22-azido-1,1,1-triphenyl-2,5,8,11,14,17,20-heptaoxadocosane | 745048-18-4

• 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: 22-azido-1,1,1-triphenyl-2,5,8,11,14,17,20-heptaoxadocosane
• 英文别名: [2-[2-[2-[2-[2-[2-(2-Azidoethoxy)ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy-diphenylmethyl]benzene
• CAS: 745048-18-4
• 化学式: C₃₃H₄₃N₃O₇
• 分子量: 593.72
• InChiKey: XYUWKBOKZFGOTN-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.8
• 重原子数：
  43
• 可旋转键数：
  25
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.45
• 拓扑面积：
  79
• 氢给体数：
  0
• 氢受体数：
  9

反应信息

• 作为反应物：
  描述：

  22-azido-1,1,1-triphenyl-2,5,8,11,14,17,20-heptaoxadocosane 在 甲醇 、 对甲苯磺酸 、 三乙胺 作用下， 以 二氯甲烷 为溶剂， 反应 2.0h， 生成 20-azido-3,6,9,12,15,18-hexaoxaicos-1-ylmethanesulfonate
  参考文献：
  名称：

  Fluorescent Pirenzepine Derivatives as Potential Bitopic Ligands of the Human M1 Muscarinic Receptor

  摘要：

  Following a recent description of fluorescence resonance energy transfer between enhanced green fluorescent protein (EGFP)-fused human muscarinic M1 receptors and Bodipy-labeled pirenzepine, we synthesized seven fluorescent derivatives of this antagonist in order to further characterize ligand-receptor interactions. These compounds carry Bodipy [558/568], Rhodamine Red-X [560/580], or Fluorolink Cy3 [550/570] fluorophores connected to pirenzepine through various linkers. All molecules reversibly bind with high affinity to M1 receptors (radioligand and energy transfer binding experiments) provided that the linker contains more than six atoms. The energy transfer efficiency exhibits modest variations among ligands, indicating that the distance separating EGFP from the fluorophores remains almost constant. This also supports the notion that the fluorophores may bind to the receptor protein. Kinetic analyses reveal that the dissociation of two Bodipy derivatives (10 or 12 atom long linkers) is sensitive to the presence of the allosteric modulator brucine, while that of all other molecules (15-24 atom long linkers) is not. The data favor the idea that these analogues might interact with both the acetylcholine and the brucine binding domains.

  DOI：

  10.1021/jm040800a
• 作为产物：
  描述：

  三苯基甲醇 在 sodium azide 、 potassium tert-butylate 、 对甲苯磺酸 、 三乙胺 作用下， 以 二氯甲烷 、 乙腈 、 叔丁醇 、 苯 为溶剂， 反应 10.0h， 生成 22-azido-1,1,1-triphenyl-2,5,8,11,14,17,20-heptaoxadocosane
  参考文献：
  名称：

  Fluorescent Pirenzepine Derivatives as Potential Bitopic Ligands of the Human M1 Muscarinic Receptor

  摘要：

  Following a recent description of fluorescence resonance energy transfer between enhanced green fluorescent protein (EGFP)-fused human muscarinic M1 receptors and Bodipy-labeled pirenzepine, we synthesized seven fluorescent derivatives of this antagonist in order to further characterize ligand-receptor interactions. These compounds carry Bodipy [558/568], Rhodamine Red-X [560/580], or Fluorolink Cy3 [550/570] fluorophores connected to pirenzepine through various linkers. All molecules reversibly bind with high affinity to M1 receptors (radioligand and energy transfer binding experiments) provided that the linker contains more than six atoms. The energy transfer efficiency exhibits modest variations among ligands, indicating that the distance separating EGFP from the fluorophores remains almost constant. This also supports the notion that the fluorophores may bind to the receptor protein. Kinetic analyses reveal that the dissociation of two Bodipy derivatives (10 or 12 atom long linkers) is sensitive to the presence of the allosteric modulator brucine, while that of all other molecules (15-24 atom long linkers) is not. The data favor the idea that these analogues might interact with both the acetylcholine and the brucine binding domains.

  DOI：

  10.1021/jm040800a

文献信息

• Fluorescent Pirenzepine Derivatives as Potential Bitopic Ligands of the Human M1 Muscarinic Receptor
  作者：Chouaib Tahtaoui、Isabelle Parrot、Philippe Klotz、Fabrice Guillier、Jean-Luc Galzi、Marcel Hibert、Brigitte Ilien

  DOI：10.1021/jm040800a

  日期：2004.8.1

  Following a recent description of fluorescence resonance energy transfer between enhanced green fluorescent protein (EGFP)-fused human muscarinic M1 receptors and Bodipy-labeled pirenzepine, we synthesized seven fluorescent derivatives of this antagonist in order to further characterize ligand-receptor interactions. These compounds carry Bodipy [558/568], Rhodamine Red-X [560/580], or Fluorolink Cy3 [550/570] fluorophores connected to pirenzepine through various linkers. All molecules reversibly bind with high affinity to M1 receptors (radioligand and energy transfer binding experiments) provided that the linker contains more than six atoms. The energy transfer efficiency exhibits modest variations among ligands, indicating that the distance separating EGFP from the fluorophores remains almost constant. This also supports the notion that the fluorophores may bind to the receptor protein. Kinetic analyses reveal that the dissociation of two Bodipy derivatives (10 or 12 atom long linkers) is sensitive to the presence of the allosteric modulator brucine, while that of all other molecules (15-24 atom long linkers) is not. The data favor the idea that these analogues might interact with both the acetylcholine and the brucine binding domains.