(+/-)-(9E)-9-ethylidene-3,6,6-trimethyl-7-oxobicyclo[3.3.1]non-3-ene-1-carboxylic acid | 888325-35-7

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: (+/-)-(9E)-9-ethylidene-3,6,6-trimethyl-7-oxobicyclo[3.3.1]non-3-ene-1-carboxylic acid
• CAS: 888325-35-7
• 化学式: C₁₅H₂₀O₃
• 分子量: 248.322
• InChiKey: FXKXSLDCTQWVHM-BJMVGYQFSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.97
• 重原子数：
  18.0
• 可旋转键数：
  1.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.6
• 拓扑面积：
  54.37
• 氢给体数：
  1.0
• 氢受体数：
  2.0

反应信息

• 作为反应物：
  描述：

  (+/-)-(9E)-9-ethylidene-3,6,6-trimethyl-7-oxobicyclo[3.3.1]non-3-ene-1-carboxylic acid 在 diphenyl azodiphosphate 、 三乙胺 作用下， 以 甲苯 为溶剂， 反应 25.0h， 生成 (+/-)-methyl (9E)-ethylidene-3,6,6-trimethyl-7-oxobicyclo[3.3.1]non-3-en-1-ylcarbamate
  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：

  (+/-)-(9Z/E)-9-ethylidene-3,6,6-trimethyl-7-oxobicyclo[3.3.1]non-3-ene-1-carboxylic acid methyl ester 在 sodium hydroxide 作用下， 以 四氢呋喃 、 甲醇 为溶剂， 反应 48.0h， 以180 mg的产率得到(+/-)-(9E)-9-ethylidene-3,6,6-trimethyl-7-oxobicyclo[3.3.1]non-3-ene-1-carboxylic acid
  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