(S)-1-[3-(tert-Butyl-dimethyl-silanyloxy)-2,2-dimethyl-propylcarbamoyl]-piperidine-2-carboxylic acid benzyl ester | 175721-98-9

• 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: (S)-1-[3-(tert-Butyl-dimethyl-silanyloxy)-2,2-dimethyl-propylcarbamoyl]-piperidine-2-carboxylic acid benzyl ester
• 英文别名: benzyl (2S)-1-[[3-[tert-butyl(dimethyl)silyl]oxy-2,2-dimethylpropyl]carbamoyl]piperidine-2-carboxylate
• CAS: 175721-98-9
• 化学式: C₂₅H₄₂N₂O₄Si
• 分子量: 462.705
• InChiKey: MBUQESOUBMKTRJ-NRFANRHFSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.34
• 重原子数：
  32
• 可旋转键数：
  10
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.68
• 拓扑面积：
  67.9
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  (S)-1-[3-(tert-Butyl-dimethyl-silanyloxy)-2,2-dimethyl-propylcarbamoyl]-piperidine-2-carboxylic acid benzyl ester 在 triethylamine trihydrofluoride 作用下， 以 四氢呋喃 为溶剂， 反应 4.0h， 以76%的产率得到(S)-1-(3-Hydroxy-2,2-dimethyl-propylcarbamoyl)-piperidine-2-carboxylic acid benzyl ester
  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-氨基-2,2-二甲基-1-丙醇 在 4-二甲氨基吡啶 、 三乙胺 作用下， 以 二氯甲烷 为溶剂， 反应 4.0h， 生成 (S)-1-[3-(tert-Butyl-dimethyl-silanyloxy)-2,2-dimethyl-propylcarbamoyl]-piperidine-2-carboxylic acid benzyl ester
  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

文献信息

• Structure-Based Design of Novel, Urea-Containing FKBP12 Inhibitors
  作者：Peter S. Dragovich、John E. Barker、Judy French、Michael Imbacuan、Vincent J. Kalish、Charles R. Kissinger、Daniel R. Knighton、Cristina T. Lewis、Ellen W. Moomaw、Hans E. Parge、Laura A. K. Pelletier、Thomas J. Prins、Richard E. Showalter、John H. Tatlock、Kathleen D. Tucker、J. Ernest Villafranca

  DOI：10.1021/jm950798a

  日期：1996.1.1

  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.