3-(4-(2-(methylthio)pyrimidin-4-yl)-2-(trifluoromethyl)phenoxy)propan-1-ol | 1243143-30-7

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 二嗪类
• 英文名称: 3-(4-(2-(methylthio)pyrimidin-4-yl)-2-(trifluoromethyl)phenoxy)propan-1-ol
• CAS: 1243143-30-7
• 化学式: C₁₅H₁₅F₃N₂O₂S
• 分子量: 344.358
• InChiKey: UANIFDGGYSTYHD-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.65
• 重原子数：
  23.0
• 可旋转键数：
  6.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  55.24
• 氢给体数：
  1.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  3-(4-(2-(methylthio)pyrimidin-4-yl)-2-(trifluoromethyl)phenoxy)propan-1-ol 在 Oxone 作用下， 以 水 、 乙腈 为溶剂， 反应 12.0h， 生成
  参考文献：
  名称：

  4-(3-Trifluoromethylphenyl)-pyrimidine-2-carbonitrile as cathepsin S inhibitors: N3, not N1 is critically important

  摘要：

  Using computer aided modelling studies, a new extended P2/S2 interaction was identified. This extended region can accommodate a variety of functional groups, such as aryls and basic amines. It was discovered that the N3 nitrogen of the pyrimidine-2-carbonitrile is critical for its cathepsin cysteine protease inhibition. N1 nitrogen also contributes to the inhibitory activity, but to a very limited degree. An 'in situ double activation' mechanism was proposed to explain these results. (C) 2010 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2010.06.043
• 作为产物：
  描述：

  2-甲硫基-4-氯嘧啶 、 3-(4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)-2-(trifluoromethyl)phenoxy)-propan-1-ol 在 potassium phosphate 、 tris-(dibenzylideneacetone)dipalladium(0) 、 三环己基膦 作用下， 以 1,4-二氧六环 、 水 为溶剂， 反应 3.0h， 生成 3-(4-(2-(methylthio)pyrimidin-4-yl)-2-(trifluoromethyl)phenoxy)propan-1-ol
  参考文献：
  名称：

  4-(3-Trifluoromethylphenyl)-pyrimidine-2-carbonitrile as cathepsin S inhibitors: N3, not N1 is critically important

  摘要：

  Using computer aided modelling studies, a new extended P2/S2 interaction was identified. This extended region can accommodate a variety of functional groups, such as aryls and basic amines. It was discovered that the N3 nitrogen of the pyrimidine-2-carbonitrile is critical for its cathepsin cysteine protease inhibition. N1 nitrogen also contributes to the inhibitory activity, but to a very limited degree. An 'in situ double activation' mechanism was proposed to explain these results. (C) 2010 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2010.06.043