6-chloro-3,4-dihydro-2H-1,4-benzoxazine-2-carboxylic acid hydrazide | 866134-48-7

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: 6-chloro-3,4-dihydro-2H-1,4-benzoxazine-2-carboxylic acid hydrazide
• 英文别名: 6-chloro-3,4-dihydro-2H-1,4-benzoxazine-2-carbohydrazide
• CAS: 866134-48-7
• 化学式: C₉H₁₀ClN₃O₂
• 分子量: 227.65
• InChiKey: YKOXYTVXRJJPIO-UHFFFAOYSA-N

物化性质

• 沸点：
  488.6±45.0 °C(Predicted)
• 密度：
  1.400±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.9
• 重原子数：
  15
• 可旋转键数：
  1
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.22
• 拓扑面积：
  76.4
• 氢给体数：
  3
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  6-chloro-3,4-dihydro-2H-1,4-benzoxazine-2-carboxylic acid hydrazide 、 4-氨基乙基联苯 、 二吡啶硫碳酸酯 在 potassium hydroxide 作用下， 以 N,N-二甲基甲酰胺 、 乙醇 、 水 为溶剂， 反应 8.0h， 以82%的产率得到5-(4-chlorobenzyloxymethyl)-4-(4-phenylbenzyl)-2,4-dihydro[1,2,4]triazole-3-thiol potassium salt
  参考文献：
  名称：

  New non-hydroxamic ADAMTS-5 inhibitors based on the 1,2,4-triazole-3-thiol scaffold

  摘要：

  In this Letter we describe the design, synthesis, screening, and optimization of a new family of ADAMTS-5 inhibitors. These inhibitors display an original 1,2,4-triazole-3-thiol scaffold as a putative zinc binding-group. In vitro results are rationalized by in silico docking of the compounds in ADAMTS-5's crystal structure. (C) 2010 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2010.08.108
• 作为产物：
  描述：

  4-氯-2-氨基苯酚 在 potassium carbonate 、 一水合肼 作用下， 以 乙醇 、 丙酮 为溶剂， 反应 20.0h， 生成 6-chloro-3,4-dihydro-2H-1,4-benzoxazine-2-carboxylic acid hydrazide
  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