(E)-3-[4-[3-[4-[(E)-2-carboxyethenyl]phenyl]-2-oxoimidazolidin-1-yl]phenyl]prop-2-enoic acid | 1428236-91-2

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 肉桂酸及其衍生物
• 英文名称: (E)-3-[4-[3-[4-[(E)-2-carboxyethenyl]phenyl]-2-oxoimidazolidin-1-yl]phenyl]prop-2-enoic acid
• CAS: 1428236-91-2
• 化学式: C₂₁H₁₈N₂O₅
• 分子量: 378.384
• InChiKey: IUQASTYWCWYXGZ-YDWXAUTNSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.5
• 重原子数：
  28
• 可旋转键数：
  6
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.1
• 拓扑面积：
  98.2
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  对溴苯甲醛 在 N,N-二甲基丙烯基脲 、 tris(dibenzylideneacetone)dipalladium(0) chloroform complex 、 正丁基锂 、 caesium carbonate 、 4,5-双二苯基膦-9,9-二甲基氧杂蒽 、 sodium hydroxide 作用下， 以 四氢呋喃 、 乙醇 、 正己烷 、 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 23.5h， 生成 (E)-3-[4-[3-[4-[(E)-2-carboxyethenyl]phenyl]-2-oxoimidazolidin-1-yl]phenyl]prop-2-enoic acid
  参考文献：
  名称：

  Novel symmetrical ureas as modulators of protein arginine methyl transferases

  摘要：

  Methylation of histone arginine residues is an epigenetic mark related to gene expression that is implicated in a variety of biological processes and can be reversed by small-molecule modulators of protein arginine methyltransferases (PRMTs). A series of symmetrical ureas, designed as analogues of the known PRMT1 inhibitor AMI-1 have been synthesized using Pd-catalyzed Ar-N amide bond formation processes or carbonylation reactions as key steps. Their inhibitory profile has been characterized. The enzymatic assays showed a weak effect on PRMT1 and PRMT5 activity for most of the compounds. The acyclic urea that exhibited the strongest effect on the inhibition of the PRMT1 activity also showed the greatest effect on the expression of some androgen receptor target genes (TMPRSS2 and FKBP5), which may be related with its enzymatic activity. Surprisingly, AMI-1 behaved as an activator of PRMT5 activity, a result not reported so far. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2013.01.017

文献信息

• Novel symmetrical ureas as modulators of protein arginine methyl transferases
  作者：Noelia Fontán、Patricia García-Domínguez、Rosana Álvarez、Ángel R. de Lera

  DOI：10.1016/j.bmc.2013.01.017

  日期：2013.4

  Methylation of histone arginine residues is an epigenetic mark related to gene expression that is implicated in a variety of biological processes and can be reversed by small-molecule modulators of protein arginine methyltransferases (PRMTs). A series of symmetrical ureas, designed as analogues of the known PRMT1 inhibitor AMI-1 have been synthesized using Pd-catalyzed Ar-N amide bond formation processes or carbonylation reactions as key steps. Their inhibitory profile has been characterized. The enzymatic assays showed a weak effect on PRMT1 and PRMT5 activity for most of the compounds. The acyclic urea that exhibited the strongest effect on the inhibition of the PRMT1 activity also showed the greatest effect on the expression of some androgen receptor target genes (TMPRSS2 and FKBP5), which may be related with its enzymatic activity. Surprisingly, AMI-1 behaved as an activator of PRMT5 activity, a result not reported so far. (C) 2013 Elsevier Ltd. All rights reserved.