6-fluoro-1-(2-fluoro-4-(trifluoromethyl)benzyl)-7-(4-methylpiperazin-1-yl)-4-oxo-N'-(2-phenylacetyl)-1,4-dihydroquinoline-3-carbohydrazide | 1240410-53-0

• 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: 6-fluoro-1-(2-fluoro-4-(trifluoromethyl)benzyl)-7-(4-methylpiperazin-1-yl)-4-oxo-N'-(2-phenylacetyl)-1,4-dihydroquinoline-3-carbohydrazide
• CAS: 1240410-53-0
• 化学式: C₃₁H₂₈F₅N₅O₃
• 分子量: 613.587
• InChiKey: GXKJHCXMIRLZHV-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.1
• 重原子数：
  44.0
• 可旋转键数：
  6.0
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.26
• 拓扑面积：
  86.68
• 氢给体数：
  2.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  6-fluoro-1-(2-fluoro-4-(trifluoromethyl)benzyl)-7-(4-methylpiperazin-1-yl)-4-oxo-N'-(2-phenylacetyl)-1,4-dihydroquinoline-3-carbohydrazide 在 碘 、 三乙胺 作用下， 以 二氯甲烷 为溶剂， 生成 3-(5-benzyl-[1,3,4]oxadiazol-2-yl)-1-(4-(2-fluoro-4-trifluormethyl)-benzyl)-6-fluoro-7-(4-methyl-piperazin-1-yl)-1H-quinolin-4-one
  参考文献：
  名称：

  3-Heterocyclyl quinolone inhibitors of the HCV NS5B polymerase

  摘要：

  The discovery and optimization of a novel class of quinolone small-molecules that inhibit NS5B polymerase, a key enzyme of the HCV viral life-cycle, is described. Our research led to the replacement of a hydrolytically labile ester functionality with bio-isosteric heterocycles. An X-ray crystal structure of a key analog bound to NS5B facilitated the optimization of this series of compounds to afford increased activity against the target enzyme and in the cell-based replicon assay system. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2011.11.013
• 作为产物：
  描述：

  在 N,N-二异丙基乙胺 、 三氯乙腈 作用下， 以 四氢呋喃 为溶剂， 反应 0.42h， 生成 6-fluoro-1-(2-fluoro-4-(trifluoromethyl)benzyl)-7-(4-methylpiperazin-1-yl)-4-oxo-N'-(2-phenylacetyl)-1,4-dihydroquinoline-3-carbohydrazide
  参考文献：
  名称：

  3-Heterocyclyl quinolone inhibitors of the HCV NS5B polymerase

  摘要：

  The discovery and optimization of a novel class of quinolone small-molecules that inhibit NS5B polymerase, a key enzyme of the HCV viral life-cycle, is described. Our research led to the replacement of a hydrolytically labile ester functionality with bio-isosteric heterocycles. An X-ray crystal structure of a key analog bound to NS5B facilitated the optimization of this series of compounds to afford increased activity against the target enzyme and in the cell-based replicon assay system. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2011.11.013