SN56 | 1272483-42-7

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 噻吩并噻唑类
• 英文名称: SN56
• 英文别名: 3-(2-(azepan-1-yl)ethyl)-4-bromo-6-propylbenzo[d]thiazol-2(3H)-one hydrochloride
• CAS: 1272483-42-7
• 化学式: C₁₈H₂₅BrN₂OS*ClH
• 分子量: 433.84
• InChiKey: ADNOPNXZTXIYIF-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.08
• 重原子数：
  24.0
• 可旋转键数：
  5.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.61
• 拓扑面积：
  25.24
• 氢给体数：
  0.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  SN56 在 tritium 作用下， 生成 [(3)H]-SN56
  参考文献：
  名称：

  Synthesis and characterization of [3H]-SN56, a novel radioligand for the σ1 receptor

  摘要：

  The study of the binding characteristics of a ligands in vivo and in vitro requires radiolabeled probes with high affinity and selectivity. The radioligand presently used for in vitro studies of the sigma(1) receptor, [H-3](+)-pentazocine, has significant limitations; it is difficult to synthesize, has limited chemical stability, and can be problematic to obtain. Evaluation of a series of novel 2(3H)-benzothiazolone compounds revealed SN56 to have sub-nanomolar and preferential affinity for the sigma(1) subtype, relative to sigma(2) and non-sigma, binding sites. The goal of this study was to characterize the binding of [H-3]-SN56 to sigma(1) receptors isolated from rat brain. Standard in vitro binding techniques were utilized to 1) determine the specificity and affinity of binding to sigma(1) receptors, 2) confirm that [H-3]-SN56 labels sites previously identified as sigma(1) by comparing binding to sites labeled by [H-3](+)-pentazocine, and 3) characterize the kinetics of binding. The results indicate that [H-3]-SN56 exhibits 1) specific, saturable, and reversible binding to the sigma(1) receptor, with B-max = 340 +/- 10 fmol/mg and K-d = 0.069 +/- 0.0074 nM, 2) competitive displacement by classical sigma compounds, yielding sigma K-1(i) values consistent with those reported in the literature, and 3) binding kinetics compatible with a 90 mm incubation, and filtration for separation of free and bound radioligand. The results of these studies suggest that [H-3]-SN56 may serve as a viable alternative to [H-3](+)-pentazocine in radioligand binding assays. (C) 2010 Elsevier B.V. All rights reserved.

  DOI：

  10.1016/j.ejphar.2010.10.099
• 作为产物：
  描述：

  6-丙基-1,3-苯并噻唑-2-醇 在 溴 、 碳酸氢钠 、 溶剂黄146 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 16.0h， 生成 SN56
  参考文献：
  名称：

  Synthesis and characterization of [3H]-SN56, a novel radioligand for the σ1 receptor

  摘要：

  The study of the binding characteristics of a ligands in vivo and in vitro requires radiolabeled probes with high affinity and selectivity. The radioligand presently used for in vitro studies of the sigma(1) receptor, [H-3](+)-pentazocine, has significant limitations; it is difficult to synthesize, has limited chemical stability, and can be problematic to obtain. Evaluation of a series of novel 2(3H)-benzothiazolone compounds revealed SN56 to have sub-nanomolar and preferential affinity for the sigma(1) subtype, relative to sigma(2) and non-sigma, binding sites. The goal of this study was to characterize the binding of [H-3]-SN56 to sigma(1) receptors isolated from rat brain. Standard in vitro binding techniques were utilized to 1) determine the specificity and affinity of binding to sigma(1) receptors, 2) confirm that [H-3]-SN56 labels sites previously identified as sigma(1) by comparing binding to sites labeled by [H-3](+)-pentazocine, and 3) characterize the kinetics of binding. The results indicate that [H-3]-SN56 exhibits 1) specific, saturable, and reversible binding to the sigma(1) receptor, with B-max = 340 +/- 10 fmol/mg and K-d = 0.069 +/- 0.0074 nM, 2) competitive displacement by classical sigma compounds, yielding sigma K-1(i) values consistent with those reported in the literature, and 3) binding kinetics compatible with a 90 mm incubation, and filtration for separation of free and bound radioligand. The results of these studies suggest that [H-3]-SN56 may serve as a viable alternative to [H-3](+)-pentazocine in radioligand binding assays. (C) 2010 Elsevier B.V. All rights reserved.

  DOI：

  10.1016/j.ejphar.2010.10.099