12-hydroxy-12-oxo-1-dodecyl (2S)-1-(3,3-dimethyl-1,2-dioxo-4-hydroxybutyl)-2-piperidinecarboxylate | 152754-59-1

• 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: 12-hydroxy-12-oxo-1-dodecyl (2S)-1-(3,3-dimethyl-1,2-dioxo-4-hydroxybutyl)-2-piperidinecarboxylate
• CAS: 152754-59-1
• 化学式: C₂₄H₄₁NO₇
• 分子量: 455.592
• InChiKey: FYFIQPRXFZTAIC-IBGZPJMESA-N

物化性质

• 沸点：
  601.5±65.0 °C(predicted)
• 密度：
  1.129±0.06 g/cm3(Temp: 20 °C; Press: 760 Torr)(predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.48
• 重原子数：
  32.0
• 可旋转键数：
  16.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.83
• 拓扑面积：
  121.21
• 氢给体数：
  2.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  12-hydroxy-12-oxo-1-dodecyl (2S)-1-(3,3-dimethyl-1,2-dioxo-4-hydroxybutyl)-2-piperidinecarboxylate 在 4-二甲氨基吡啶 、 三乙胺 作用下， 以 四氢呋喃 、 甲苯 为溶剂， 反应 26.0h， 生成 (21S)-1-aza-4,4-dimethyl-6,19-dioxa-2,3,7,20-tetraoxobicyclo<19.4.0>pentacosane
  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：

  12-(benzyloxy)-12-oxo-1-dodecyl (2S)-1-(4-((benzyloxy)methoxy)-3,3-dimethyl-1,2-dioxobutyl)-2-piperidinecarboxylate 在 三氯化铝 、 N,N-二甲基苯胺 作用下， 以 二氯甲烷 为溶剂， 反应 5.0h， 以44%的产率得到12-hydroxy-12-oxo-1-dodecyl (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