2-(10-(4-benzylpiperazin-1-yl)decyl)isoindoline-1,3-dione

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 异吲哚及其衍生物
• 英文名称: 2-(10-(4-benzylpiperazin-1-yl)decyl)isoindoline-1,3-dione
• 英文别名: 2-[10-(4-Benzylpiperazin-1-yl)decyl]isoindole-1,3-dione；2-[10-(4-benzylpiperazin-1-yl)decyl]isoindole-1,3-dione
• 化学式: C₂₉H₃₉N₃O₂
• 分子量: 461.648
• InChiKey: LDSMHKUMCZOLHV-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.8
• 重原子数：
  34
• 可旋转键数：
  13
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.52
• 拓扑面积：
  43.9
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  氯化苄 在 potassium carbonate 作用下， 以 四氢呋喃 、 N,N-二甲基甲酰胺 为溶剂， 反应 7.0h， 生成 2-(10-(4-benzylpiperazin-1-yl)decyl)isoindoline-1,3-dione
  参考文献：
  名称：

  Design, synthesis and bioactivity of novel phthalimide derivatives as acetylcholinesterase inhibitors

  摘要：

  A series of novel phthalimide derivatives related to benzylpiperazine were synthesized and evaluated as cholinesterase inhibitors. The results showed that all compounds were able to inhibit acetylcholinesterase (AChE), with two of them dramatically inhibiting butyrylcholinesterase (BuChE). Most compounds exhibited potent anti-AChE activity in the range of nM concentrations. In particular, compounds 7aIII and 10a showed the most potent activity with the IC50 values of 18.44 nM and 13.58 nM, respectively. To understand the excellent activity of these compounds, the structure-activity relationship was further examined. The protein-ligand docking study demonstrated that the target compounds have special binding modes and these results are in agreement with the kinetic study. (C) 2015 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2015.07.052

文献信息

• Design, synthesis and bioactivity of novel phthalimide derivatives as acetylcholinesterase inhibitors
  作者：Weijie Si、Tao Zhang、Lanxiang Zhang、Xiangdong Mei、Mengya Dong、Kaixin Zhang、Jun Ning

  DOI：10.1016/j.bmcl.2015.07.052

  日期：2016.5

  A series of novel phthalimide derivatives related to benzylpiperazine were synthesized and evaluated as cholinesterase inhibitors. The results showed that all compounds were able to inhibit acetylcholinesterase (AChE), with two of them dramatically inhibiting butyrylcholinesterase (BuChE). Most compounds exhibited potent anti-AChE activity in the range of nM concentrations. In particular, compounds 7aIII and 10a showed the most potent activity with the IC50 values of 18.44 nM and 13.58 nM, respectively. To understand the excellent activity of these compounds, the structure-activity relationship was further examined. The protein-ligand docking study demonstrated that the target compounds have special binding modes and these results are in agreement with the kinetic study. (C) 2015 Elsevier Ltd. All rights reserved.