rhodamine red-X | 178623-12-6

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并吡喃
• 英文名称: rhodamine red-X
• 英文别名: 5-(5-carboxypentylsulfamoyl)-2-[3-(diethylamino)-6-diethylazaniumylidenexanthen-9-yl]benzenesulfonate
• CAS: 178623-12-6
• 化学式: C₃₃H₄₁N₃O₈S₂
• 分子量: 671.836
• InChiKey: XLXOKMFKGASILN-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3
• 重原子数：
  46
• 可旋转键数：
  14
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.39
• 拓扑面积：
  173
• 氢给体数：
  2
• 氢受体数：
  10

反应信息

• 作为反应物：
  描述：

  11-[(4-{2-[2(2-Aminoethoxy)ethoxy]ethyl}piperazine-1-yl)acetyl]-5,11-dihydro-6H-pyrido-[2,3-b][1,4]benzodiazepine-6-one 、 rhodamine red-X 在 N,N-二异丙基乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 2.0h， 生成 N-{6-diethylamino-9-[4-({[6-oxo-6-({2-[2-(2-{4-[2-oxo-2-(6-oxo-5,6-dihydro-11H-pyrido[2,3-b][1,4]benzodiazepin-11-yl)ethyl]piperazin-1-yl}ethoxy)ethoxy]ethyl}amino)hexyl]amino}sulfonyl)-2-sulfophenyl]-3H-xanthen-3-ylidene}-N-ethyl ethanaminium
  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：

  在 盐酸 作用下， 以 1,4-二氧六环 为溶剂， 以60%的产率得到rhodamine red-X
  参考文献：
  名称：

  Chemical Optimization of New Ligands of the Low-Density Lipoprotein Receptor as Potential Vectors for Central Nervous System Targeting

  摘要：

  Drug delivery to the central nervous system is hindered by the presence of physiological barriers such as the blood-brain barrier. To accomplish the task of nutrient transport, the brain endothelium is endowed with various transport systems, induding receptor-mediated transcytosis (RMT). This system can be used to shuttle therapeutics into the central nervous system (CNS) in a noninvasive manner. Therefore, the low-density lipoprotein receptor (LDLR) is a relevant target for delivering drugs. From an initial phage display biopanning a series of peptide ligands for the LDLR was optimized leading to size reduction and improved receptor binding affinity with the identification of peptide 22 and its analogues. Further real-time biphoton microscopy experiments on living mice demonstrated the ability of peptide 22 to efficiently and quickly cross CNS physiological barriers. This validation of peptide 22 led us to explore its binding on the extracellular LDLR domain from an NMR-oriented structural study and docking experiments.

  DOI：

  10.1021/jm2014919

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.
• Chemical Optimization of New Ligands of the Low-Density Lipoprotein Receptor as Potential Vectors for Central Nervous System Targeting
  作者：Jean-Daniel Malcor、Nadine Payrot、Marion David、Aude Faucon、Karima Abouzid、Guillaume Jacquot、Nicolas Floquet、Franck Debarbieux、Geneviève Rougon、Jean Martinez、Michel Khrestchatisky、Patrick Vlieghe、Vincent Lisowski

  DOI：10.1021/jm2014919

  日期：2012.3.8

  Drug delivery to the central nervous system is hindered by the presence of physiological barriers such as the blood-brain barrier. To accomplish the task of nutrient transport, the brain endothelium is endowed with various transport systems, induding receptor-mediated transcytosis (RMT). This system can be used to shuttle therapeutics into the central nervous system (CNS) in a noninvasive manner. Therefore, the low-density lipoprotein receptor (LDLR) is a relevant target for delivering drugs. From an initial phage display biopanning a series of peptide ligands for the LDLR was optimized leading to size reduction and improved receptor binding affinity with the identification of peptide 22 and its analogues. Further real-time biphoton microscopy experiments on living mice demonstrated the ability of peptide 22 to efficiently and quickly cross CNS physiological barriers. This validation of peptide 22 led us to explore its binding on the extracellular LDLR domain from an NMR-oriented structural study and docking experiments.