4-((4-(4-fluorophenyl)piperazin-1-yl)sulfonyl)-1,3-dimethoxy-7-nitro-9H-xanthen-9-one

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并吡喃
• 英文名称: 4-((4-(4-fluorophenyl)piperazin-1-yl)sulfonyl)-1,3-dimethoxy-7-nitro-9H-xanthen-9-one
• 英文别名: 4-((4-(4-fluorophenyl)piperazin-1-yl)sulfonyl)-1,3-Dimethoxy-7-nitro-9H-xanthen-9-one (1f)；4-[4-(4-fluorophenyl)piperazin-1-yl]sulfonyl-1,3-dimethoxy-7-nitroxanthen-9-one
• 化学式: C₂₅H₂₂FN₃O₈S
• 分子量: 543.529
• InChiKey: HDFDSEUGQQZIIK-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.6
• 重原子数：
  38
• 可旋转键数：
  5
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.24
• 拓扑面积：
  140
• 氢给体数：
  0
• 氢受体数：
  11

反应信息

• 作为产物：
  描述：

  5-硝基水杨酸 在 氯磺酸 、 甲烷磺酸 、 四磷十氧化物 、 potassium carbonate 作用下， 以 1,4-二氧六环 、 二氯甲烷 为溶剂， 反应 14.5h， 生成 4-((4-(4-fluorophenyl)piperazin-1-yl)sulfonyl)-1,3-dimethoxy-7-nitro-9H-xanthen-9-one
  参考文献：
  名称：

  Synthesis, Biological Evaluation, and Molecular Docking Studies of Xanthone Sulfonamides as ACAT Inhibitors

  摘要：

  Three series of xanthone sulfonamides were synthesized, and their inhibitory activities against acyl‐CoA: cholesterol acyltransferase (ACAT) were evaluated. Results showed that most of the title compounds exhibited strong inhibitory activity against ACAT, of which compounds 1c, 1e, 1f, 2d, 2e, and 3d were proved to be more active than the positive control Sandoz 58‐035. Computational docking experiments indicated that the interaction between inhibitors and ACAT contained the H‐bond interaction, the hydrophobic interaction, and the narrow hydrophobic cleft.

  DOI：

  10.1111/cbdd.12419

文献信息

• Synthesis, Biological Evaluation, and Molecular Docking Studies of Xanthone Sulfonamides as ACAT Inhibitors
  作者：Xiang Li、Yan Zou、Qingjie Zhao、Yan Yang、Maocheng Wu、Ting Huang、Honggang Hu、Qiuye Wu

  DOI：10.1111/cbdd.12419

  日期：2015.3

  Three series of xanthone sulfonamides were synthesized, and their inhibitory activities against acyl‐CoA: cholesterol acyltransferase (ACAT) were evaluated. Results showed that most of the title compounds exhibited strong inhibitory activity against ACAT, of which compounds 1c, 1e, 1f, 2d, 2e, and 3d were proved to be more active than the positive control Sandoz 58‐035. Computational docking experiments indicated that the interaction between inhibitors and ACAT contained the H‐bond interaction, the hydrophobic interaction, and the narrow hydrophobic cleft.