2-((5-hydroxy-4-oxo-2-phenyl-4H-chromen-7-yl)oxy)-N-(pyridin-2-yl)acetamide | 920430-49-5

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 黄酮类化合物
• 英文名称: 2-((5-hydroxy-4-oxo-2-phenyl-4H-chromen-7-yl)oxy)-N-(pyridin-2-yl)acetamide
• 英文别名: 2-(5-hydroxy-4-oxo-2-phenylchromen-7-yl)oxy-N-pyridin-2-ylacetamide
• CAS: 920430-49-5
• 化学式: C₂₂H₁₆N₂O₅
• 分子量: 388.379
• InChiKey: GYMXKFUFOSAHPS-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.6
• 重原子数：
  29
• 可旋转键数：
  5
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.05
• 拓扑面积：
  97.8
• 氢给体数：
  2
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  白杨素 在 potassium carbonate 、 N,N-二异丙基乙胺 、 Methanaminium,N-[(dimethylamino)(3H-1,2,3-triazolo[4,5-b]pyridin-3-yloxy)methylene]-N-methyl-, hexafluorophosphate(1-) 、 sodium iodide 、 sodium hydroxide 作用下， 以 甲醇 、 N,N-二甲基甲酰胺 、 丙酮 为溶剂， 反应 51.25h， 生成 2-((5-hydroxy-4-oxo-2-phenyl-4H-chromen-7-yl)oxy)-N-(pyridin-2-yl)acetamide
  参考文献：
  名称：

  Synthesis and anti-inflammatory in vitro, in silico, and in vivo studies of flavone analogues

  摘要：

  Chrysin and 7-hydroxy flavone were prepared by Baker-Venkatraman rearrangement followed by esterification at 7th position and replacement of ester with acetamide linking to different heterocyclic moieties synthesized 13a-g and 14a-g series of flavones analogues. These were screened against COX-2 and COX-1 enzymes for inhibition by in vitro assay and COX-2 for in silico docking studies. The compound 14a was found to be most active with IC50 of 3.11 A mu M concentration, with highest binding energy of -12.4 kcal/mole and 77.2 and 80.5 % inhibition at 3 and 5 h post-carrageenan induced in paw oedema.

  DOI：

  10.1007/s00044-015-1317-9

文献信息

• Structure-based design of flavone-based inhibitors of wild-type and T315I mutant of ABL
  作者：Hyeonjeong Choe、Jieun Kim、Sungwoo Hong

  DOI：10.1016/j.bmcl.2013.05.095

  日期：2013.8

  The existence of drug resistance caused by mutations in the break-point cluster region-Abelson (BCR-ABL) tyrosine kinase domain remains a clinical challenge due to limited treatment options for effective CML therapies. Here, we report a series of flavone-based common inhibitors equipotent for the wild type and the most drug-resistant T315I mutant of BCR-ABL. The original hit 1 was extensively modified through a structure-based drug design strategy, especially by varying the C7 acetamide appendage of the scaffold to exploit extended interactions with P-loop residues. Structural features relevant to the stabilization of the newly identified inhibitors in the ATP-binding site of ABL are discussed in detail. (C) 2013 Elsevier Ltd. All rights reserved.