2-(4-fluorophenyl)-3-(pyridin-4-yl)furan | 1143460-60-9

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: 2-(4-fluorophenyl)-3-(pyridin-4-yl)furan
• 英文别名: 4-[2-(4-fluorophenyl)furan-3-yl]pyridine
• CAS: 1143460-60-9
• 化学式: C₁₅H₁₀FNO
• 分子量: 239.249
• InChiKey: SOYRTOOOBWIXML-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.3
• 重原子数：
  18
• 可旋转键数：
  2
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  26
• 氢给体数：
  0
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  4-(4-fluorophenyl)-4-oxo-3-(pyridin-4-yl)butanal 在 盐酸 作用下， 以 溶剂黄146 为溶剂， 反应 4.0h， 以1.15 g的产率得到2-(4-fluorophenyl)-3-(pyridin-4-yl)furan
  参考文献：
  名称：

  Role of the Hydrogen Bonding Heteroatom−Lys53 Interaction between the p38α Mitogen-Activated Protein (MAP) Kinase and Pyridinyl-Substituted 5-Membered Heterocyclic Ring Inhibitors

  摘要：

  In the framework of Investigating the role of heteroatoms in pyridinyl-substituted 5-membered (hetero)cycles as potential p38 alpha MAP kinase inhibitor scaffolds, cyclopentene, pyrrole, furan, and imidazole analogues were synthesized and tested with respect to their ability to inhibit p38a MAP kinase. The vicinal pyridine/4-fluorophenyl pharmacophore was conserved, such as in the prototypical imidazole inhibitor SB203580. The strength of the HB interaction was calculated and compared to the biological data.

  DOI：

  10.1021/jm801467h

文献信息

• Role of the Hydrogen Bonding Heteroatom−Lys53 Interaction between the p38α Mitogen-Activated Protein (MAP) Kinase and Pyridinyl-Substituted 5-Membered Heterocyclic Ring Inhibitors
  作者：Bassam Abu Thaher、Pierre Koch、Verena Schattel、Stefan Laufer

  DOI：10.1021/jm801467h

  日期：2009.4.23

  In the framework of Investigating the role of heteroatoms in pyridinyl-substituted 5-membered (hetero)cycles as potential p38 alpha MAP kinase inhibitor scaffolds, cyclopentene, pyrrole, furan, and imidazole analogues were synthesized and tested with respect to their ability to inhibit p38a MAP kinase. The vicinal pyridine/4-fluorophenyl pharmacophore was conserved, such as in the prototypical imidazole inhibitor SB203580. The strength of the HB interaction was calculated and compared to the biological data.