N-[1-(2-carbamoylethyl)-2-[(4-cyanobenzene)amido]-1H-1,3-benzodiazol-5-yl]-4-fluoro-N-methylbenzamide | 1085938-33-5

• 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: N-[1-(2-carbamoylethyl)-2-[(4-cyanobenzene)amido]-1H-1,3-benzodiazol-5-yl]-4-fluoro-N-methylbenzamide
• 英文别名: N-[1-(3-amino-3-oxopropyl)-5-[(4-fluorobenzoyl)-methylamino]benzimidazol-2-yl]-4-cyanobenzamide
• CAS: 1085938-33-5
• 化学式: C₂₆H₂₁FN₆O₃
• 分子量: 484.49
• InChiKey: IOQHKVXGXHYAJS-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.2
• 重原子数：
  36
• 可旋转键数：
  7
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.12
• 拓扑面积：
  134
• 氢给体数：
  2
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  对氰基苯甲酸 、 N-[2-amino-1-(3-amino-3-oxopropyl)-1H-benzimidazol-5-yl]-4-fluoro-N-methylbenzamide 在 benzotriazol-1-yloxyl-tris-(pyrrolidino)-phosphonium hexafluorophosphate 、 N,N-二异丙基乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 24.0h， 生成 N-[1-(2-carbamoylethyl)-2-[(4-cyanobenzene)amido]-1H-1,3-benzodiazol-5-yl]-4-fluoro-N-methylbenzamide
  参考文献：
  名称：

  Itk kinase inhibitors: Initial efforts to improve the metabolical stability and the cell activity of the benzimidazole lead

  摘要：

  Previously, we reported a series of novel benzimidazole based Itk inhibitors that exhibited excellent enzymatic potency and selectivity but low microsomal stability. Employing a structure based approach a new series of inhibitors with comparable potency and selectivity to the original series and with a potential for improved microsome stability was identified. (c) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2008.09.017

文献信息

• Crystal structure of the ITK kinase domain
  申请人：Bentzien Martin Joerg

  公开号：US20070032403A1

  公开（公告）日：2007-02-08

  Disclosed are polypeptides encoding the ITK kinase domain and nucleic acids encoding such polypeptides, crystal structures of various polypeptide-ligand complexes comprising the ITK kinase domain bound to a ligand, methods of producing the aforementioned polypeptides and nucleic acids which encode them and methods of producing crystal structures of the aforementioned polypeptides comprising the ITK kinase domain bound to a ligand.
• Itk kinase inhibitors: Initial efforts to improve the metabolical stability and the cell activity of the benzimidazole lead
  作者：Kevin J. Moriarty、Michael Winters、Lei Qiao、Declan Ryan、Renee DesJarlis、Darius Robinson、Brian N. Cook、Mohammed A. Kashem、Paul V. Kaplita、Lisa H. Liu、Thomas M. Farrell、Hnin Hnin Khine、Josephine King、Steven S. Pullen、Gregory P. Roth、Ronald Magolda、Hidenori Takahashi

  DOI：10.1016/j.bmcl.2008.09.017

  日期：2008.10

  Previously, we reported a series of novel benzimidazole based Itk inhibitors that exhibited excellent enzymatic potency and selectivity but low microsomal stability. Employing a structure based approach a new series of inhibitors with comparable potency and selectivity to the original series and with a potential for improved microsome stability was identified. (c) 2008 Elsevier Ltd. All rights reserved.