O-[[4-(4-fluorophenyl)phenyl]methyl]hydroxylamine | 881377-34-0

• 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: O-[[4-(4-fluorophenyl)phenyl]methyl]hydroxylamine
• CAS: 881377-34-0
• 化学式: C₁₃H₁₂FNO
• 分子量: 217.243
• InChiKey: CEIHYBHLDPBHIX-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.6
• 重原子数：
  16
• 可旋转键数：
  3
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.08
• 拓扑面积：
  35.2
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  O-[[4-(4-fluorophenyl)phenyl]methyl]hydroxylamine 、 5-butyryl-2,2-dimethyl-4,6-dioxocyclohexanecarbonitrile 在 溶剂黄146 作用下， 以 乙醇 为溶剂， 反应 16.0h， 以340 mg的产率得到(Z)-5-(1-((4-fluorobiphenyl-4-yl)methoxyimino)butyl)-2,2-dimethyl-4,6-dioxocyclohexanecarbonitrile
  参考文献：
  名称：

  Binding Inhibitors of the Bacterial Sliding Clamp by Design

  摘要：

  The bacterial replisome is a target for the development of new antibiotics to combat drug resistant strains. The beta(2) sliding clamp is an essential component of the replicative machinery, providing a platform for recruitment and function of other replisomal components and ensuring polymerase processivity during DNA replication and repair. A single binding region of the clamp is utilized by its binding partners, which all contain conserved binding motifs. The C-terminal Leu and Phe residues of these motifs are integral to the binding interaction. We acquired three-dimensional structural information on the binding site in beta(2) by a study of the binding of modified peptides. Development of a three-dimensional pharmacophore based on the C-terminal dipeptide of the motif enabled identification of compounds that on further development inhibited alpha-beta(2) interaction at low micromolar concentrations. We report the crystal structure of the complex containing one of these inhibitors, a biphenyl oxime, bound to beta(2), as a starting point for further inhibitor design.

  DOI：

  10.1021/jm2004333
• 作为产物：
  描述：

  2-[(4'-fluorobiphenyl-4-yl)methoxy]isoindoline-1,3-dione 在 哌嗪 作用下， 以 乙醇 为溶剂， 反应 2.0h， 生成 O-[[4-(4-fluorophenyl)phenyl]methyl]hydroxylamine
  参考文献：
  名称：

  Binding Inhibitors of the Bacterial Sliding Clamp by Design

  摘要：

  The bacterial replisome is a target for the development of new antibiotics to combat drug resistant strains. The beta(2) sliding clamp is an essential component of the replicative machinery, providing a platform for recruitment and function of other replisomal components and ensuring polymerase processivity during DNA replication and repair. A single binding region of the clamp is utilized by its binding partners, which all contain conserved binding motifs. The C-terminal Leu and Phe residues of these motifs are integral to the binding interaction. We acquired three-dimensional structural information on the binding site in beta(2) by a study of the binding of modified peptides. Development of a three-dimensional pharmacophore based on the C-terminal dipeptide of the motif enabled identification of compounds that on further development inhibited alpha-beta(2) interaction at low micromolar concentrations. We report the crystal structure of the complex containing one of these inhibitors, a biphenyl oxime, bound to beta(2), as a starting point for further inhibitor design.

  DOI：

  10.1021/jm2004333