3-[3-(Benzylmethylamino)propoxy]xanthen-9-one | 164934-29-6

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并吡喃
• 英文名称: 3-[3-(Benzylmethylamino)propoxy]xanthen-9-one
• 英文别名: 3-[3-[benzyl(methyl)amino]propoxy]xanthen-9-one
• CAS: 164934-29-6
• 化学式: C₂₄H₂₃NO₃
• 分子量: 373.452
• InChiKey: OTLLABLRJBVBHD-UHFFFAOYSA-N

物化性质

• 沸点：
  533.5±50.0 °C(Predicted)
• 密度：
  1.198±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  4.8
• 重原子数：
  28
• 可旋转键数：
  7
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.21
• 拓扑面积：
  38.8
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  3-[3-(Benzylmethylamino)propoxy]xanthen-9-one 在 palladium on activated charcoal 氢溴酸 、 氢气 、 三乙胺 作用下， 以 四氢呋喃 、 水 、 甲苯 为溶剂， 反应 27.0h， 生成 3-[N-methyl-N-(3-hydroxybenzyl)amino]propoxyxanthen-9-one
  参考文献：
  名称：

  Valentini, Piero; Rampa, Angela; Bisi, Alessandra, Medicinal Chemistry Research, 1995, vol. 5, # 4, p. 255 - 264

  摘要：

  DOI：
• 作为产物：
  描述：

  西伯尔链接剂 在 potassium carbonate 作用下， 以 丙酮 、 甲苯 为溶剂， 反应 44.0h， 生成 3-[3-(Benzylmethylamino)propoxy]xanthen-9-one
  参考文献：
  名称：

  Valentini, Piero; Rampa, Angela; Bisi, Alessandra, Medicinal Chemistry Research, 1995, vol. 5, # 4, p. 255 - 264

  摘要：

  DOI：

文献信息

• Cholinesterase inhibitors: SAR and enzyme inhibitory activity of 3-[ω-(benzylmethylamino)alkoxy]xanthen-9-ones
  作者：Lorna Piazzi、Federica Belluti、Alessandra Bisi、Silvia Gobbi、Stefano Rizzo、Manuela Bartolini、Vincenza Andrisano、Maurizio Recanatini、Angela Rampa

  DOI：10.1016/j.bmc.2006.09.026

  日期：2007.1.1

  In this work, we further investigated a previously introduced class of cholinesterase inhibitors. The removal of the carbarnic function from the lead compound xanthostigmine led to a reversible cholinesterase inhibitors 3. Some new 3-[omega-(benzylmethylamino)alkoxy]xanthen-9-one analogs were designed, synthesized, and evaluated for their inhibitory activity against both acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE). The length of the alkoxy chain of compound 3 was increased and different substituents were introduced. From the IC50 values, it clearly appears that the carbamic residue is crucial to obtain highly potent AChE inhibitors. On the other hand, peculiarity of these compounds is the high selectivity toward BuChE with respect to AChE, being compound 12 the most selective one (6000-fold). The development of selective BuChE inhibitors may be of great interest to clarify the physiological role of this enzyme and to provide novel therapeutics for various diseases. (c) 2006 Elsevier Ltd. All rights reserved.
• Valentini, Piero; Rampa, Angela; Bisi, Alessandra, Medicinal Chemistry Research, 1995, vol. 5, # 4, p. 255 - 264
  作者：Valentini, Piero、Rampa, Angela、Bisi, Alessandra、Fabbri, Giuseppina、Andrisano, Vincenza、Cavrini, Vanni

  DOI：——

  日期：——