(2S)-1-(4-((benzyloxy)methoxy)-3,3-dimethyl-1,2-dioxobutyl)-2-piperidinecarboxylic acid | 152754-49-9

• 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: (2S)-1-(4-((benzyloxy)methoxy)-3,3-dimethyl-1,2-dioxobutyl)-2-piperidinecarboxylic acid
• 英文别名: (2S)-1-{4-[(benzyloxy)methoxy]-3,3-dimethyl-1,2-dioxobutyl}-2-piperidinecarboxylic acid
• CAS: 152754-49-9
• 化学式: C₂₀H₂₇NO₆
• 分子量: 377.437
• InChiKey: ZPABHZHEXKVECS-INIZCTEOSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.24
• 重原子数：
  27.0
• 可旋转键数：
  9.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.55
• 拓扑面积：
  93.14
• 氢给体数：
  1.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  (2S)-1-(4-((benzyloxy)methoxy)-3,3-dimethyl-1,2-dioxobutyl)-2-piperidinecarboxylic acid 在 4-二甲氨基吡啶 、 三氯化铝 、 D(+)-10-樟脑磺酸 、 N,N-二甲基苯胺 、 N,N'-二环己基碳二亚胺 作用下， 以 二氯甲烷 为溶剂， 反应 23.0h， 生成 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
• 作为产物：
  描述：

  ethyl (2S)-1-(4-((benzyloxy)methoxy)-3,3-dimethyl-1,2-dioxobutyl)-2-piperidinecarboxylate 在 lithium hydroxide 作用下， 以 甲醇 为溶剂， 反应 3.0h， 以100%的产率得到(2S)-1-(4-((benzyloxy)methoxy)-3,3-dimethyl-1,2-dioxobutyl)-2-piperidinecarboxylic acid
  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