3-[4-(2-methylsulfanylphenyl)piperazin-1-yl]propionitrile | 1178860-83-7

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 二嗪烷类
• 英文名称: 3-[4-(2-methylsulfanylphenyl)piperazin-1-yl]propionitrile
• 英文别名: 3-[4-(2-Methylsulfanylphenyl)piperazin-1-yl]propanenitrile
• CAS: 1178860-83-7
• 化学式: C₁₄H₁₉N₃S
• 分子量: 261.391
• InChiKey: OVTCRXAOORGEOO-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.1
• 重原子数：
  18
• 可旋转键数：
  4
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  55.6
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  3-[4-(2-methylsulfanylphenyl)piperazin-1-yl]propionitrile 在 lithium aluminium tetrahydride 作用下， 以 乙醚 为溶剂， 以18%的产率得到3-[4-(2-methylsulfanylphenyl)piperazin-1-yl]propylamine
  参考文献：
  名称：

  Dopamine D₂, D₃, and D₄ Selective Phenylpiperazines as Molecular Probes To Explore the Origins of Subtype Specific Receptor Binding

  摘要：

  Assembling phenylpiperazines with 7a-azaindole via different spacer elements, we developed subtype selective dopamine receptor ligands of types 1a,c,2a, and 3a preferentially interacting with D-4, D-2, and D-3, respectively, To complete this set, the methylthio analogues 2b and 3b exceeding the affinity of 2a and 3a by one order of magnitude and the structural intermediate 1b were synthesized. These chemically similar but biologically divergent target compounds served as molecular probes for radioligand displacement experiments, mutagenesis, and docking studies on homology models based on the recent crystal structure of the beta(2)-adrenergic receptor. Specific interactions with the highly conserved amino acids ASP(3.32) and His(6.55) and less conserved residues at positions 2.61, 2,64, 3.28, and 3.29 were identified. Inclusion of a carefully modeled extracellular loop 2 displayed two nonconserved residues in EL2 that differently contribute to ligand binding. Obviously, subtype selectivity is caused by nonconserved but frequently mediated by conserved amino acids.

  DOI：

  10.1021/jm900690y
• 作为产物：
  描述：

  1-(2-甲基巯苯基)哌嗪 、 3-溴丙腈 在 potassium carbonate 、 sodium iodide 作用下， 以 乙腈 为溶剂， 反应 24.0h， 以67%的产率得到3-[4-(2-methylsulfanylphenyl)piperazin-1-yl]propionitrile
  参考文献：
  名称：

  Dopamine D₂, D₃, and D₄ Selective Phenylpiperazines as Molecular Probes To Explore the Origins of Subtype Specific Receptor Binding

  摘要：

  Assembling phenylpiperazines with 7a-azaindole via different spacer elements, we developed subtype selective dopamine receptor ligands of types 1a,c,2a, and 3a preferentially interacting with D-4, D-2, and D-3, respectively, To complete this set, the methylthio analogues 2b and 3b exceeding the affinity of 2a and 3a by one order of magnitude and the structural intermediate 1b were synthesized. These chemically similar but biologically divergent target compounds served as molecular probes for radioligand displacement experiments, mutagenesis, and docking studies on homology models based on the recent crystal structure of the beta(2)-adrenergic receptor. Specific interactions with the highly conserved amino acids ASP(3.32) and His(6.55) and less conserved residues at positions 2.61, 2,64, 3.28, and 3.29 were identified. Inclusion of a carefully modeled extracellular loop 2 displayed two nonconserved residues in EL2 that differently contribute to ligand binding. Obviously, subtype selectivity is caused by nonconserved but frequently mediated by conserved amino acids.

  DOI：

  10.1021/jm900690y

文献信息

• Dopamine D₂, D₃, and D₄ Selective Phenylpiperazines as Molecular Probes To Explore the Origins of Subtype Specific Receptor Binding
  作者：Katharina Ehrlich、Angela Götz、Stefan Bollinger、Nuska Tschammer、Laura Bettinetti、Steffen Härterich、Harald Hübner、Harald Lanig、Peter Gmeiner

  DOI：10.1021/jm900690y

  日期：2009.8.13

  Assembling phenylpiperazines with 7a-azaindole via different spacer elements, we developed subtype selective dopamine receptor ligands of types 1a,c,2a, and 3a preferentially interacting with D-4, D-2, and D-3, respectively, To complete this set, the methylthio analogues 2b and 3b exceeding the affinity of 2a and 3a by one order of magnitude and the structural intermediate 1b were synthesized. These chemically similar but biologically divergent target compounds served as molecular probes for radioligand displacement experiments, mutagenesis, and docking studies on homology models based on the recent crystal structure of the beta(2)-adrenergic receptor. Specific interactions with the highly conserved amino acids ASP(3.32) and His(6.55) and less conserved residues at positions 2.61, 2,64, 3.28, and 3.29 were identified. Inclusion of a carefully modeled extracellular loop 2 displayed two nonconserved residues in EL2 that differently contribute to ligand binding. Obviously, subtype selectivity is caused by nonconserved but frequently mediated by conserved amino acids.