methyl 15-(3-nitrophenyl)pentadec-12-enoate | 121269-67-8

• 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: methyl 15-(3-nitrophenyl)pentadec-12-enoate
• CAS: 121269-67-8
• 化学式: C₂₂H₃₃NO₄
• 分子量: 375.508
• InChiKey: CETMQCDFTLYAEK-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  6.16
• 重原子数：
  27.0
• 可旋转键数：
  15.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.59
• 拓扑面积：
  69.44
• 氢给体数：
  0.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  methyl 15-(3-nitrophenyl)pentadec-12-enoate 在 palladium on activated charcoal 吡啶 、 盐酸 、 4-二甲氨基吡啶 、 氢氧化钾 、 sodium tetrahydroborate 、 氢气 、 碘 、 N,N'-二环己基碳二亚胺 、 potassium iodide 、 sodium nitrite 作用下， 以 四氢呋喃 、 甲醇 、 二氯甲烷 、 氯仿 、 水 、 乙酸乙酯 、 苯 为溶剂， 反应 14.75h， 生成 1-<15-(3-iodophenyl)pentadecanoyl>-2-acetyl-3-O-trityl-rac-glycerol
  参考文献：
  名称：

  Iodoaryl analogs of dioctanoylglycerol and 1-oleoyl-2-acetylglycerol as probes for protein kinase C

  摘要：

  Analogues of dioctanoylglycerol (diC8) and 1-oleoyl-2-acetylglycerol (OAG) containing an iodoaryl group have been synthesized and shown to compete with [3H]phorbol dibutyrate [( ([3H]PDBu) for binding to protein kinase C in a crude rat brain preparation. Phorbol diesters have been shown to bind specifically to protein kinase C and the PDBu receptor has been copurified with protein kinase C activity. All three diacylglycerol analogues were comparable to OAG in binding affinity. In an assay of protein kinase C activation, the diC8 analogue was more active than the OAG analogues, thus demonstrating greater structural specificity under the conditions of this assay.

  DOI：

  10.1021/jm00129a014
• 作为产物：
  描述：

  3-(3-硝基苯基)丙酸 在 吡啶 、 三氟化硼 、 potassium tert-butylate 、 三溴化磷 作用下， 以 四氢呋喃 、 二氯甲烷 、 乙腈 、 苯 为溶剂， 反应 55.5h， 生成 methyl 15-(3-nitrophenyl)pentadec-12-enoate
  参考文献：
  名称：

  Iodoaryl analogs of dioctanoylglycerol and 1-oleoyl-2-acetylglycerol as probes for protein kinase C

  摘要：

  Analogues of dioctanoylglycerol (diC8) and 1-oleoyl-2-acetylglycerol (OAG) containing an iodoaryl group have been synthesized and shown to compete with [3H]phorbol dibutyrate [( ([3H]PDBu) for binding to protein kinase C in a crude rat brain preparation. Phorbol diesters have been shown to bind specifically to protein kinase C and the PDBu receptor has been copurified with protein kinase C activity. All three diacylglycerol analogues were comparable to OAG in binding affinity. In an assay of protein kinase C activation, the diC8 analogue was more active than the OAG analogues, thus demonstrating greater structural specificity under the conditions of this assay.

  DOI：

  10.1021/jm00129a014