1-[5-Tert-butyl-2-(4-methylphenyl)pyrazol-3-yl]-3-[4-(1,2,4-triazol-4-yl)phenyl]urea | 1454771-53-9

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 唑类
• 英文名称: 1-[5-Tert-butyl-2-(4-methylphenyl)pyrazol-3-yl]-3-[4-(1,2,4-triazol-4-yl)phenyl]urea
• 英文别名: 1-[5-tert-butyl-2-(4-methylphenyl)pyrazol-3-yl]-3-[4-(1,2,4-triazol-4-yl)phenyl]urea
• CAS: 1454771-53-9
• 化学式: C₂₃H₂₅N₇O
• 分子量: 415.498
• InChiKey: QWBIFVYQZVMANV-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4
• 重原子数：
  31
• 可旋转键数：
  5
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.22
• 拓扑面积：
  89.7
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  5-叔丁基-2-对甲苯基-2H-吡唑-3-胺 在 吡啶 作用下， 以 四氢呋喃 、 二甲基亚砜 为溶剂， 反应 17.0h， 生成 1-[5-Tert-butyl-2-(4-methylphenyl)pyrazol-3-yl]-3-[4-(1,2,4-triazol-4-yl)phenyl]urea
  参考文献：
  名称：

  Fragment-based discovery of focal adhesion kinase inhibitors

  摘要：

  Chemically diverse fragment hits of focal adhesion kinase (FAK) were discovered by surface plasmon resonance (SPR) screening of our in-house fragment library. Site specific binding of the primary hits was confirmed in a competition setup using a high-affinity ATP-site inhibitor of FAK. Protein crystallography revealed the binding mode of 41 out of 48 selected fragment hits within the ATP-site. Structural comparison of the fragment binding modes with a DFG-out inhibitor of FAK initiated first synthetic follow-up optimization leading to improved binding affinity. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2013.07.050

文献信息

• Fragment-based discovery of focal adhesion kinase inhibitors
  作者：Ulrich Grädler、Jörg Bomke、Djordje Musil、Verena Dresing、Martin Lehmann、Günter Hölzemann、Hartmut Greiner、Christina Esdar、Mireille Krier、Timo Heinrich

  DOI：10.1016/j.bmcl.2013.07.050

  日期：2013.10

  Chemically diverse fragment hits of focal adhesion kinase (FAK) were discovered by surface plasmon resonance (SPR) screening of our in-house fragment library. Site specific binding of the primary hits was confirmed in a competition setup using a high-affinity ATP-site inhibitor of FAK. Protein crystallography revealed the binding mode of 41 out of 48 selected fragment hits within the ATP-site. Structural comparison of the fragment binding modes with a DFG-out inhibitor of FAK initiated first synthetic follow-up optimization leading to improved binding affinity. (C) 2013 Elsevier Ltd. All rights reserved.