[(8bS)-4-benzyl-3,8b-dimethyl-2,3a-dihydro-1H-pyrrolo[2,3-b]indol-7-yl] N-(4-propan-2-ylphenyl)carbamate | 912960-23-7

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吲哚及其衍生物
• 英文名称: [(8bS)-4-benzyl-3,8b-dimethyl-2,3a-dihydro-1H-pyrrolo[2,3-b]indol-7-yl] N-(4-propan-2-ylphenyl)carbamate
• CAS: 912960-23-7
• 化学式: C₂₉H₃₃N₃O₂
• 分子量: 455.6
• InChiKey: BNHHOLFSTKWHNP-ACEFPKFPSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.9
• 重原子数：
  34
• 可旋转键数：
  6
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.34
• 拓扑面积：
  44.8
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  [(8bS)-4-benzyl-3,8b-dimethyl-2,3a-dihydro-1H-pyrrolo[2,3-b]indol-7-yl] N-(4-propan-2-ylphenyl)carbamate 在 palladium dihydroxide 氢气 、 三氟乙酸 作用下， 以 甲醇 、 水 为溶剂， 反应 1.0h， 以65.7%的产率得到[(8bS)-3,8b-dimethyl-1,2,3a,4-tetrahydropyrrolo[2,3-b]indol-7-yl] N-(4-propan-2-ylphenyl)carbamate
  参考文献：
  名称：

  Synthesis of Novel Phenserine-Based-Selective Inhibitors of Butyrylcholinesterase for Alzheimer's Disease

  摘要：

  Four novel analogues (8-11) of cymserine (2) were synthesized by methods similar to those recently developed for the total syntheses of N-8-norphenserine (Yu, Q. S.; et al. J. Med. Chem. 1997, 40, 2895-2901) and N-1,N-8-bisnorphenserine (Yu, Q. S.; et al. J. Med. Chem. 1998, 41, 2371-2379). As our structure-activity studies predicted, these compounds are highly potent and selective inhibitors of human butyryleholinesterase (BChE) and will test the novel hypothesis that BChE inhibitors are useful in the treatment of Alzheimer's disease. In a similar manner, the same modifications that provided BChE selectivity were applied to the acetylcholinesterase (AChE)-selective inhibitor, tolserine (5), to provide the novel tolserine analogues 12-15. As predicted, these modifications altered the AChE-selective action of tolserine (5) to favor a lack of cholinesterase enzyme subtype selectivity.

  DOI：

  10.1021/jm980459s
• 作为产物：
  描述：

  (3aS)-N⁸-benzylnoresermethole 在 sodium 、 三溴化硼 作用下， 以 二氯甲烷 为溶剂， 反应 0.1h， 生成 [(8bS)-4-benzyl-3,8b-dimethyl-2,3a-dihydro-1H-pyrrolo[2,3-b]indol-7-yl] N-(4-propan-2-ylphenyl)carbamate
  参考文献：
  名称：

  Synthesis of Novel Phenserine-Based-Selective Inhibitors of Butyrylcholinesterase for Alzheimer's Disease

  摘要：

  Four novel analogues (8-11) of cymserine (2) were synthesized by methods similar to those recently developed for the total syntheses of N-8-norphenserine (Yu, Q. S.; et al. J. Med. Chem. 1997, 40, 2895-2901) and N-1,N-8-bisnorphenserine (Yu, Q. S.; et al. J. Med. Chem. 1998, 41, 2371-2379). As our structure-activity studies predicted, these compounds are highly potent and selective inhibitors of human butyryleholinesterase (BChE) and will test the novel hypothesis that BChE inhibitors are useful in the treatment of Alzheimer's disease. In a similar manner, the same modifications that provided BChE selectivity were applied to the acetylcholinesterase (AChE)-selective inhibitor, tolserine (5), to provide the novel tolserine analogues 12-15. As predicted, these modifications altered the AChE-selective action of tolserine (5) to favor a lack of cholinesterase enzyme subtype selectivity.

  DOI：

  10.1021/jm980459s

文献信息

• Synthesis of Novel Phenserine-Based-Selective Inhibitors of Butyrylcholinesterase for Alzheimer's Disease
  作者：Qian-sheng Yu、Harold W. Holloway、Tadanobu Utsuki、Arnold Brossi、Nigel H. Greig

  DOI：10.1021/jm980459s

  日期：1999.5.1

  Four novel analogues (8-11) of cymserine (2) were synthesized by methods similar to those recently developed for the total syntheses of N-8-norphenserine (Yu, Q. S.; et al. J. Med. Chem. 1997, 40, 2895-2901) and N-1,N-8-bisnorphenserine (Yu, Q. S.; et al. J. Med. Chem. 1998, 41, 2371-2379). As our structure-activity studies predicted, these compounds are highly potent and selective inhibitors of human butyryleholinesterase (BChE) and will test the novel hypothesis that BChE inhibitors are useful in the treatment of Alzheimer's disease. In a similar manner, the same modifications that provided BChE selectivity were applied to the acetylcholinesterase (AChE)-selective inhibitor, tolserine (5), to provide the novel tolserine analogues 12-15. As predicted, these modifications altered the AChE-selective action of tolserine (5) to favor a lack of cholinesterase enzyme subtype selectivity.