1-[(4-Chlorophenyl)methyl]-6,7-dimethoxy-3-(5-phenethyl-1,2,4-oxadiazol-3-yl)quinolin-4-one | 1356183-28-2

• 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: 1-[(4-Chlorophenyl)methyl]-6,7-dimethoxy-3-(5-phenethyl-1,2,4-oxadiazol-3-yl)quinolin-4-one
• 英文别名: 1-[(4-chlorophenyl)methyl]-6,7-dimethoxy-3-[5-(2-phenylethyl)-1,2,4-oxadiazol-3-yl]quinolin-4-one
• CAS: 1356183-28-2
• 化学式: C₂₈H₂₄ClN₃O₄
• 分子量: 501.969
• InChiKey: CUGXVGUDHBVRFW-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.9
• 重原子数：
  36
• 可旋转键数：
  8
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.18
• 拓扑面积：
  77.7
• 氢给体数：
  0
• 氢受体数：
  7

反应信息

• 作为产物：
  描述：

  1-(4-chloro-benzyl)-6,7-dimethoxy-4-oxo-1,4-dihydro-quinoline-3-carbonitrile 在 羟胺 、 O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate 、 N,N-二异丙基乙胺 作用下， 以 乙醇 、 水 为溶剂， 反应 0.05h， 生成 1-[(4-Chlorophenyl)methyl]-6,7-dimethoxy-3-(5-phenethyl-1,2,4-oxadiazol-3-yl)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

文献信息

• 3-Heterocyclyl quinolone inhibitors of the HCV NS5B polymerase
  作者：Dange V. Kumar、Roopa Rai、Ken A. Brameld、Jennifer Riggs、John R. Somoza、Ravi Rajagopalan、James W. Janc、Yu M. Xia、Tony L. Ton、Huiyong Hu、Isabelle Lehoux、Joseph D. Ho、Wendy B. Young、Barry Hart、Michael J. Green

  DOI：10.1016/j.bmcl.2011.11.013

  日期：2012.1

  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.