1-[[1-(5-chloro-2,4-dihydroxyphenyl)-2-oxo-3H-benzimidazol-5-yl]methyl]-3-ethylurea | 936218-58-5

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并咪唑类
• 英文名称: 1-[[1-(5-chloro-2,4-dihydroxyphenyl)-2-oxo-3H-benzimidazol-5-yl]methyl]-3-ethylurea
• CAS: 936218-58-5
• 化学式: C₁₇H₁₇ClN₄O₄
• 分子量: 376.799
• InChiKey: MLVRXZUTFAOHBQ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.5
• 重原子数：
  26
• 可旋转键数：
  4
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.18
• 拓扑面积：
  114
• 氢给体数：
  5
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  4-氟-3-硝基苯甲腈 在 硼烷四氢呋喃络合物 、 10% palladium on activated charcoal 、 氢气 、 三溴化硼 、 potassium carbonate 、 三乙胺 作用下， 以 N,N-二甲基乙酰胺 为溶剂， 生成 1-[[1-(5-chloro-2,4-dihydroxyphenyl)-2-oxo-3H-benzimidazol-5-yl]methyl]-3-ethylurea
  参考文献：
  名称：

  N-Aryl-benzimidazolones as novel small molecule HSP90 inhibitors

  摘要：

  We describe the development of a novel series of N-aryl-benzimidazolone HSP90 inhibitors ( 9) targeting the N-terminal ATP-ase site. SAR development was influenced by structure-based design based around Xray structures of ligand bound HSP90 complexes. Lead compounds exhibited high binding affinities, ATPase inhibition and cellular client protein degradation. (C) 2010 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2010.10.010

文献信息

• Heat-shock protein binders
  申请人：Bruncko Milan

  公开号：US20070105862A1

  公开（公告）日：2007-05-10

  Compounds which bind to and inhibit the activity of HSP90, compositions containing the compounds and methods of treating diseases that are caused or exascerbated by overexpression of HSP90 are disclosed.

  本发明公开了结合并抑制HSP90活性的化合物、含有该化合物的组合物以及治疗由HSP90过度表达引起或加重的疾病的方法。
• N-Aryl-benzimidazolones as novel small molecule HSP90 inhibitors
  作者：Milan Bruncko、Stephen K. Tahir、Xiaohong Song、Jun Chen、Hong Ding、Jeffrey R. Huth、Sha Jin、Russell A. Judge、David J. Madar、Chang H. Park、Cheol-Min Park、Andrew M. Petros、Christin Tse、Saul H. Rosenberg、Steven W. Elmore

  DOI：10.1016/j.bmcl.2010.10.010

  日期：2010.12

  We describe the development of a novel series of N-aryl-benzimidazolone HSP90 inhibitors ( 9) targeting the N-terminal ATP-ase site. SAR development was influenced by structure-based design based around Xray structures of ligand bound HSP90 complexes. Lead compounds exhibited high binding affinities, ATPase inhibition and cellular client protein degradation. (C) 2010 Elsevier Ltd. All rights reserved.