5-(2-chlorophenyl)-4-(3-chlorophenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione | 713096-39-0

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 唑类
• 英文名称: 5-(2-chlorophenyl)-4-(3-chlorophenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
• 英文别名: 3-(2-chlorophenyl)-4-(3-chlorophenyl)-1H-1,2,4-triazole-5-thione
• CAS: 713096-39-0
• 化学式: C₁₄H₉Cl₂N₃S
• 分子量: 322.218
• InChiKey: YYIJGKCGSLRVRG-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.4
• 重原子数：
  20
• 可旋转键数：
  2
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  59.7
• 氢给体数：
  1
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  5-(2-chlorophenyl)-4-(3-chlorophenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione 、 溴乙酸 在 potassium hydroxide 作用下， 以 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 0.33h， 生成 2-[[5-(2-Chlorophenyl)-4-(3-chlorophenyl)-1,2,4-triazol-3-yl]sulfanyl]acetic acid
  参考文献：
  名称：

  Discovery of Protein–Protein Interaction Inhibitors of Replication Protein A

  摘要：

  Replication protein A (RPA) is a ssDNA binding protein that is essential for DNA replication and repair. The initiation of the DNA damage response by RPA is mediated by protein protein interactions involving the N-terminal domain of the 70 kDa subunit with partner proteins. Inhibition of these interactions increases sensitivity toward DNA damage and replication stress and may therefore be a potential strategy for cancer drug discovery. Toward this end, we have discovered two lead series of compounds, derived from hits obtained from a fragment-based screen that bind to RPA70N with low micromolar affinity and inhibit the binding of an ATRIP-derived peptide to RPA. These compounds may offer a promising starting point for the discovery of clinically useful RP inhibitors.

  DOI：

  10.1021/ml400032y
• 作为产物：
  描述：

  N-(3-chlorophenyl)-1H-imidazole-1-carbothioamide 在 potassium hydroxide 作用下， 以 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 0.92h， 生成 5-(2-chlorophenyl)-4-(3-chlorophenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione
  参考文献：
  名称：

  Discovery of Protein–Protein Interaction Inhibitors of Replication Protein A

  摘要：

  Replication protein A (RPA) is a ssDNA binding protein that is essential for DNA replication and repair. The initiation of the DNA damage response by RPA is mediated by protein protein interactions involving the N-terminal domain of the 70 kDa subunit with partner proteins. Inhibition of these interactions increases sensitivity toward DNA damage and replication stress and may therefore be a potential strategy for cancer drug discovery. Toward this end, we have discovered two lead series of compounds, derived from hits obtained from a fragment-based screen that bind to RPA70N with low micromolar affinity and inhibit the binding of an ATRIP-derived peptide to RPA. These compounds may offer a promising starting point for the discovery of clinically useful RP inhibitors.

  DOI：

  10.1021/ml400032y