N-benzyloxycarbonyl-6,7-dihydro-5H-benzocyclohepten-7-amine | 1394920-14-9

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 英文名称: N-benzyloxycarbonyl-6,7-dihydro-5H-benzocyclohepten-7-amine
• CAS: 1394920-14-9
• 化学式: C₁₉H₁₉NO₂
• 分子量: 293.365
• InChiKey: IZAFJXIGTOZXNO-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.94
• 重原子数：
  22.0
• 可旋转键数：
  3.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.21
• 拓扑面积：
  38.33
• 氢给体数：
  1.0
• 氢受体数：
  2.0

反应信息

• 作为反应物：
  描述：

  N-benzyloxycarbonyl-6,7-dihydro-5H-benzocyclohepten-7-amine 在 盐酸 、 copper(I) bromide dimethylsulfide complex 、 5%-palladium/activated carbon 、 氢气 、 重水 、 戴斯-马丁氧化剂 、 间氯过氧苯甲酸 作用下， 以 四氢呋喃 、 1,4-二氧六环 、 乙醚 、 二氯甲烷 、 水 为溶剂， 反应 68.75h， 生成 cis-5-(2-phenylethyl)-7-amino-5,7,8,9-tetrahydrobenzocyclohepten-6-one hydrochloride
  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
• 作为产物：
  描述：

  5,6-dehydrobenzocyclohepten-7-one 在 titanium(IV) isopropylate 、 sodium tetrahydroborate 、 氨 、 sodium carbonate 作用下， 以 四氢呋喃 、 乙醇 为溶剂， 反应 9.0h， 生成 N-benzyloxycarbonyl-6,7-dihydro-5H-benzocyclohepten-7-amine
  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