2-[4-[[[4-(4-Chlorophenyl)-6-cyclopropyl-1,3,5-triazin-2-yl]amino]methyl]phenyl]acetic acid | 1622386-69-9

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 三嗪类
• 英文名称: 2-[4-[[[4-(4-Chlorophenyl)-6-cyclopropyl-1,3,5-triazin-2-yl]amino]methyl]phenyl]acetic acid
• 英文别名: 2-[4-[[[4-(4-chlorophenyl)-6-cyclopropyl-1,3,5-triazin-2-yl]amino]methyl]phenyl]acetic acid
• CAS: 1622386-69-9
• 化学式: C₂₁H₁₉ClN₄O₂
• 分子量: 394.86
• InChiKey: PPPWGCVQMNAKQA-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.1
• 重原子数：
  28
• 可旋转键数：
  7
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.24
• 拓扑面积：
  88
• 氢给体数：
  2
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  对氯苯甲腈 在 sodium methylate 、 溶剂黄146 、 三氯氧磷 作用下， 以 甲醇 、 乙腈 为溶剂， 反应 5.0h， 生成 2-[4-[[[4-(4-Chlorophenyl)-6-cyclopropyl-1,3,5-triazin-2-yl]amino]methyl]phenyl]acetic acid
  参考文献：
  名称：

  Discovery of triazines as selective PDE4B versus PDE4D inhibitors

  摘要：

  In this study we report a series of triazine derivatives that are potent inhibitors of PDE4B. We also provide a series of structure activity relationships that demonstrate the triazine core can be used to generate subtype selective inhibitors of PDE4B versus PDE4D. A high resolution co-crystal structure shows that the inhibitors interact with a C-terminal regulatory helix (CR3) locking the enzyme in an inactive 'closed' conformation. The results show that the compounds interact with both catalytic domain and CR3 residues. This provides the first structure-based approach to engineer PDE4B-selective inhibitors. (C) 2014 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2014.06.002

文献信息

• Discovery of triazines as selective PDE4B versus PDE4D inhibitors
  作者：Timothy J. Hagen、Xuesheng Mo、Alex B. Burgin、David Fox、Zheng Zhang、Mark E. Gurney

  DOI：10.1016/j.bmcl.2014.06.002

  日期：2014.8

  In this study we report a series of triazine derivatives that are potent inhibitors of PDE4B. We also provide a series of structure activity relationships that demonstrate the triazine core can be used to generate subtype selective inhibitors of PDE4B versus PDE4D. A high resolution co-crystal structure shows that the inhibitors interact with a C-terminal regulatory helix (CR3) locking the enzyme in an inactive 'closed' conformation. The results show that the compounds interact with both catalytic domain and CR3 residues. This provides the first structure-based approach to engineer PDE4B-selective inhibitors. (C) 2014 Elsevier Ltd. All rights reserved.