N-(o-Nitro-benzoyl)-N'-carbamimidoyl-hydrazin

• 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-(o-Nitro-benzoyl)-N'-carbamimidoyl-hydrazin
• 英文别名: N-(o-Nitrobenzoyl)-N'-guanyl-hydrazin；[(2-Nitrophenyl)formohydrazido]methanimidamide；N-(diaminomethylideneamino)-2-nitrobenzamide
• 化学式: C₈H₉N₅O₃
• 分子量: 223.191
• InChiKey: WXRFUVQFPQGDJJ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1
• 重原子数：
  16
• 可旋转键数：
  2
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  139
• 氢给体数：
  3
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  N-(o-Nitro-benzoyl)-N'-carbamimidoyl-hydrazin 在 sodium hydroxide 作用下， 以 乙醇 、 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 5.0h， 生成 2-(2-nitrophenyl)-5-(methylthio)-[1,2,4]triazolo[1,5-a][1,3,5]triazin-7-one
  参考文献：
  名称：

  Synthesis, anti-thymidine phosphorylase activity and molecular docking of 5-thioxo-[1,2,4]triazolo[1,5-a][1,3,5]triazin-7-ones

  摘要：

  In our lead finding program, a series of 5-thioxo-[1,2,4] triazolo[1,5-a][1,3,5]triazin-7-ones and their 5-thio- alkyl derivatives were designed and synthesized which contained different substituents at ortho-position of 2-phenyl ring attached to the fused ring structure. The preliminary pharmacological evaluation demonstrated that the synthesized compounds exhibited a varying degree of inhibitory activity towards thymidine phosphorylase (TP), comparable to reference compound, 7-Deazaxanthine (7-DX, 2) (IC50 value = 42.63 mu M). The study also inferred that the ortho-substituted group at the phenyl ring and 5-thio-alkyl moiety imparted steric hindrance effects in the binding site of the enzyme, leading to a reduced inhibitory response. In addition, compound 3a was identified as a mixed-type inhibitor of TP. Moreover, computational docking study was performed to illustrate the important structural information on the plausible ligand-enzyme binding interactions. (C) 2013 Elsevier Inc. All rights reserved.

  DOI：

  10.1016/j.bioorg.2013.07.004
• 作为产物：
  描述：

  肼甲酰亚胺酰胺一氯化氢 、 2-硝基苯甲酰氯 生成 N-(o-Nitro-benzoyl)-N'-carbamimidoyl-hydrazin
  参考文献：
  名称：

  Synthesis, anti-thymidine phosphorylase activity and molecular docking of 5-thioxo-[1,2,4]triazolo[1,5-a][1,3,5]triazin-7-ones

  摘要：

  In our lead finding program, a series of 5-thioxo-[1,2,4] triazolo[1,5-a][1,3,5]triazin-7-ones and their 5-thio- alkyl derivatives were designed and synthesized which contained different substituents at ortho-position of 2-phenyl ring attached to the fused ring structure. The preliminary pharmacological evaluation demonstrated that the synthesized compounds exhibited a varying degree of inhibitory activity towards thymidine phosphorylase (TP), comparable to reference compound, 7-Deazaxanthine (7-DX, 2) (IC50 value = 42.63 mu M). The study also inferred that the ortho-substituted group at the phenyl ring and 5-thio-alkyl moiety imparted steric hindrance effects in the binding site of the enzyme, leading to a reduced inhibitory response. In addition, compound 3a was identified as a mixed-type inhibitor of TP. Moreover, computational docking study was performed to illustrate the important structural information on the plausible ligand-enzyme binding interactions. (C) 2013 Elsevier Inc. All rights reserved.

  DOI：

  10.1016/j.bioorg.2013.07.004

文献信息

• Synthesis, anti-thymidine phosphorylase activity and molecular docking of 5-thioxo-[1,2,4]triazolo[1,5-a][1,3,5]triazin-7-ones
  作者：Hriday Bera、Min Huey Lee、Lingyi Sun、Anton V. Dolzhenko、Wai Keung Chui

  DOI：10.1016/j.bioorg.2013.07.004

  日期：2013.10

  In our lead finding program, a series of 5-thioxo-[1,2,4] triazolo[1,5-a][1,3,5]triazin-7-ones and their 5-thio- alkyl derivatives were designed and synthesized which contained different substituents at ortho-position of 2-phenyl ring attached to the fused ring structure. The preliminary pharmacological evaluation demonstrated that the synthesized compounds exhibited a varying degree of inhibitory activity towards thymidine phosphorylase (TP), comparable to reference compound, 7-Deazaxanthine (7-DX, 2) (IC50 value = 42.63 mu M). The study also inferred that the ortho-substituted group at the phenyl ring and 5-thio-alkyl moiety imparted steric hindrance effects in the binding site of the enzyme, leading to a reduced inhibitory response. In addition, compound 3a was identified as a mixed-type inhibitor of TP. Moreover, computational docking study was performed to illustrate the important structural information on the plausible ligand-enzyme binding interactions. (C) 2013 Elsevier Inc. All rights reserved.