(E)-3-(4-chlorophenyl)-1-(2-hydroxy-4-(3-methylbut-2-enyloxy)phenyl)prop-2-en-1-one | 1152162-34-9

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 直链 1,3-二芳基丙烷
• 英文名称: (E)-3-(4-chlorophenyl)-1-(2-hydroxy-4-(3-methylbut-2-enyloxy)phenyl)prop-2-en-1-one
• 英文别名: Substituted chalcone, 5e；(E)-3-(4-chlorophenyl)-1-[2-hydroxy-4-(3-methylbut-2-enoxy)phenyl]prop-2-en-1-one
• CAS: 1152162-34-9
• 化学式: C₂₀H₁₉ClO₃
• 分子量: 342.822
• InChiKey: HJVCKPFGGRPXTK-BJMVGYQFSA-N

物化性质

• 熔点：
  185 °C(Solvent: Methanol)
• 沸点：
  530.9±50.0 °C(predicted)
• 密度：
  1.208±0.06 g/cm3(Temp: 20 °C; Press: 760 Torr)(predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  6
• 重原子数：
  24
• 可旋转键数：
  6
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.15
• 拓扑面积：
  46.5
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  1-[2-羟基-4-(3-甲基-2-丁烯氧基)-苯基]-乙酮 、 4-氯苯甲醛 在 barium hydroxide octahydrate 作用下， 以 乙醇 为溶剂， 反应 24.0h， 以75%的产率得到(E)-3-(4-chlorophenyl)-1-(2-hydroxy-4-(3-methylbut-2-enyloxy)phenyl)prop-2-en-1-one
  参考文献：
  名称：

  Chalcones: A Valid Scaffold for Monoamine Oxidases Inhibitors

  摘要：

  A large series of substituted chalcones have been synthesized and tested in vitro for their ability to inhibit human monoamine oxidases A and B (hMAO-A and hMAO-B). While all the compounds showed hMAO-B selective activity in the micro- and nanomolar ranges, the best results were obtained in the presence of chlorine and hydroxyl or methoxyl substituents. To better understand the enzyme-inhibitor interaction and to explain the selectivity of the most active compounds toward hMAO-B, molecular modeling studies were carried out on new, high resolution, hMAO-B crystallographic structures. For the only compound that also showed activity against hMAO-A as well as low selectivity, the molecular modeling study was also performed on the hMAO-A crystallographic structure. The docking technique provided new insight on the inhibition mechanism and the rational drug design of more potent/selective hMAO inhibitors based on the chalcone scaffold.

  DOI：

  10.1021/jm801590u

文献信息

• Chalcones: A Valid Scaffold for Monoamine Oxidases Inhibitors
  作者：Franco Chimenti、Rossella Fioravanti、Adriana Bolasco、Paola Chimenti、Daniela Secci、Francesca Rossi、Matilde Yáñez、Francisco Orallo、Francesco Ortuso、Stefano Alcaro

  DOI：10.1021/jm801590u

  日期：2009.5.14

  A large series of substituted chalcones have been synthesized and tested in vitro for their ability to inhibit human monoamine oxidases A and B (hMAO-A and hMAO-B). While all the compounds showed hMAO-B selective activity in the micro- and nanomolar ranges, the best results were obtained in the presence of chlorine and hydroxyl or methoxyl substituents. To better understand the enzyme-inhibitor interaction and to explain the selectivity of the most active compounds toward hMAO-B, molecular modeling studies were carried out on new, high resolution, hMAO-B crystallographic structures. For the only compound that also showed activity against hMAO-A as well as low selectivity, the molecular modeling study was also performed on the hMAO-A crystallographic structure. The docking technique provided new insight on the inhibition mechanism and the rational drug design of more potent/selective hMAO inhibitors based on the chalcone scaffold.