(2S)-piperidine-1,2-dicarboxylic acid 1-tert-butyl 2-<3'-(3-methoxyphenyl)propyl> diester | 175721-88-7

• 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)-piperidine-1,2-dicarboxylic acid 1-tert-butyl 2-<3'-(3-methoxyphenyl)propyl> diester
• 英文别名: 1-O-tert-butyl 2-O-[3-(3-methoxyphenyl)propyl] (2S)-piperidine-1,2-dicarboxylate
• CAS: 175721-88-7
• 化学式: C₂₁H₃₁NO₅
• 分子量: 377.481
• InChiKey: PCVGWBVHYPVPLU-SFHVURJKSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.2
• 重原子数：
  27
• 可旋转键数：
  9
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.62
• 拓扑面积：
  65.1
• 氢给体数：
  0
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  (2S)-piperidine-1,2-dicarboxylic acid 1-tert-butyl 2-<3'-(3-methoxyphenyl)propyl> diester 在 盐酸 、 三乙胺 作用下， 以 1,4-二氧六环 、 二氯甲烷 为溶剂， 反应 3.0h， 生成 3-(3-methoxyphenyl)propyl (2S)-1-(2,2-dimethylpropylcarbamoyl)piperidine-2-carboxylate
  参考文献：
  名称：

  Structure-Based Design of Novel, Urea-Containing FKBP12 Inhibitors

  摘要：

  The structure-based design and subsequent chemical synthesis of novel, urea-containing FKBP12 inhibitors are described. These compounds are shown to disrupt the cis-trans peptidylprolyl isomerase activity of FKBP12 with inhibition constants (K-i,K-app) approaching 0.10 mu M. Analyses of several X-ray crystal structures of FKBP12-urea complexes demonstrate that the urea-containing inhibitors associate with FKBP12 in a manner that is similar to, but significantly different from, that observed for the natural product FK506.

  DOI：

  10.1021/jm950798a
• 作为产物：
  描述：

  3-(3-甲氧基苯基)-1-丙醇 、 N-Boc-L-哌啶-2-羧酸 在 4-二甲氨基吡啶 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 作用下， 以 二氯甲烷 为溶剂， 反应 3.0h， 生成 (2S)-piperidine-1,2-dicarboxylic acid 1-tert-butyl 2-<3'-(3-methoxyphenyl)propyl> diester
  参考文献：
  名称：

  Structure-Based Design of Novel, Urea-Containing FKBP12 Inhibitors

  摘要：

  The structure-based design and subsequent chemical synthesis of novel, urea-containing FKBP12 inhibitors are described. These compounds are shown to disrupt the cis-trans peptidylprolyl isomerase activity of FKBP12 with inhibition constants (K-i,K-app) approaching 0.10 mu M. Analyses of several X-ray crystal structures of FKBP12-urea complexes demonstrate that the urea-containing inhibitors associate with FKBP12 in a manner that is similar to, but significantly different from, that observed for the natural product FK506.

  DOI：

  10.1021/jm950798a