Chk1 was solved, indicating that it binds to an allosteric site approximately 13A from the ATP binding site. Preliminary data is presented for several of these compounds.

  DOI：

  10.1016/j.bmcl.2008.12.076