7-amino 5-benzylidene-5,7,8,9-tetrahydrobenzocyclohepten-6-one | 1023619-82-0

• 分子结构分类: 有机化合物 - 有机氮化合物
• 英文名称: 7-amino 5-benzylidene-5,7,8,9-tetrahydrobenzocyclohepten-6-one
• 英文别名: 7-amino-5-benzylidene-8,9-dihydro-7H-benzo[7]annulen-6-one
• CAS: 1023619-82-0
• 化学式: C₁₈H₁₇NO
• 分子量: 263.339
• InChiKey: LLPUGHKEWRHKIU-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.3
• 重原子数：
  20
• 可旋转键数：
  1
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.17
• 拓扑面积：
  43.1
• 氢给体数：
  1
• 氢受体数：
  2

反应信息

• 作为产物：
  描述：

  7-(tert-butyloxycarbonylamino)-5,7,8,9-tetrahydro-benzocyclohepten-6-one 在 盐酸 、 5%-palladium/activated carbon 、 氢气 、 lithium hexamethyldisilazane 作用下， 以 四氢呋喃 、 1,4-二氧六环 、 六甲基磷酰三胺 、 水 为溶剂， 反应 27.83h， 生成 7-amino 5-benzylidene-5,7,8,9-tetrahydrobenzocyclohepten-6-one
  参考文献：
  名称：

  Rapid and efficient synthesis of a novel series of substituted aminobenzosuberone derivatives as potent, selective, non-peptidic neutral aminopeptidase inhibitors

  摘要：

  Racemic 5-substituted 7-aminobenzocyclohepten-6-one were synthesized and evaluated for their ability to inhibit metalloaminopeptidase activities. Unexpectedly, 5-thio substituted compounds showed enhanced inhibition potency with K-i values in the nanomolar range against the 'one zinc' aminopeptidases from the M1 family, while most of them were rather poor inhibitors of the 'two zincs' enzymes from the M17 family. This interesting selectivity profile may guide the design of new, specific inhibitors of target mammalian aminopeptidases with one active site zinc. (C) 2012 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2012.06.041

文献信息

• Rapid and efficient synthesis of a novel series of substituted aminobenzosuberone derivatives as potent, selective, non-peptidic neutral aminopeptidase inhibitors
  作者：Sébastien Albrecht、Emmanuel Salomon、Albert Defoin、Céline Tarnus

  DOI：10.1016/j.bmc.2012.06.041

  日期：2012.8

  Racemic 5-substituted 7-aminobenzocyclohepten-6-one were synthesized and evaluated for their ability to inhibit metalloaminopeptidase activities. Unexpectedly, 5-thio substituted compounds showed enhanced inhibition potency with K-i values in the nanomolar range against the 'one zinc' aminopeptidases from the M1 family, while most of them were rather poor inhibitors of the 'two zincs' enzymes from the M17 family. This interesting selectivity profile may guide the design of new, specific inhibitors of target mammalian aminopeptidases with one active site zinc. (C) 2012 Elsevier Ltd. All rights reserved.