ethyl (2S)-1-(3,3-dimethyl-1,2-dioxo-4-hydroxybutyl)-2-piperidinecarboxylate | 152754-48-8

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: ethyl (2S)-1-(3,3-dimethyl-1,2-dioxo-4-hydroxybutyl)-2-piperidinecarboxylate
• CAS: 152754-48-8
• 化学式: C₁₄H₂₃NO₅
• 分子量: 285.34
• InChiKey: IWYFEOXKRXOJPL-JTQLQIEISA-N

物化性质

• 沸点：
  405.6±55.0 °C(Predicted)
• 密度：
  1.171±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.52
• 重原子数：
  20.0
• 可旋转键数：
  5.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.79
• 拓扑面积：
  83.91
• 氢给体数：
  1.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  ethyl (2S)-1-(3,3-dimethyl-1,2-dioxo-4-hydroxybutyl)-2-piperidinecarboxylate 在 4-二甲氨基吡啶 、 lithium hydroxide 、 对甲苯磺酸 、 三乙胺 、 三氟乙酸 作用下， 以 四氢呋喃 、 甲醇 、 二氯甲烷 、 苯 为溶剂， 反应 6.0h， 生成
  参考文献：
  名称：

  Design, synthesis, and kinetic evaluation of high-affinity FKBP ligands and the X-ray crystal structures of their complexes with FKBP12

  摘要：

  The design and synthesis of high-affinity FKBP12 ligands is described. These compounds potently inhibit the cis-trans-peptidylprolyl isomerase (rotamase) activity catalyzed by FKBP12 with inhibition constants (K(i,app)) as low as 1 nM, yet they possess remarkable structural simplicity relative to FK506 and rapamycin, from which they are conceptually derived. The atomic structures of three FKBP12-ligand complexes and of one unbound ligand were determined by X-ray crystallography and are compared to the FKBP12-FK506 and FKBP12-rapamycin complexes.

  DOI：

  10.1021/ja00075a008
• 作为产物：
  描述：

  二氢-4,4-二甲基-2,3-呋喃二酮 、 (s)-哌啶-2-羧酸乙酯 在 4-二甲氨基吡啶 作用下， 以 甲苯 为溶剂， 反应 18.0h， 以82%的产率得到ethyl (2S)-1-(3,3-dimethyl-1,2-dioxo-4-hydroxybutyl)-2-piperidinecarboxylate
  参考文献：
  名称：

  Design, synthesis, and kinetic evaluation of high-affinity FKBP ligands and the X-ray crystal structures of their complexes with FKBP12

  摘要：

  The design and synthesis of high-affinity FKBP12 ligands is described. These compounds potently inhibit the cis-trans-peptidylprolyl isomerase (rotamase) activity catalyzed by FKBP12 with inhibition constants (K(i,app)) as low as 1 nM, yet they possess remarkable structural simplicity relative to FK506 and rapamycin, from which they are conceptually derived. The atomic structures of three FKBP12-ligand complexes and of one unbound ligand were determined by X-ray crystallography and are compared to the FKBP12-FK506 and FKBP12-rapamycin complexes.

  DOI：

  10.1021/ja00075a008

文献信息

• Reactive group-embedded affinity labeling reagent for efficient intracellular protein labeling
  作者：Yousuke Takaoka、Yuuki Nukadzuka、Minoru Ueda

  DOI：10.1016/j.bmc.2017.02.059

  日期：2017.6

  Affinity labeling of a target protein is a powerful method for chemical biology studies. However, it is still difficult to label intracellular proteins efficiently in living cells. We propose the novel design strategy of a reactive group-embedded affinity labeling reagent for efficient protein labeling. With FKBP12 as the model target protein, the ligand binding pocket-oriented labeling reagent could

  靶蛋白的亲和标记是化学生物学研究的有力方法。但是，仍然难以有效标记活细胞中的细胞内蛋白质。我们提出了一种新型的设计策略，即反应性嵌入基团的亲和标记试剂可以有效地进行蛋白质标记。以FKBP12为模型目标蛋白，配体结合型口袋定向标记试剂可以标记细胞内蛋白质，而蛋白质表面定向试剂则不能在活细胞中标记，部分原因是由于大分子拥挤效应下细胞内蛋白质的波动。这些结果为有效的细胞内蛋白质标记提供了新的见识。