1-methyl-5-[2-[4-(trifluoromethyl)phenyl]ethylimino]-7,8-dihydro-6H-quinolin-2-one

• 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-methyl-5-[2-[4-(trifluoromethyl)phenyl]ethylimino]-7,8-dihydro-6H-quinolin-2-one
• 化学式: C₁₉H₁₉F₃N₂O
• 分子量: 348.368
• InChiKey: CJHPYBRRLWPZEV-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.2
• 重原子数：
  25
• 可旋转键数：
  3
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.37
• 拓扑面积：
  32.7
• 氢给体数：
  0
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  1-methyl-5-[2-[4-(trifluoromethyl)phenyl]ethylimino]-7,8-dihydro-6H-quinolin-2-one 在 sodium tetrahydroborate 作用下， 以 乙醇 为溶剂， 反应 1.0h， 生成 5-[[2-(4-trifluoromethylphenyl)ethyl]amino]-5,6,7,8-tetrahydro-1-methyl-2(1H)-quinolinone
  参考文献：
  名称：

  Synthesis and Evaluation of 5-Amino-5,6,7,8-tetrahydroquinolinones as Potential Agents for the Treatment of Alzheimer's Disease

  摘要：

  A series of 5-amino-5,6,7,8-tetrahydroquinolinones was designed and synthesized as acetylcholinesterase inhibitors. The compounds are related to hyperzine A, a naturally occurring cholinesterase inhibitor. They inhibit acetylcholinesterase in vitro, and many are active in vivo in reversing a scopolamine-induced impairment of 24 h memory in a passive avoidance paradigm. Although these compounds were designed as partial structures of huperzine A, it is unlikely that they bind to the enzyme in a similar fashion, since they lack the unsaturated three-carbon bridge of huperzine A and both the quinolinone nitrogen and the amino group must be substituted in order to obtain good enzyme affinity.

  DOI：

  10.1021/jm00018a025
• 作为产物：
  描述：

  7,8-二氢-1H,6H-喹啉-2,5-二酮 在 lithium hydride 、 对甲苯磺酸 作用下， 以 甲苯 为溶剂， 反应 106.0h， 生成 1-methyl-5-[2-[4-(trifluoromethyl)phenyl]ethylimino]-7,8-dihydro-6H-quinolin-2-one
  参考文献：
  名称：

  Synthesis and Evaluation of 5-Amino-5,6,7,8-tetrahydroquinolinones as Potential Agents for the Treatment of Alzheimer's Disease

  摘要：

  A series of 5-amino-5,6,7,8-tetrahydroquinolinones was designed and synthesized as acetylcholinesterase inhibitors. The compounds are related to hyperzine A, a naturally occurring cholinesterase inhibitor. They inhibit acetylcholinesterase in vitro, and many are active in vivo in reversing a scopolamine-induced impairment of 24 h memory in a passive avoidance paradigm. Although these compounds were designed as partial structures of huperzine A, it is unlikely that they bind to the enzyme in a similar fashion, since they lack the unsaturated three-carbon bridge of huperzine A and both the quinolinone nitrogen and the amino group must be substituted in order to obtain good enzyme affinity.

  DOI：

  10.1021/jm00018a025