4-chloro-N-([(4-cyclohexylbutyl)carbamothioyl]amino)benzamide | 1489288-58-5

• 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: 4-chloro-N-([(4-cyclohexylbutyl)carbamothioyl]amino)benzamide
• 英文别名: 1-[(4-Chlorobenzoyl)amino]-3-(4-cyclohexylbutyl)thiourea；1-[(4-chlorobenzoyl)amino]-3-(4-cyclohexylbutyl)thiourea
• CAS: 1489288-58-5
• 化学式: C₁₈H₂₆ClN₃OS
• 分子量: 367.943
• InChiKey: QISOBBHFYDPGMO-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.8
• 重原子数：
  24
• 可旋转键数：
  6
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.56
• 拓扑面积：
  85.2
• 氢给体数：
  3
• 氢受体数：
  2

反应信息

• 作为产物：
  描述：

  4-环己基正丁胺 以 N,N-二甲基甲酰胺 为溶剂， 反应 3.0h， 生成 4-chloro-N-([(4-cyclohexylbutyl)carbamothioyl]amino)benzamide
  参考文献：
  名称：

  Aggrecanase-2 inhibitors based on the acylthiosemicarbazide zinc-binding group

  摘要：

  Osteoarthritis is a disabling disease characterized by the articular cartilage breakdown. Aggrecanases are potential therapeutic targets for the treatment of this pathology. At the starting point of this project, an acylthiosemicarbazide was discovered to inhibit aggrecanase-2. The acylthiosemicarbazide Zn binding group is also a convenient linker for library synthesis. A focused library of 920 analogs was thus prepared and screened to establish structure-activity relationships. The modification of the acylthiosemicarbazide was also explored. This strategy combining library design and discrete compounds synthesis yielded inhibitor 35, that is highly selective for aggrecanases over a panel of metalloproteases and inhibits the degradation of native fully glycosylated aggrecan. A docking study generated binding conformations explaining the structure activity relationships. (C) 2013 Elsevier Masson SAS. All rights reserved.

  DOI：

  10.1016/j.ejmech.2013.08.027

文献信息

• Aggrecanase-2 inhibitors based on the acylthiosemicarbazide zinc-binding group
  作者：Lucie Maingot、Jamal Elbakali、Julie Dumont、Damien Bosc、Nicolas Cousaert、Agathe Urban、Gaelle Deglane、Bruno Villoutreix、Hideaki Nagase、Olivier Sperandio、Florence Leroux、Benoit Deprez、Rebecca Deprez-Poulain

  DOI：10.1016/j.ejmech.2013.08.027

  日期：2013.11

  Osteoarthritis is a disabling disease characterized by the articular cartilage breakdown. Aggrecanases are potential therapeutic targets for the treatment of this pathology. At the starting point of this project, an acylthiosemicarbazide was discovered to inhibit aggrecanase-2. The acylthiosemicarbazide Zn binding group is also a convenient linker for library synthesis. A focused library of 920 analogs was thus prepared and screened to establish structure-activity relationships. The modification of the acylthiosemicarbazide was also explored. This strategy combining library design and discrete compounds synthesis yielded inhibitor 35, that is highly selective for aggrecanases over a panel of metalloproteases and inhibits the degradation of native fully glycosylated aggrecan. A docking study generated binding conformations explaining the structure activity relationships. (C) 2013 Elsevier Masson SAS. All rights reserved.