12-(benzyloxy)-12-oxo-1-dodecyl (2S)-1-(4-((benzyloxy)methoxy)-3,3-dimethyl-1,2-dioxobutyl)-2-piperidinecarboxylate | 152754-51-3

• 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-(benzyloxy)-12-oxo-1-dodecyl (2S)-1-(4-((benzyloxy)methoxy)-3,3-dimethyl-1,2-dioxobutyl)-2-piperidinecarboxylate
• 英文别名: 12-(benzyloxy)-12-oxo-1-dodecyl (2S)-1-{4-[(benzyloxy)methoxy]-3,3-dimethyl-1,2-dioxobutyl}-2-piperidinecarboxylate
• CAS: 152754-51-3
• 化学式: C₃₉H₅₅NO₈
• 分子量: 665.868
• InChiKey: YCZVPFTUODJLRO-UMSFTDKQSA-N

物化性质

• 沸点：
  713.8±70.0 °C(predicted)
• 密度：
  1.112±0.06 g/cm3(Temp: 20 °C; Press: 760 Torr)(predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  7.34
• 重原子数：
  48.0
• 可旋转键数：
  23.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.59
• 拓扑面积：
  108.44
• 氢给体数：
  0.0
• 氢受体数：
  8.0

反应信息

• 作为反应物：
  描述：

  12-(benzyloxy)-12-oxo-1-dodecyl (2S)-1-(4-((benzyloxy)methoxy)-3,3-dimethyl-1,2-dioxobutyl)-2-piperidinecarboxylate 在 4-二甲氨基吡啶 、 三氯化铝 、 N,N-二甲基苯胺 、 三乙胺 作用下， 以 四氢呋喃 、 二氯甲烷 、 甲苯 为溶剂， 反应 31.0h， 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：

  溴甲苯 在 4-二甲氨基吡啶 、 D(+)-10-樟脑磺酸 、 potassium hydrogencarbonate 、 N,N'-二环己基碳二亚胺 作用下， 以 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 36.0h， 生成 12-(benzyloxy)-12-oxo-1-dodecyl (2S)-1-(4-((benzyloxy)methoxy)-3,3-dimethyl-1,2-dioxobutyl)-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