tert-butylN-[8-(piperazin-1-yl)octyl]carbamate | 2276787-51-8

• 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: tert-butylN-[8-(piperazin-1-yl)octyl]carbamate
• 英文别名: tert-butyl N-(8-piperazin-1-yloctyl)carbamate
• CAS: 2276787-51-8
• 化学式: C₁₇H₃₅N₃O₂
• 分子量: 313.484
• InChiKey: WUVBWALHOSQGSI-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.76
• 重原子数：
  22.0
• 可旋转键数：
  9.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.94
• 拓扑面积：
  53.6
• 氢给体数：
  2.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  tert-butylN-[8-(piperazin-1-yl)octyl]carbamate 在 三氟乙酸 作用下， 以 乙醇 为溶剂， 生成
  参考文献：
  名称：

  Fluorescent Benzothiazinone Analogues Efficiently and Selectively Label Dpre1 in Mycobacteria and Actinobacteria

  摘要：

  Benzothiazinones (BTZ) are highly potent bactericidal inhibitors of mycobacteria and the lead compound, BTZ043, and the optimized drug candidate, PBTZ169, have potential for the treatment of tuberculosis. Here, we exploited the tractability of the BTZ scaffold by attaching a range of fluorophores to the 2-substituent of the BTZ ring via short linkers. We show by means of fluorescence imaging that the most advanced derivative, JN108, is capable of efficiently labeling its target, the essential flavoenzyme DprE1, both in cell-free extracts and after purification as well as in growing cells of different actinobacterial species. DprE1 displays a polar localization in Mycobacterium tuberculosis, M. marinum, M. smegmatis, and Nocardia farcinica but not in Corynebacterium glutamicum. Finally, mutation of the cysteine residue in DprE1 in these species, to which BTZ covalently binds, abolishes completely the interaction with JN108, thereby highlighting the specificity of this fluorescent probe.

  DOI：

  10.1021/acschembio.8b00790
• 作为产物：
  描述：

  8-氨基-1-辛醇 在 四溴化碳 、 potassium carbonate 、 三苯基膦 、 sodium hydroxide 作用下， 以 乙醇 、 二氯甲烷 、 水 、 乙腈 为溶剂， 生成 tert-butylN-[8-(piperazin-1-yl)octyl]carbamate
  参考文献：
  名称：

  Fluorescent Benzothiazinone Analogues Efficiently and Selectively Label Dpre1 in Mycobacteria and Actinobacteria

  摘要：

  Benzothiazinones (BTZ) are highly potent bactericidal inhibitors of mycobacteria and the lead compound, BTZ043, and the optimized drug candidate, PBTZ169, have potential for the treatment of tuberculosis. Here, we exploited the tractability of the BTZ scaffold by attaching a range of fluorophores to the 2-substituent of the BTZ ring via short linkers. We show by means of fluorescence imaging that the most advanced derivative, JN108, is capable of efficiently labeling its target, the essential flavoenzyme DprE1, both in cell-free extracts and after purification as well as in growing cells of different actinobacterial species. DprE1 displays a polar localization in Mycobacterium tuberculosis, M. marinum, M. smegmatis, and Nocardia farcinica but not in Corynebacterium glutamicum. Finally, mutation of the cysteine residue in DprE1 in these species, to which BTZ covalently binds, abolishes completely the interaction with JN108, thereby highlighting the specificity of this fluorescent probe.

  DOI：

  10.1021/acschembio.8b00790