(+/-)-3,3-dimethyl-4-[(2-methoxyethoxy)methoxy]-1-cyclohexanone | 888325-28-8

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: (+/-)-3,3-dimethyl-4-[(2-methoxyethoxy)methoxy]-1-cyclohexanone
• 英文别名: 4-(2-Methoxyethoxymethoxy)-3,3-dimethylcyclohexan-1-one
• CAS: 888325-28-8
• 化学式: C₁₂H₂₂O₄
• 分子量: 230.304
• InChiKey: LOKKLQLQSTWJQR-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.9
• 重原子数：
  16
• 可旋转键数：
  6
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.92
• 拓扑面积：
  44.8
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  (+/-)-3,3-dimethyl-4-[(2-methoxyethoxy)methoxy]-1-cyclohexanone 在 potassium hydride 、 双(三甲基硅烷基)氨基钾 、 四甲基胍 作用下， 以 四氢呋喃 、 N,N-二甲基甲酰胺 、 甲苯 为溶剂， 反应 60.25h， 生成 (+/-)-(9Z)-7-((2-methoxyethoxy)methoxy)-9-ethylidene-3,6,6-trimethylbicyclo[3.3.1]non-3-ene-1-carboxylic acid methyl ester
  参考文献：
  名称：

  Discovery of Huperzine A−Tacrine Hybrids as Potent Inhibitors of Human Cholinesterases Targeting Their Midgorge Recognition Sites

  摘要：

  We describe herein the development of novel huperzine A-tacrine hybrids characterized by 3-methylbicyclo[3.3.1] non-3-ene scaffolds. These compounds were specifically designed to establish tight interactions, through different binding modes, with the midgorge recognition sites of human acetylcholinesterase (hAChE: Y72, D74) and human butyrylcholinesterase (hBuChE: N68, D70) and their catalytic or peripheral sites. Compounds 5a-c show a markedly improved biological profile relative to tacrine and huperzine A.

  DOI：

  10.1021/jm060257t
• 作为产物：
  描述：

  7,7-dimethyl-1,4-dioxaspiro[4.5]decan-8-one 在 盐酸 、 sodium tetrahydroborate 、 N,N-二异丙基乙胺 作用下， 以 乙醇 、 二氯甲烷 、 丙酮 为溶剂， 反应 77.0h， 生成 (+/-)-3,3-dimethyl-4-[(2-methoxyethoxy)methoxy]-1-cyclohexanone
  参考文献：
  名称：

  Discovery of Huperzine A−Tacrine Hybrids as Potent Inhibitors of Human Cholinesterases Targeting Their Midgorge Recognition Sites

  摘要：

  We describe herein the development of novel huperzine A-tacrine hybrids characterized by 3-methylbicyclo[3.3.1] non-3-ene scaffolds. These compounds were specifically designed to establish tight interactions, through different binding modes, with the midgorge recognition sites of human acetylcholinesterase (hAChE: Y72, D74) and human butyrylcholinesterase (hBuChE: N68, D70) and their catalytic or peripheral sites. Compounds 5a-c show a markedly improved biological profile relative to tacrine and huperzine A.

  DOI：

  10.1021/jm060257t