(S)-1-[3,3-Dimethyl-2-oxo-4-(tetrahydro-pyran-2-yloxy)-butyryl]-piperidine-2-carboxylic acid | 155399-03-4

• 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: (S)-1-[3,3-Dimethyl-2-oxo-4-(tetrahydro-pyran-2-yloxy)-butyryl]-piperidine-2-carboxylic acid
• CAS: 155399-03-4
• 化学式: C₁₇H₂₇NO₆
• 分子量: 341.404
• InChiKey: PDOYEMRHSBZFCV-UEWDXFNNSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.59
• 重原子数：
  24.0
• 可旋转键数：
  6.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.82
• 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：

  (S)-1-[3,3-Dimethyl-2-oxo-4-(tetrahydro-pyran-2-yloxy)-butyryl]-piperidine-2-carboxylic acid 在 4-二甲氨基吡啶 、 三乙胺 、 三氟乙酸 作用下， 以 四氢呋喃 、 二氯甲烷 、 甲苯 、 苯 为溶剂， 反应 28.0h， 生成 (2R,5S)-13,13-dimethyl-2-(2-phenylethyl)-3,15,23-trioxa-10-azatricyclo[22.3.1.05,10]octacosa-1(28),24,26-triene-4,11,12,16-tetrone
  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-(3,3-dimethyl-1,2-dioxo-4-hydroxybutyl)-2-piperidinecarboxylate 在 lithium hydroxide 、 对甲苯磺酸 作用下， 以 四氢呋喃 、 甲醇 为溶剂， 反应 2.0h， 生成 (S)-1-[3,3-Dimethyl-2-oxo-4-(tetrahydro-pyran-2-yloxy)-butyryl]-piperidine-2-carboxylic 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