2-(11-(4-(5-methoxy-1H-indol-3yl)-5,6-dihydropyridin-1(2H)-yl)undecyl) isoindoline-1,3-dione | 1035985-34-2

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 异吲哚及其衍生物
• 英文名称: 2-(11-(4-(5-methoxy-1H-indol-3yl)-5,6-dihydropyridin-1(2H)-yl)undecyl) isoindoline-1,3-dione
• CAS: 1035985-34-2
• 化学式: C₃₃H₄₁N₃O₃
• 分子量: 527.707
• InChiKey: WUSITQLZEAKKAJ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  7.07
• 重原子数：
  39.0
• 可旋转键数：
  14.0
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.45
• 拓扑面积：
  65.64
• 氢给体数：
  1.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  2-(11-(4-(5-methoxy-1H-indol-3yl)-5,6-dihydropyridin-1(2H)-yl)undecyl) isoindoline-1,3-dione 在 一水合肼 作用下， 生成 11-(4-(5-methoxy-1H-indol-3-yl)-5,6-dihydropyridin-1(2H)-yl)undecan-1-amine
  参考文献：
  名称：

  Biotin tethered homotryptamine derivatives: High affinity probes of the human serotonin transporter (hSERT)

  摘要：

  Quantum dot conjugates of compounds capable of inhibiting the serotonin transporter (SERT) could form the basis of fluorescent probes for live cell imaging of membrane bound SERT. Additionally, quantum dot-SERT antagonist conjugates may be amenable to fluorescence-based, high-throughput assays for this transporter. This Letter describes the synthesis of SERT-selective ligands amenable to conjugation to quantum dots via a biotin-streptavidin binding interaction. SERT selectivity and affinity were incorporated into the ligand via a tetrahydropyridine or cyclohexylamine derivative and the affinity of these compounds for SERT was measured by their ability to produce SERT-dependent currents in Xenopus laveis oocytes. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2011.01.102
• 作为产物：
  描述：

  N-(11-bromoundecyl)phthalimide 、 5-甲氧基-3-(1,2,3,6-四氢-4-吡啶)-1H-吲哚 在 三乙胺 作用下， 生成 2-(11-(4-(5-methoxy-1H-indol-3yl)-5,6-dihydropyridin-1(2H)-yl)undecyl) isoindoline-1,3-dione
  参考文献：
  名称：

  Biotin tethered homotryptamine derivatives: High affinity probes of the human serotonin transporter (hSERT)

  摘要：

  Quantum dot conjugates of compounds capable of inhibiting the serotonin transporter (SERT) could form the basis of fluorescent probes for live cell imaging of membrane bound SERT. Additionally, quantum dot-SERT antagonist conjugates may be amenable to fluorescence-based, high-throughput assays for this transporter. This Letter describes the synthesis of SERT-selective ligands amenable to conjugation to quantum dots via a biotin-streptavidin binding interaction. SERT selectivity and affinity were incorporated into the ligand via a tetrahydropyridine or cyclohexylamine derivative and the affinity of these compounds for SERT was measured by their ability to produce SERT-dependent currents in Xenopus laveis oocytes. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2011.01.102

文献信息

• A Fluorescence Displacement Assay for Antidepressant Drug Discovery Based on Ligand-Conjugated Quantum Dots
  作者：Jerry C. Chang、Ian D. Tomlinson、Michael R. Warnement、Hideki Iwamoto、Louis J. DeFelice、Randy D. Blakely、Sandra J. Rosenthal

  DOI：10.1021/ja204301g

  日期：2011.11.9

  The serotonin (5-hydroxytryptamine, 5-HT) transporter (SERT) protein plays a central role in terminating 5-HT neurotransmission and is the most important therapeutic target for the treatment of major depression and anxiety disorders. We report an innovative, versatile, and target-selective quantum dot (QD) labeling approach for SERT in single Xenopus oocytes that can be adopted as a drug-screening platform. Our labeling approach employs a custom-made, QD-tagged indoleamine derivative ligand, IDT318, that is structurally similar to 5-HT and accesses the primary binding site with enhanced human SERT selectivity. Incubating QD-labeled oocytes with paroxetine (Paxil), a high-affinity SERT-specific inhibitor, showed a concentration- and time-dependent decrease in QD fluorescence, demonstrating the Utility of our approach for the identification of SERT modulators. Furthermore, with the development of ligands aimed at other pharmacologically, relevant target, our approach May potentially form the basis for a multitarget drug discovery platform.