1-ethyl-3-(6-(5-methoxypyridin-3-yl)benzo[d]thiazol-2-yl)urea

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并噻唑类
• 英文名称: 1-ethyl-3-(6-(5-methoxypyridin-3-yl)benzo[d]thiazol-2-yl)urea
• 英文别名: 1-Ethyl-3-[6-(5-methoxypyridin-3-yl)-1,3-benzothiazol-2-yl]urea；1-ethyl-3-[6-(5-methoxypyridin-3-yl)-1,3-benzothiazol-2-yl]urea
• 化学式: C₁₆H₁₆N₄O₂S
• 分子量: 328.395
• InChiKey: NRQJNWMHLPKGKI-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.6
• 重原子数：
  23
• 可旋转键数：
  4
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.19
• 拓扑面积：
  104
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  5-甲氧基-3-吡啶硼酸频哪醇酯 在 (1,1'-bis(diphenylphosphino)ferrocene)palladium(II) dichloride 、 sodium carbonate 、 三乙胺 作用下， 以 乙二醇二甲醚 、 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 8.0h， 生成 1-ethyl-3-(6-(5-methoxypyridin-3-yl)benzo[d]thiazol-2-yl)urea
  参考文献：
  名称：

  Structural Basis for Isoform Selectivity in a Class of Benzothiazole Inhibitors of Phosphoinositide 3-Kinase γ

  摘要：

  Phosphoinositide 3-kinase gamma (PI3K gamma) is an attractive target to potentially treat a range of disease states. Herein, we describe the evolution of a reported phenylthiazole pan-PI3K inhibitor into a family of potent and selective benzothiazole inhibitors. Using X-ray crystallography, we discovered that compound 22 occupies a previously unreported hydrophobic binding cleft adjacent to the ATP binding site of PI3K gamma, and achieves its selectivity by exploiting natural sequence differences among PI3K isoforms in this region.

  DOI：

  10.1021/jm500362j

文献信息

• Structural Basis for Isoform Selectivity in a Class of Benzothiazole Inhibitors of Phosphoinositide 3-Kinase γ
  作者：Philip N. Collier、Gabriel Martinez-Botella、Mark Cornebise、Kevin M. Cottrell、John D. Doran、James P. Griffith、Sudipta Mahajan、François Maltais、Cameron S. Moody、Emilie Porter Huck、Tiansheng Wang、Alex M. Aronov

  DOI：10.1021/jm500362j

  日期：2015.1.8

  Phosphoinositide 3-kinase gamma (PI3K gamma) is an attractive target to potentially treat a range of disease states. Herein, we describe the evolution of a reported phenylthiazole pan-PI3K inhibitor into a family of potent and selective benzothiazole inhibitors. Using X-ray crystallography, we discovered that compound 22 occupies a previously unreported hydrophobic binding cleft adjacent to the ATP binding site of PI3K gamma, and achieves its selectivity by exploiting natural sequence differences among PI3K isoforms in this region.