3-(9H-purin-6-ylamino)-4-methyl-N-(3-(trifluoromethyl)phenyl)benzamide | 958840-14-7

• 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: 3-(9H-purin-6-ylamino)-4-methyl-N-(3-(trifluoromethyl)phenyl)benzamide
• 英文别名: 4-methyl-3-(7H-purin-6-ylamino)-N-[3-(trifluoromethyl)phenyl]benzamide
• CAS: 958840-14-7
• 化学式: C₂₀H₁₅F₃N₆O
• 分子量: 412.374
• InChiKey: GTBSGAPIEKIYFO-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.1
• 重原子数：
  30
• 可旋转键数：
  4
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.1
• 拓扑面积：
  95.6
• 氢给体数：
  3
• 氢受体数：
  8

反应信息

• 作为产物：
  描述：

  N-(3-氨基-4-甲基苯基)-3-(三氟甲基)苯甲酰胺 、 6-氯嘌呤 在 tris-(dibenzylideneacetone)dipalladium(0) 、 2-(二叔丁基膦)联苯 、 sodium t-butanolate 作用下， 以 甲苯 为溶剂， 反应 48.0h， 以40%的产率得到3-(9H-purin-6-ylamino)-4-methyl-N-(3-(trifluoromethyl)phenyl)benzamide
  参考文献：
  名称：

  Discovery and structural analysis of Eph receptor tyrosine kinase inhibitors

  摘要：

  The Eph family of receptor tyrosine kinases has drawn growing attention due to their role in regulating diverse biological phenomena. However, pharmacological interrogation of Eph kinase function has been hampered by a lack of potent and selective Eph kinase inhibitors. Here we report the discovery of compounds 6 and 9 using a rationally designed kinase-directed library which potently inhibit Eph receptor tyrosine kinases, particularly EphB2 with cellular EC(50)s of 40 nM. Crystallographic data of EphA3 and EphA7 in complex with the inhibitors show that they bind to the 'DFG-out' inactive kinase conformation and provide valuable information for structure-based design of second generation inhibitors. (C) 2009 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2009.05.029

文献信息

• Discovery and structural analysis of Eph receptor tyrosine kinase inhibitors
  作者：Yongmun Choi、Farisa Syeda、John R. Walker、Patrick J. Finerty、Dominic Cuerrier、Amy Wojciechowski、Qingsong Liu、Sirano Dhe-Paganon、Nathanael S. Gray

  DOI：10.1016/j.bmcl.2009.05.029

  日期：2009.8

  The Eph family of receptor tyrosine kinases has drawn growing attention due to their role in regulating diverse biological phenomena. However, pharmacological interrogation of Eph kinase function has been hampered by a lack of potent and selective Eph kinase inhibitors. Here we report the discovery of compounds 6 and 9 using a rationally designed kinase-directed library which potently inhibit Eph receptor tyrosine kinases, particularly EphB2 with cellular EC(50)s of 40 nM. Crystallographic data of EphA3 and EphA7 in complex with the inhibitors show that they bind to the 'DFG-out' inactive kinase conformation and provide valuable information for structure-based design of second generation inhibitors. (C) 2009 Elsevier Ltd. All rights reserved.