1-[(3-Chloro-1-benzothiophene-2-carbonyl)amino]-3-(3,4-dichlorophenyl)thiourea | 201614-03-1

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并噻吩类
• 英文名称: 1-[(3-Chloro-1-benzothiophene-2-carbonyl)amino]-3-(3,4-dichlorophenyl)thiourea
• CAS: 201614-03-1
• 化学式: C₁₆H₁₀Cl₃N₃OS₂
• 分子量: 430.766
• InChiKey: KBOKCKUBIQIFDP-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.9
• 重原子数：
  25
• 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：
  114
• 氢给体数：
  3
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  1-[(3-Chloro-1-benzothiophene-2-carbonyl)amino]-3-(3,4-dichlorophenyl)thiourea 在 potassium hydroxide 作用下， 以 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 0.5h， 生成
  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：

  3,4-二氯苯胺 以 N,N-二甲基甲酰胺 为溶剂， 反应 0.75h， 生成 1-[(3-Chloro-1-benzothiophene-2-carbonyl)amino]-3-(3,4-dichlorophenyl)thiourea
  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

文献信息

• Discovery of Protein–Protein Interaction Inhibitors of Replication Protein A
  作者：James D. Patrone、J. Phillip Kennedy、Andreas O. Frank、Michael D. Feldkamp、Bhavatarini Vangamudi、Nicholas F. Pelz、Olivia W. Rossanese、Alex G. Waterson、Walter J. Chazin、Stephen W. Fesik

  DOI：10.1021/ml400032y

  日期：2013.7.11

  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.