3-(3-benzyl-2,4-dioxoquinazolin-1-yl)-N-methylbenzamide | 114934-49-5

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 二氮杂萘
• 英文名称: 3-(3-benzyl-2,4-dioxoquinazolin-1-yl)-N-methylbenzamide
• CAS: 114934-49-5
• 化学式: C₂₃H₁₉N₃O₃
• 分子量: 385.422
• InChiKey: RTRBVEMNVFXHFI-UHFFFAOYSA-N

物化性质

• 熔点：
  250-251 °C
• 密度：
  1.309±0.06 g/cm3(Temp: 20 °C; Press: 760 Torr)(predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.1
• 重原子数：
  29
• 可旋转键数：
  4
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.09
• 拓扑面积：
  69.7
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  间氨基苯甲酸 在 盐酸 、 camphor-10-sulfonic acid 、 铜 、 potassium carbonate 、 copper(I) bromide 、 lithium iodide 作用下， 以 N,N-二甲基甲酰胺 、 xylene 为溶剂， 反应 223.5h， 生成 3-(3-benzyl-2,4-dioxoquinazolin-1-yl)-N-methylbenzamide
  参考文献：
  名称：

  Structure-activity relationship of quinazolinedione inhibitors of calcium-independent phosphodiesterase

  摘要：

  A series of quinazolinediones and azaquinazolinediones is described which possess potent inhibitory activity toward the calcium-independent phosphodiesterase enzyme (CaIPDE). In vivo testing showed that this in vitro activity translates to animal models predictive of chronic diseases such as depression and inflammation. These results support the hypothesis that inhibition of CaIPDE may lead to useful activity in such chronic diseases.

  DOI：

  10.1021/jm00106a024

文献信息

• LOWE, JOHN ADAMS (III)
  作者：LOWE, JOHN ADAMS (III)

  DOI：——

  日期：——
• LOWE, J. A.
  作者：LOWE, J. A.

  DOI：——

  日期：——
• Structure-activity relationship of quinazolinedione inhibitors of calcium-independent phosphodiesterase
  作者：John A. Lowe、Robert L. Archer、Douglas S. Chapin、John B. Cheng、David Helweg、Jonathan L. Johnson、B. Kenneth Koe、Lorraine A. Lebel、Peter F. Moore

  DOI：10.1021/jm00106a024

  日期：1991.2

  A series of quinazolinediones and azaquinazolinediones is described which possess potent inhibitory activity toward the calcium-independent phosphodiesterase enzyme (CaIPDE). In vivo testing showed that this in vitro activity translates to animal models predictive of chronic diseases such as depression and inflammation. These results support the hypothesis that inhibition of CaIPDE may lead to useful activity in such chronic diseases.