(E)-3-(3,4-dihydroxyphenyl)-N-tritylacrylamide | 1441337-89-8

• 分子结构分类: 有机化合物 - 苯类化合物 - 三苯基化合物
• 英文名称: (E)-3-(3,4-dihydroxyphenyl)-N-tritylacrylamide
• CAS: 1441337-89-8
• 化学式: C₂₈H₂₃NO₃
• 分子量: 421.496
• InChiKey: ULULWGPDFITFRQ-HTXNQAPBSA-N

物化性质

• 沸点：
  696.2±55.0 °C(Predicted)
• 密度：
  1.249±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  5.22
• 重原子数：
  32.0
• 可旋转键数：
  6.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.04
• 拓扑面积：
  69.56
• 氢给体数：
  3.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  (E)-3-(3,4-dihydroxyphenyl)-N-tritylacrylamide 在 三乙胺 、 三乙基硅烷 作用下， 以 二氯甲烷 为溶剂， 反应 3.0h， 以68%的产率得到3,4-二羟基肉桂酰胺
  参考文献：
  名称：

  Identification of Cinnamic Acid Derivatives As Novel Antagonists of the Prokaryotic Proton-Gated Ion Channel GLIC

  摘要：

  Pentameric ligand gated ion channels (pLGICs) mediate signal transduction. The binding of an extracellular ligand is coupled to the transmembrane channel opening. So far, all known agonists bind at the interface between subunits in a topologically conserved "orthosteric site" whose amino acid composition defines the pharmacological specificity of pLGIC subtypes. A striking exception is the bacterial proton-activated GLIC protein, exhibiting an uncommon orthosteric binding site in terms of sequence and local architecture. Among a library of Gloeobacter violaceus metabolites, we identified a series of cinnamic acid derivatives, which antagonize the GLIC proton-elicited response. Structure activity analysis shows a key contribution of the carboxylate moiety to GLIC inhibition. Molecular docking coupled to site-directed mutagenesis support that is located below the classical orthosteric site. These antagonists provide new tools to modulate conformation used as a prototypic pLGIC, and opens new avenues to study the signal transduction mechanism. the binding pocket of GLIC, currently used as a prototypic pLGIC, and opens new avenues to study the signal transduction mechanism.

  DOI：

  10.1021/jm400374q
• 作为产物：
  描述：

  TRANS-咖啡酸 、 三苯甲胺 在 C₁₁H₁₉N₆OP⁽¹⁺⁾*F₆P^(1-) 、 N,N-二异丙基乙胺 作用下， 以 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 96.0h， 以28%的产率得到(E)-3-(3,4-dihydroxyphenyl)-N-tritylacrylamide
  参考文献：
  名称：

  Identification of Cinnamic Acid Derivatives As Novel Antagonists of the Prokaryotic Proton-Gated Ion Channel GLIC

  摘要：

  Pentameric ligand gated ion channels (pLGICs) mediate signal transduction. The binding of an extracellular ligand is coupled to the transmembrane channel opening. So far, all known agonists bind at the interface between subunits in a topologically conserved "orthosteric site" whose amino acid composition defines the pharmacological specificity of pLGIC subtypes. A striking exception is the bacterial proton-activated GLIC protein, exhibiting an uncommon orthosteric binding site in terms of sequence and local architecture. Among a library of Gloeobacter violaceus metabolites, we identified a series of cinnamic acid derivatives, which antagonize the GLIC proton-elicited response. Structure activity analysis shows a key contribution of the carboxylate moiety to GLIC inhibition. Molecular docking coupled to site-directed mutagenesis support that is located below the classical orthosteric site. These antagonists provide new tools to modulate conformation used as a prototypic pLGIC, and opens new avenues to study the signal transduction mechanism. the binding pocket of GLIC, currently used as a prototypic pLGIC, and opens new avenues to study the signal transduction mechanism.

  DOI：

  10.1021/jm400374q