1-硝基-3-[4-(3-硝基苯氧基)丁氧基]苯 | 14467-66-4

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 中文名称: 1-硝基-3-[4-(3-硝基苯氧基)丁氧基]苯
• 英文名称: 1,4-bis(3-nitrophenoxy)butane
• 英文别名: 1-Nitro-3-[4-(3-nitrophenoxy)butoxy]benzene
• CAS: 14467-66-4
• 化学式: C₁₆H₁₆N₂O₆
• 分子量: 332.313
• InChiKey: QPRWHRQOHBUZMI-UHFFFAOYSA-N

物化性质

• 熔点：
  133 °C
• 沸点：
  523.2±35.0 °C(Predicted)
• 密度：
  1.303±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.9
• 重原子数：
  24
• 可旋转键数：
  7
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.25
• 拓扑面积：
  110
• 氢给体数：
  0
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  1-硝基-3-[4-(3-硝基苯氧基)丁氧基]苯 在 钯 氢气 作用下， 以 1,4-二氧六环 、 乙醇 为溶剂， 20.0 ℃ 、400.01 kPa 条件下， 反应 7.0h， 以91%的产率得到3,3'-(butane-1,4-diyldioxy)bisaniline
  参考文献：
  名称：

  Homo- and hetero-bivalent edrophonium-like ammonium salts as highly potent, dual binding site AChE inhibitors

  摘要：

  A number of mono- and bis-quaternary ammonium salts, containing edrophonium-like and coumarin moieties tethered by an appropriate linker, proved to be highly potent and selective dual binding site acetylcholinesterase inhibitors with good selectivity over butyrylcholinesterase. Homobivalent bis-quaternary inhibitors 11 and 12, differing by only one methylene unit in the linker, were the most potent and selective inhibitors exhibiting a sub-nanomolar affinity (IC50 = 0.49 and 0.17 nM, respectively) and a high butyryl-/acetylcholinesterase affinity ratio (SI = 1465 and 4165, respectively). The corresponding hetero-bivalent coumarinic inhibitors 13 and 14 were also endowed with excellent inhibitory potency but a lower AChE selectivity (IC50 = 2.1 and 1.0 nM, and SI = 505 and 708, respectively). Docking simulations enabled clear interpretation of the structure-affinity relationships and detection of key binding interactions at the primary and peripheral AChE binding sites. (C) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2008.06.022
• 作为产物：
  描述：

  1,4-二溴丁烷 、 间硝基苯酚 在 potassium carbonate 作用下， 以 乙腈 为溶剂， 反应 24.0h， 以87%的产率得到1-硝基-3-[4-(3-硝基苯氧基)丁氧基]苯
  参考文献：
  名称：

  Homo- and hetero-bivalent edrophonium-like ammonium salts as highly potent, dual binding site AChE inhibitors

  摘要：

  A number of mono- and bis-quaternary ammonium salts, containing edrophonium-like and coumarin moieties tethered by an appropriate linker, proved to be highly potent and selective dual binding site acetylcholinesterase inhibitors with good selectivity over butyrylcholinesterase. Homobivalent bis-quaternary inhibitors 11 and 12, differing by only one methylene unit in the linker, were the most potent and selective inhibitors exhibiting a sub-nanomolar affinity (IC50 = 0.49 and 0.17 nM, respectively) and a high butyryl-/acetylcholinesterase affinity ratio (SI = 1465 and 4165, respectively). The corresponding hetero-bivalent coumarinic inhibitors 13 and 14 were also endowed with excellent inhibitory potency but a lower AChE selectivity (IC50 = 2.1 and 1.0 nM, and SI = 505 and 708, respectively). Docking simulations enabled clear interpretation of the structure-affinity relationships and detection of key binding interactions at the primary and peripheral AChE binding sites. (C) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2008.06.022

文献信息

• Baliah, V.; Aparajithan, K., Journal of the Indian Chemical Society, 1992, vol. 69, # 5, p. 255 - 259
  作者：Baliah, V.、Aparajithan, K.

  DOI：——

  日期：——
• GB1020306
  申请人：——

  公开号：——

  公开（公告）日：——
• Homo- and hetero-bivalent edrophonium-like ammonium salts as highly potent, dual binding site AChE inhibitors
  作者：Francesco Leonetti、Marco Catto、Orazio Nicolotti、Leonardo Pisani、Anna Cappa、Angela Stefanachi、Angelo Carotti

  DOI：10.1016/j.bmc.2008.06.022

  日期：2008.8

  A number of mono- and bis-quaternary ammonium salts, containing edrophonium-like and coumarin moieties tethered by an appropriate linker, proved to be highly potent and selective dual binding site acetylcholinesterase inhibitors with good selectivity over butyrylcholinesterase. Homobivalent bis-quaternary inhibitors 11 and 12, differing by only one methylene unit in the linker, were the most potent and selective inhibitors exhibiting a sub-nanomolar affinity (IC50 = 0.49 and 0.17 nM, respectively) and a high butyryl-/acetylcholinesterase affinity ratio (SI = 1465 and 4165, respectively). The corresponding hetero-bivalent coumarinic inhibitors 13 and 14 were also endowed with excellent inhibitory potency but a lower AChE selectivity (IC50 = 2.1 and 1.0 nM, and SI = 505 and 708, respectively). Docking simulations enabled clear interpretation of the structure-affinity relationships and detection of key binding interactions at the primary and peripheral AChE binding sites. (C) 2008 Elsevier Ltd. All rights reserved.