3-[4-(bromomethyl)phenyl]-6,7-dimethoxy-2H-2-chromenone | 949580-70-5

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 异黄酮类化合物
• 英文名称: 3-[4-(bromomethyl)phenyl]-6,7-dimethoxy-2H-2-chromenone
• 英文别名: 3-(4-bromomethylphenyl)-6,7-dimethoxychromen-2-one；3-[4-(Bromomethyl)phenyl]-6,7-dimethoxychromen-2-one
• CAS: 949580-70-5
• 化学式: C₁₈H₁₅BrO₄
• 分子量: 375.219
• InChiKey: OURWZQBDKZKAIS-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4
• 重原子数：
  23
• 可旋转键数：
  4
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.17
• 拓扑面积：
  44.8
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  N-乙基苄胺 、 3-[4-(bromomethyl)phenyl]-6,7-dimethoxy-2H-2-chromenone 以 甲苯 为溶剂， 反应 15.0h， 以38%的产率得到AP 2243
  参考文献：
  名称：

  Extensive SAR and Computational Studies of 3-{4-[(Benzylmethylamino)methyl]phenyl}-6,7-dimethoxy-2H-2-chromenone (AP2238) Derivatives

  摘要：

  AP2238 was the first compound published to bind both anionic sites of the human acetylcholinesterase, allowing the simultaneous inhibition of the catalytic and the amyloid-beta pro-aggregating activities of AChE. Here we attempted to derive a comprehensive structure-activity relationship picture for this molecule, affording 28 derivatives for which AChE and BChE inhibitory activities were evaluated. Selected compounds were also tested for their ability to prevent the AChE-induced A beta-aggregation. Moreover, docking simulations and molecular orbital calculations were performed.

  DOI：

  10.1021/jm070100g
• 作为产物：
  描述：

  2,4,5-三甲氧基苯甲醛 在 N-溴代丁二酰亚胺(NBS) 、 乙酸酐 、 三氯化硼 、 过氧化苯甲酰 作用下， 以 四氯化碳 、 二氯甲烷 为溶剂， 生成 3-[4-(bromomethyl)phenyl]-6,7-dimethoxy-2H-2-chromenone
  参考文献：
  名称：

  3-(4-{[Benzyl(methyl)amino]methyl}phenyl)-6,7-dimethoxy-2H-2-chromenone (AP2238) Inhibits Both Acetylcholinesterase and Acetylcholinesterase-Induced β-Amyloid Aggregation:  A Dual Function Lead for Alzheimer's Disease Therapy

  摘要：

  In recent years, the investigation of acetylcholinesterase (AChE) inhibitors has gained further interest, because the involvement of the peripheral site of the enzyme in the beta-amyloid (Abeta) aggregation process has been disclosed. We present here, for the first time, a direct evidence of the Abeta antiaggregating action of an AChE inhibitor (AP2238) purposely designed to bind at both the catalytic and the peripheral sites of the human enzyme.

  DOI：

  10.1021/jm0340602

文献信息

• Extensive SAR and Computational Studies of 3-{4-[(Benzylmethylamino)methyl]phenyl}-6,7-dimethoxy-2<i>H</i>-2-chromenone (AP2238) Derivatives
  作者：Lorna Piazzi、Andrea Cavalli、Federica Belluti、Alessandra Bisi、Silvia Gobbi、Stefano Rizzo、Manuela Bartolini、Vincenza Andrisano、Maurizio Recanatini、Angela Rampa

  DOI：10.1021/jm070100g

  日期：2007.8.1

  AP2238 was the first compound published to bind both anionic sites of the human acetylcholinesterase, allowing the simultaneous inhibition of the catalytic and the amyloid-beta pro-aggregating activities of AChE. Here we attempted to derive a comprehensive structure-activity relationship picture for this molecule, affording 28 derivatives for which AChE and BChE inhibitory activities were evaluated. Selected compounds were also tested for their ability to prevent the AChE-induced A beta-aggregation. Moreover, docking simulations and molecular orbital calculations were performed.
• 3-(4-{[Benzyl(methyl)amino]methyl}phenyl)-6,7-dimethoxy-2<i>H</i>-2-chromenone (AP2238) Inhibits Both Acetylcholinesterase and Acetylcholinesterase-Induced β-Amyloid Aggregation:  A Dual Function Lead for Alzheimer's Disease Therapy
  作者：Lorna Piazzi、Angela Rampa、Alessandra Bisi、Silvia Gobbi、Federica Belluti、Andrea Cavalli、Manuela Bartolini、Vincenza Andrisano、Piero Valenti、Maurizio Recanatini

  DOI：10.1021/jm0340602

  日期：2003.6.1

  In recent years, the investigation of acetylcholinesterase (AChE) inhibitors has gained further interest, because the involvement of the peripheral site of the enzyme in the beta-amyloid (Abeta) aggregation process has been disclosed. We present here, for the first time, a direct evidence of the Abeta antiaggregating action of an AChE inhibitor (AP2238) purposely designed to bind at both the catalytic and the peripheral sites of the human enzyme.