3-acetyl-1-[(4-fluorophenyl)methyl]-7-(piperazin-1-yl)quinolin-4(1H)-one | 1598381-63-5

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 喹啉及其衍生物
• 英文名称: 3-acetyl-1-[(4-fluorophenyl)methyl]-7-(piperazin-1-yl)quinolin-4(1H)-one
• CAS: 1598381-63-5
• 化学式: C₂₂H₂₂FN₃O₂
• 分子量: 379.434
• InChiKey: OKMUIBOVOVWNCL-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.8
• 重原子数：
  28.0
• 可旋转键数：
  4.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.27
• 拓扑面积：
  54.34
• 氢给体数：
  1.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  3-acetyl-1-[(4-fluorophenyl)methyl]-7-(piperazin-1-yl)quinolin-4(1H)-one 在 sodium ethanolate 、 sodium hydroxide 作用下， 以 四氢呋喃 、 甲醇 为溶剂， 反应 2.67h， 生成 4-[1-[(4-fluorophenyl)methyl]-7-(piperazin-1-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid
  参考文献：
  名称：

  Basic Quinolinonyl Diketo Acid Derivatives as Inhibitors of HIV Integrase and their Activity against RNase H Function of Reverse Transcriptase

  摘要：

  A series of antiviral basic quinolinonyl diketo acid derivatives were developed as inhibitors of HIV-1 IN. Compounds 12d,f,i inhibited HIV-1 IN with IC50 values below 100 nM for strand transfer and showed a 2 order of magnitude selectivity over 3'-processing. These strand transfer selective inhibitors also inhibited HIV-1 RNase H with low micromolar potencies. Molecular modeling studies based on both the HIV-1 IN and RNase H catalytic core domains provided new structural insights for the future development of these compounds as dual HIV-1 IN and RNase H inhibitors.

  DOI：

  10.1021/jm5001503
• 作为产物：
  描述：

  3-氟苯胺 在 diphenyl ether-biphenyl eutectic 、 potassium carbonate 、 三乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 9.17h， 生成 3-acetyl-1-[(4-fluorophenyl)methyl]-7-(piperazin-1-yl)quinolin-4(1H)-one
  参考文献：
  名称：

  Basic Quinolinonyl Diketo Acid Derivatives as Inhibitors of HIV Integrase and their Activity against RNase H Function of Reverse Transcriptase

  摘要：

  A series of antiviral basic quinolinonyl diketo acid derivatives were developed as inhibitors of HIV-1 IN. Compounds 12d,f,i inhibited HIV-1 IN with IC50 values below 100 nM for strand transfer and showed a 2 order of magnitude selectivity over 3'-processing. These strand transfer selective inhibitors also inhibited HIV-1 RNase H with low micromolar potencies. Molecular modeling studies based on both the HIV-1 IN and RNase H catalytic core domains provided new structural insights for the future development of these compounds as dual HIV-1 IN and RNase H inhibitors.

  DOI：

  10.1021/jm5001503