N-(3-aminopropyl)-N-[3-(1,2,3,4-tetrahydroacridin-9-ylamino)propyl]acetamide | 1026920-27-3

• 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: N-(3-aminopropyl)-N-[3-(1,2,3,4-tetrahydroacridin-9-ylamino)propyl]acetamide
• CAS: 1026920-27-3
• 化学式: C₂₁H₃₀N₄O
• 分子量: 354.495
• InChiKey: GDLIFRVGCIDUBB-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.6
• 重原子数：
  26
• 可旋转键数：
  8
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.52
• 拓扑面积：
  71.2
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  9-氯-1,2,3,4-四氢吖啶 、 N-(3-aminopropyl)-N-[3-(1,2,3,4-tetrahydroacridin-9-ylamino)propyl]acetamide 在 三乙胺 作用下， 以 戊醇 为溶剂， 反应 10.0h， 生成 N,N-bis[3-(1,2,3,4-tetrahydroacridin-9-ylamino)propyl]acetamide
  参考文献：
  名称：

  Specific Targeting of Acetylcholinesterase and Butyrylcholinesterase Recognition Sites. Rational Design of Novel, Selective, and Highly Potent Cholinesterase Inhibitors

  摘要：

  Tacrine-based AChE and BuChE inhibitors were designed by investigating the topology of the active site gorge of the two enzymes. The homobivalent ligands characterized by a nitrogen-bridged atom at the tether level could be considered among the most potent and selective cholinesterase inhibitors described to date. The nitrogen-containing homobivalent ligands 3e,g and the sulfur-containing 3h validated the hypothesis of extra sites of interaction in the AChE and BuChE active site gorges.

  DOI：

  10.1021/jm0255668
• 作为产物：
  描述：

  3,3'-二氨基二丙基胺 在 氢氧化钾 、 TEA 、 三氟乙酸 作用下， 以 二氯甲烷 、 甲苯 为溶剂， 反应 15.0h， 生成 N-(3-aminopropyl)-N-[3-(1,2,3,4-tetrahydroacridin-9-ylamino)propyl]acetamide
  参考文献：
  名称：

  Specific Targeting of Acetylcholinesterase and Butyrylcholinesterase Recognition Sites. Rational Design of Novel, Selective, and Highly Potent Cholinesterase Inhibitors

  摘要：

  Tacrine-based AChE and BuChE inhibitors were designed by investigating the topology of the active site gorge of the two enzymes. The homobivalent ligands characterized by a nitrogen-bridged atom at the tether level could be considered among the most potent and selective cholinesterase inhibitors described to date. The nitrogen-containing homobivalent ligands 3e,g and the sulfur-containing 3h validated the hypothesis of extra sites of interaction in the AChE and BuChE active site gorges.

  DOI：

  10.1021/jm0255668

文献信息

• Specific Targeting of Acetylcholinesterase and Butyrylcholinesterase Recognition Sites. Rational Design of Novel, Selective, and Highly Potent Cholinesterase Inhibitors
  作者：Luisa Savini、Alessandra Gaeta、Caterina Fattorusso、Bruno Catalanotti、Giuseppe Campiani、Luisa Chiasserini、Cesare Pellerano、Ettore Novellino、Dawn McKissic、Ashima Saxena

  DOI：10.1021/jm0255668

  日期：2003.1.1

  Tacrine-based AChE and BuChE inhibitors were designed by investigating the topology of the active site gorge of the two enzymes. The homobivalent ligands characterized by a nitrogen-bridged atom at the tether level could be considered among the most potent and selective cholinesterase inhibitors described to date. The nitrogen-containing homobivalent ligands 3e,g and the sulfur-containing 3h validated the hypothesis of extra sites of interaction in the AChE and BuChE active site gorges.