4-(2-(1-benzylpiperidin-4-ylamino)-2-oxoethyl)-phenyl butylcarbamate | 1261287-17-5

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 哌啶类
• 英文名称: 4-(2-(1-benzylpiperidin-4-ylamino)-2-oxoethyl)-phenyl butylcarbamate
• 英文别名: [4-[2-[(1-benzylpiperidin-4-yl)amino]-2-oxoethyl]phenyl] N-butylcarbamate
• CAS: 1261287-17-5
• 化学式: C₂₅H₃₃N₃O₃
• 分子量: 423.555
• InChiKey: SVXXZBLSJBBBKW-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.1
• 重原子数：
  31
• 可旋转键数：
  10
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.44
• 拓扑面积：
  70.7
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  4-(2-(1-benzylpiperidin-4-ylamino)-2-oxoethyl)-phenyl butylcarbamate 在 盐酸 作用下， 以 乙醇 为溶剂， 生成 4-(2-(1-benzylpiperidin-4-ylamino)-2-oxoethyl)-phenyl butylcarbamate hydrochloride
  参考文献：
  名称：

  Novel alkyl- and arylcarbamate derivatives with N-benzylpiperidine and N-benzylpiperazine moieties as cholinesterases inhibitors

  摘要：

  The study presents synthesis and biological activity of novel alkyl- and arylcarbamate derivatives with N-benzylpiperidine and N-benzylpiperazine moieties designed as cholinesterases inhibitors. These fragments turned out to determine compounds' selectivity between AChE and BuChE. Derivatives of N-benzylpiperazine (16-25) were selective BuChE inhibitors with 3-(2-(4-benzylpiperazin-1-yl)-2-oxoethyl)-phenyl butylcarbamate (22) being the most potent compound (pIC(50) = 5.00) while a series of carbamate derivatives of N-benzylpiperidine (5-14) displayed non-selective BuChE/AChE inhibitory activity. Molecular modelling studies point out significant differences between orientations of these two groups of compounds in the active site of AChE, which can be an explanation of their different biological activity. (C) 2010 Elsevier Masson SAS. All rights reserved.

  DOI：

  10.1016/j.ejmech.2010.09.010
• 作为产物：
  描述：

  异氰酸正丁酯 、 N-(1-benzylpiperidin-4-yl)-2-(4-hydroxyphenyl)-acetamide 在 三乙胺 作用下， 以 二氯甲烷 为溶剂， 以83%的产率得到4-(2-(1-benzylpiperidin-4-ylamino)-2-oxoethyl)-phenyl butylcarbamate
  参考文献：
  名称：

  Novel alkyl- and arylcarbamate derivatives with N-benzylpiperidine and N-benzylpiperazine moieties as cholinesterases inhibitors

  摘要：

  The study presents synthesis and biological activity of novel alkyl- and arylcarbamate derivatives with N-benzylpiperidine and N-benzylpiperazine moieties designed as cholinesterases inhibitors. These fragments turned out to determine compounds' selectivity between AChE and BuChE. Derivatives of N-benzylpiperazine (16-25) were selective BuChE inhibitors with 3-(2-(4-benzylpiperazin-1-yl)-2-oxoethyl)-phenyl butylcarbamate (22) being the most potent compound (pIC(50) = 5.00) while a series of carbamate derivatives of N-benzylpiperidine (5-14) displayed non-selective BuChE/AChE inhibitory activity. Molecular modelling studies point out significant differences between orientations of these two groups of compounds in the active site of AChE, which can be an explanation of their different biological activity. (C) 2010 Elsevier Masson SAS. All rights reserved.

  DOI：

  10.1016/j.ejmech.2010.09.010

文献信息

• Novel alkyl- and arylcarbamate derivatives with N-benzylpiperidine and N-benzylpiperazine moieties as cholinesterases inhibitors
  作者：Anna Więckowska、Marek Bajda、Natalia Guzior、Barbara Malawska

  DOI：10.1016/j.ejmech.2010.09.010

  日期：2010.12

  The study presents synthesis and biological activity of novel alkyl- and arylcarbamate derivatives with N-benzylpiperidine and N-benzylpiperazine moieties designed as cholinesterases inhibitors. These fragments turned out to determine compounds' selectivity between AChE and BuChE. Derivatives of N-benzylpiperazine (16-25) were selective BuChE inhibitors with 3-(2-(4-benzylpiperazin-1-yl)-2-oxoethyl)-phenyl butylcarbamate (22) being the most potent compound (pIC(50) = 5.00) while a series of carbamate derivatives of N-benzylpiperidine (5-14) displayed non-selective BuChE/AChE inhibitory activity. Molecular modelling studies point out significant differences between orientations of these two groups of compounds in the active site of AChE, which can be an explanation of their different biological activity. (C) 2010 Elsevier Masson SAS. All rights reserved.