4-(aminomethyl)pyrimidine-2-carbonitrile 4-methylbenzenesulfonic acid salt | 1616775-56-4

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: 4-(aminomethyl)pyrimidine-2-carbonitrile 4-methylbenzenesulfonic acid salt
• 英文别名: 4-(Aminomethyl)pyrimidine-2-carbonitrile;4-methylbenzenesulfonic acid
• CAS: 1616775-56-4
• 化学式: C₆H₆N₄*C₇H₈O₃S
• 分子量: 306.345
• InChiKey: MYFCGKNERZDTGH-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.05
• 重原子数：
  21.0
• 可旋转键数：
  2.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.15
• 拓扑面积：
  129.96
• 氢给体数：
  2.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  4-(aminomethyl)pyrimidine-2-carbonitrile 4-methylbenzenesulfonic acid salt 、 (S)-2-(2-(3,5-dichlorophenyl)acetamido)-3-methoxypropanoic acid 在 N-甲基吗啉 、 benzotriazol-1-yloxyl-tris-(pyrrolidino)-phosphonium hexafluorophosphate 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 18.0h， 以0.092 g的产率得到(S)-N-((2-cyanopyrimidin-4-yl)methyl)-2-(2-(3,5-dichlorophenyl)acetamido)-3-methoxypropanamide
  参考文献：
  名称：

  Discovery and Structure-Based Optimization of Adenain Inhibitors

  摘要：

  The cysteine protease adenain is the essential protease of adenovirus and, as such, represents a promising target for the treatment of ocular and other adenoviral infections. Through a concise two-pronged hit discovery approach we identified tetrapeptide nitrile 1 and pyrimidine nitrile 2 as complementary starting points for adenain inhibition. These hits enabled the first high-resolution X-ray cocrystal structures of adenain with inhibitors bound and revealed the binding mode of 1 and 2. The screening hits were optimized by a structure-guided medicinal chemistry strategy into low nanomolar drug-like inhibitors of adenain.

  DOI：

  10.1021/ml500224t
• 作为产物：
  描述：

  tert-butyl ((2-chloropyrimidin-4-yl)methyl)carbamate 在 三乙烯二胺 作用下， 以 二甲基亚砜 、 乙腈 为溶剂， 反应 2.0h， 生成 4-(aminomethyl)pyrimidine-2-carbonitrile 4-methylbenzenesulfonic acid salt
  参考文献：
  名称：

  Discovery and Structure-Based Optimization of Adenain Inhibitors

  摘要：

  The cysteine protease adenain is the essential protease of adenovirus and, as such, represents a promising target for the treatment of ocular and other adenoviral infections. Through a concise two-pronged hit discovery approach we identified tetrapeptide nitrile 1 and pyrimidine nitrile 2 as complementary starting points for adenain inhibition. These hits enabled the first high-resolution X-ray cocrystal structures of adenain with inhibitors bound and revealed the binding mode of 1 and 2. The screening hits were optimized by a structure-guided medicinal chemistry strategy into low nanomolar drug-like inhibitors of adenain.

  DOI：

  10.1021/ml500224t