ethyl 2-(2-aminopyrimidin-4-yl)-4-hydroxythiazole-5-carboxylate | 1612886-82-4

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 唑类
• 英文名称: ethyl 2-(2-aminopyrimidin-4-yl)-4-hydroxythiazole-5-carboxylate
• 英文别名: Ethyl 2-(2-aminopyrimidin-4-yl)-4-hydroxy-1,3-thiazole-5-carboxylate；ethyl 2-(2-aminopyrimidin-4-yl)-4-hydroxy-1,3-thiazole-5-carboxylate
• CAS: 1612886-82-4
• 化学式: C₁₀H₁₀N₄O₃S
• 分子量: 266.28
• InChiKey: FBYVCGXJFQPGCP-UHFFFAOYSA-N

物化性质

• 沸点：
  523.7±60.0 °C(predicted)
• 密度：
  1.487±0.06 g/cm3(Temp: 20 °C; Press: 760 Torr)(predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.7
• 重原子数：
  18
• 可旋转键数：
  4
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.2
• 拓扑面积：
  140
• 氢给体数：
  2
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  ethyl 2-(2-aminopyrimidin-4-yl)-4-hydroxythiazole-5-carboxylate 在 吡啶 、 trans-bis(triphenylphosphine)palladium dichloride 、 sodium carbonate decahydrate 作用下， 以 1,4-二氧六环 、 二氯甲烷 、 水 为溶剂， 反应 3.5h， 生成 ethyl 2-(2-aminopyrimidin-4-yl)-4-(3,5-dichlorophenyl)thiazole-5-carboxylate
  参考文献：
  名称：

  Synthesis and structure–activity relationship of trisubstituted thiazoles as Cdc7 kinase inhibitors

  摘要：

  The Cell division cycle 7 (Cdc7) protein kinase is essential for DNA replication and maintenance of genome stability. We systematically explored thiazole-based compounds as inhibitors of Cdc7 kinase activity in cancer cells. Our studies resulted in the identification of a potent, selective Cdc7 inhibitor that decreased phosphorylation of the direct substrate MCM2 in vitro and in vivo, and inhibited DNA synthesis and cell viability in vitro.

  DOI：

  10.1016/j.ejmech.2014.04.013
• 作为产物：
  描述：

  2-氨基-4-氰基嘧啶 在 吡啶 、 ammonium sulfide 、 三乙胺 作用下， 以 乙醇 为溶剂， 反应 18.0h， 生成 ethyl 2-(2-aminopyrimidin-4-yl)-4-hydroxythiazole-5-carboxylate
  参考文献：
  名称：

  Synthesis and structure–activity relationship of trisubstituted thiazoles as Cdc7 kinase inhibitors

  摘要：

  The Cell division cycle 7 (Cdc7) protein kinase is essential for DNA replication and maintenance of genome stability. We systematically explored thiazole-based compounds as inhibitors of Cdc7 kinase activity in cancer cells. Our studies resulted in the identification of a potent, selective Cdc7 inhibitor that decreased phosphorylation of the direct substrate MCM2 in vitro and in vivo, and inhibited DNA synthesis and cell viability in vitro.

  DOI：

  10.1016/j.ejmech.2014.04.013