1-(3,4-dichlorophenyl)-3-ethoxycarbonyl-5-phenyl-1H-pyrazole | 781663-72-7

• 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)-3-ethoxycarbonyl-5-phenyl-1H-pyrazole
• 英文别名: Ethyl 1-(3,4-dichlorophenyl)-5-phenylpyrazole-3-carboxylate
• CAS: 781663-72-7
• 化学式: C₁₈H₁₄Cl₂N₂O₂
• 分子量: 361.227
• InChiKey: AQSNRPIJHPNRQA-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.4
• 重原子数：
  24
• 可旋转键数：
  5
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.11
• 拓扑面积：
  44.1
• 氢给体数：
  0
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  1-(3,4-dichlorophenyl)-3-ethoxycarbonyl-5-phenyl-1H-pyrazole 在 锂硼氢 、 caesium carbonate 、 三苯基膦 作用下， 以 四氢呋喃 、 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 88.5h， 生成 1-(3,4-dichlorophenyl)-3-[3-fluoro-5-(4-methoxytetrahydropyran-4-yl)phenoxymethyl]-5-phenyl-1H-pyrazole
  参考文献：
  名称：

  New COX-2/5-LOX Inhibitors:  Apoptosis-Inducing Agents Potentially Useful in Prostate Cancer Chemotherapy

  摘要：

  The arachidonic acid metabolizing enzymes cyclooxygenase-2 (COX-2) and lipoxygenases (LOXs) have been found to be implicated in a variety of cancers, including prostate cancer. To develop new therapeutic treatments, it therefore seemed interesting to design dual COX-2/5-LOX inhibitors. We report here the synthesis and in vitro pharmacological properties of diarylpyrazole derivatives that have in their structure key pharmacophoric elements to obtain optimal interaction with subsites of active pockets in both enzyme systems. Using a molecular modeling approach, a set of SAR data is proposed, highlighting the importance of the sulfonyl group of one of the aryl moieties in terms of proliferation inhibition and/or apoptosis induction.

  DOI：

  10.1021/jm0407761
• 作为产物：
  描述：

  苯乙酮 在 sodium ethanolate 作用下， 以 乙醇 为溶剂， 反应 0.83h， 生成 1-(3,4-dichlorophenyl)-3-ethoxycarbonyl-5-phenyl-1H-pyrazole
  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