N-{2-[(4'-Cyano-1,1'-biphenyl-4-YL)oxy]ethyl}-N'-hydroxy-N-methylurea

• 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: N-{2-[(4'-Cyano-1,1'-biphenyl-4-YL)oxy]ethyl}-N'-hydroxy-N-methylurea
• 英文别名: 1-[2-[4-(4-cyanophenyl)phenoxy]ethyl]-3-hydroxy-1-methylurea
• 化学式: C₁₇H₁₇N₃O₃
• 分子量: 311.34
• InChiKey: GVMUNGGWXRKCEU-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.1
• 重原子数：
  23
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.18
• 拓扑面积：
  85.6
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  氰基联苯酚 在 四溴化碳 、 potassium carbonate 、 三苯基膦 、 potassium iodide 作用下， 以 四氢呋喃 、 N,N-二甲基甲酰胺 、 乙腈 为溶剂， 反应 17.0h， 生成 N-{2-[(4'-Cyano-1,1'-biphenyl-4-YL)oxy]ethyl}-N'-hydroxy-N-methylurea
  参考文献：
  名称：

  N-Hydroxyurea as zinc binding group in matrix metalloproteinase inhibition: Mode of binding in a complex with MMP-8

  摘要：

  The first crystallographic structure of an N-hydroxyurea inhibitor bound into the active site of a matrix metalloproteinase is reported. The ligand and three other analogues were prepared and studied as inhibitors of MMP-2, MMP-3, and MMP-8. The crystal structure of the complex with MMP-8 shows that the N-hydroxyurea, contrary to the analogous hydroxamate, binds the catalytic zinc ion in a monodentate rather than bidentate mode and with high out-of-plane distortion of the amide bonds.

  DOI：

  10.1016/j.bmcl.2005.09.057

文献信息

• IDENTIFICATION AND TARGETED MODULATION OF GENE SIGNALING NETWORKS
  申请人：CAMP4 THERAPEUTICS CORPORATION

  公开号：US20210254056A1

  公开（公告）日：2021-08-19

  The present invention provides methods and compositions for the evaluation, alteration and/or optimization of gene signaling. Methods and systems are also provided which exploit the information generated in the identification of new targets and non-canonical signaling pathways.
• N-Hydroxyurea as zinc binding group in matrix metalloproteinase inhibition: Mode of binding in a complex with MMP-8
  作者：Cristina Campestre、Mariangela Agamennone、Paolo Tortorella、Serena Preziuso、Alessandro Biasone、Enrico Gavuzzo、Giorgio Pochetti、Fernando Mazza、Oliver Hiller、Harald Tschesche、Valerio Consalvi、Carlo Gallina

  DOI：10.1016/j.bmcl.2005.09.057

  日期：2006.1

  The first crystallographic structure of an N-hydroxyurea inhibitor bound into the active site of a matrix metalloproteinase is reported. The ligand and three other analogues were prepared and studied as inhibitors of MMP-2, MMP-3, and MMP-8. The crystal structure of the complex with MMP-8 shows that the N-hydroxyurea, contrary to the analogous hydroxamate, binds the catalytic zinc ion in a monodentate rather than bidentate mode and with high out-of-plane distortion of the amide bonds.