N-(6,8-dichloro-1,2,3,4-tetrahydroacridin-9-yl)heptane-1,7-diamine | 365533-86-4

• 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-(6,8-dichloro-1,2,3,4-tetrahydroacridin-9-yl)heptane-1,7-diamine
• 英文别名: N1-(6,8-dichloro-1,2,3,4-tetrahydro-acridin-9-yl)-heptane-1,7-diamine；N'-(6,8-dichloro-1,2,3,4-tetrahydroacridin-9-yl)heptane-1,7-diamine
• CAS: 365533-86-4
• 化学式: C₂₀H₂₇Cl₂N₃
• 分子量: 380.36
• InChiKey: NMOOUWOMLATGHW-UHFFFAOYSA-N

物化性质

• 沸点：
  561.6±50.0 °C(Predicted)
• 密度：
  1.228±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  5.7
• 重原子数：
  25
• 可旋转键数：
  8
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.55
• 拓扑面积：
  50.9
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  6,8,9-trichloro-1,2,3,4-tetrahydroacridine 、 N-(6,8-dichloro-1,2,3,4-tetrahydroacridin-9-yl)heptane-1,7-diamine 以 戊醇 为溶剂， 生成 6,8-dichloro-N-{7-[(6,8-dichloro-1,2,3,4-tetrahydroacridin-9-yl)amino]heptyl}-1,2,3,4-tetrahydroacridin-9-amine
  参考文献：
  名称：

  Novel and potent tacrine-related hetero- and homobivalent ligands for acetylcholinesterase and butyrylcholinesterase

  摘要：

  Based upon synthetic and biochemical results, a novel and potent tacrine analogue and heterobivalent analogues of tacrine, were designed. The role played by the amino groups of homo- and heterobivalent ligands in the interaction with the peripheral and catalytic sites of AChE and BuChE were investigated. The syntheses of these materials together with the results of AChE/BuChE inhibition assays are detailed. (C) 2001 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(01)00294-3
• 作为产物：
  描述：

  ethyl 2-oxocyclohexanecarboxilate 在 三氯氧磷 作用下， 以 二苯醚 、 戊醇 为溶剂， 反应 19.17h， 生成 N-(6,8-dichloro-1,2,3,4-tetrahydroacridin-9-yl)heptane-1,7-diamine
  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