3,4-Dimethyl-7-(2-oxo-2-phenyl-ethoxy)-chromen-2-one | 314742-04-6

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 3,4-Dimethyl-7-(2-oxo-2-phenyl-ethoxy)-chromen-2-one
• 英文别名: 3,4-dimethyl-7-(2-oxo-2-phenylethoxy)-2H-chromen-2-one；3,4-dimethyl-7-phenacyloxychromen-2-one
• CAS: 314742-04-6
• 化学式: C₁₉H₁₆O₄
• mdl: MFCD01878223
• 分子量: 308.334
• InChiKey: PNPQCIMJHQSKSZ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.6
• 重原子数：
  23
• 可旋转键数：
  4
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.16
• 拓扑面积：
  52.6
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  3,4-Dimethyl-7-(2-oxo-2-phenyl-ethoxy)-chromen-2-one 在 lithium aluminium tetrahydride 作用下， 以 四氢呋喃 为溶剂， 反应 2.0h， 生成 7-(2-Hydroxy-2-phenyl-ethoxy)-3,4-dimethyl-chromen-2-one
  参考文献：
  名称：

  Structural Insights into Monoamine Oxidase Inhibitory Potency and Selectivity of 7-Substituted Coumarins from Ligand- and Target-Based Approaches

  摘要：

  A new series of 3-, 4-, 7-polysubstituted coumarins have been designed and evaluated for their monoamine oxidase A and monoamine oxidase B (MAO-A and MAO-B) inhibitory potency. Substituents at position 7 consisted of a bridge of different physicochemical nature linking a phenyl ring to the coumarin scaffold. Structure-affinity and structure-selectivity relationships, derived through CoMFA-GOLPE and docking studies, revealed the key physicochemical interactions responsible for the observed MAO-B and MAO-A inhibitory potency and suggested the main structural determinants for high selectivity toward one of the two enzymatic isoforms. The predictive power of our models was proved with the design of a new inhibitor demonstrating an outstanding MAO-B affinity (pIC(50) = 8.29) and the highest MAO-B selectivity (Delta pIC(50) = 3.39) within the entire series of ligands examined herein.

  DOI：

  10.1021/jm060183l
• 作为产物：
  描述：

  二甲基伞形酮 、 2-溴苯乙酮 在 potassium carbonate 作用下， 反应 3.0h， 以51%的产率得到3,4-Dimethyl-7-(2-oxo-2-phenyl-ethoxy)-chromen-2-one
  参考文献：
  名称：

  Human recombinant monoamine oxidase B as reliable and efficient enzyme source for inhibitor screening

  摘要：

  Interest in inhibitors of monoamine oxidase type B (MAO B) has grown in recent years, due to their therapeutic potential in aging-related neurodegenerative diseases, such as Parkinson's disease and Alzheimer's disease. This study is devoted to the use of human recombinant MAO B obtained from a Baculovirus expression system (Supersomes (TM) MAO B, BD Gentest, MA, USA) as reliable and efficient enzyme source for MAO B inhibitor screening. Comparison of inhibition potencies (pIC(50) values) determined with human cloned and human platelet MAO B for the two series of MAO B inhibitors, coumarin and 5H-indeno[1,2-c]pyridazin-5-one derivatives, showed that the difference between pIC(50) values obtained with the two enzyme sources was not significant (P > 0.05, Student's t-test). Hence, recombinant enzyme is validated as convenient enzyme source for MAO B inhibitor screening. (c) 2005 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2005.06.043

文献信息

• Structural Insights into Monoamine Oxidase Inhibitory Potency and Selectivity of 7-Substituted Coumarins from Ligand- and Target-Based Approaches
  作者：Marco Catto、Orazio Nicolotti、Francesco Leonetti、Andrea Carotti、Angelo Danilo Favia、Ramón Soto-Otero、Estefanía Méndez-Álvarez、Angelo Carotti

  DOI：10.1021/jm060183l

  日期：2006.8.1

  A new series of 3-, 4-, 7-polysubstituted coumarins have been designed and evaluated for their monoamine oxidase A and monoamine oxidase B (MAO-A and MAO-B) inhibitory potency. Substituents at position 7 consisted of a bridge of different physicochemical nature linking a phenyl ring to the coumarin scaffold. Structure-affinity and structure-selectivity relationships, derived through CoMFA-GOLPE and docking studies, revealed the key physicochemical interactions responsible for the observed MAO-B and MAO-A inhibitory potency and suggested the main structural determinants for high selectivity toward one of the two enzymatic isoforms. The predictive power of our models was proved with the design of a new inhibitor demonstrating an outstanding MAO-B affinity (pIC(50) = 8.29) and the highest MAO-B selectivity (Delta pIC(50) = 3.39) within the entire series of ligands examined herein.
• Human recombinant monoamine oxidase B as reliable and efficient enzyme source for inhibitor screening
  作者：Laura Novaroli、Marianne Reist、Elisabeth Favre、Angelo Carotti、Marco Catto、Pierre-Alain Carrupt

  DOI：10.1016/j.bmc.2005.06.043

  日期：2005.11

  Interest in inhibitors of monoamine oxidase type B (MAO B) has grown in recent years, due to their therapeutic potential in aging-related neurodegenerative diseases, such as Parkinson's disease and Alzheimer's disease. This study is devoted to the use of human recombinant MAO B obtained from a Baculovirus expression system (Supersomes (TM) MAO B, BD Gentest, MA, USA) as reliable and efficient enzyme source for MAO B inhibitor screening. Comparison of inhibition potencies (pIC(50) values) determined with human cloned and human platelet MAO B for the two series of MAO B inhibitors, coumarin and 5H-indeno[1,2-c]pyridazin-5-one derivatives, showed that the difference between pIC(50) values obtained with the two enzyme sources was not significant (P > 0.05, Student's t-test). Hence, recombinant enzyme is validated as convenient enzyme source for MAO B inhibitor screening. (c) 2005 Elsevier Ltd. All rights reserved.