1-(3,4-dichlorophenyl)-5-(4-((4-methoxybenzyl)carbamothioyl)phenyl)-1H-pyrazole-3-carboxylic acid

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 唑类
• 英文名称: 1-(3,4-dichlorophenyl)-5-(4-((4-methoxybenzyl)carbamothioyl)phenyl)-1H-pyrazole-3-carboxylic acid
• 英文别名: 1-(3,4-Dichlorophenyl)-5-[4-[(4-methoxyphenyl)methylcarbamothioyl]phenyl]pyrazole-3-carboxylic acid；1-(3,4-dichlorophenyl)-5-[4-[(4-methoxyphenyl)methylcarbamothioyl]phenyl]pyrazole-3-carboxylic acid
• 化学式: C₂₅H₁₉Cl₂N₃O₃S
• 分子量: 512.416
• InChiKey: QTWCHVWOXHAAPT-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  6
• 重原子数：
  34
• 可旋转键数：
  7
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.08
• 拓扑面积：
  109
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  4-乙酰基苯甲酸 在 劳森试剂 、 sodium ethanolate 、 1-羟基苯并三唑 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 、 三乙胺 、 lithium hydroxide 作用下， 以 四氢呋喃 、 乙醇 、 N,N-二甲基甲酰胺 为溶剂， 反应 13.33h， 生成 1-(3,4-dichlorophenyl)-5-(4-((4-methoxybenzyl)carbamothioyl)phenyl)-1H-pyrazole-3-carboxylic acid
  参考文献：
  名称：

  Diphenylpyrazoles as Replication Protein A Inhibitors

  摘要：

  Replication Protein A is the primary eukaryotic ssDNA binding protein that has a central role in initiating the cellular response to DNA damage. RPA recruits multiple proteins to sites of DNA damage via the N-terminal domain of the 70 kDa subunit (RPA70N). Here we describe the optimization of a diphenylpyrazole carboxylic acid series of inhibitors of these RPA-protein interactions. We evaluated substituents on the aromatic rings as well as the type and geometry of the linkers used to combine fragments, ultimately leading to submicromolar inhibitors of RPA70N protein-protein interactions.

  DOI：

  10.1021/ml5003629

文献信息

• Diphenylpyrazoles as Replication Protein A Inhibitors
  作者：Alex G. Waterson、J. Phillip Kennedy、James D. Patrone、Nicholas F. Pelz、Michael D. Feldkamp、Andreas O. Frank、Bhavatarini Vangamudi、Elaine M. Souza-Fagundes、Olivia W. Rossanese、Walter J. Chazin、Stephen W. Fesik

  DOI：10.1021/ml5003629

  日期：2015.2.12

  Replication Protein A is the primary eukaryotic ssDNA binding protein that has a central role in initiating the cellular response to DNA damage. RPA recruits multiple proteins to sites of DNA damage via the N-terminal domain of the 70 kDa subunit (RPA70N). Here we describe the optimization of a diphenylpyrazole carboxylic acid series of inhibitors of these RPA-protein interactions. We evaluated substituents on the aromatic rings as well as the type and geometry of the linkers used to combine fragments, ultimately leading to submicromolar inhibitors of RPA70N protein-protein interactions.