2-(3-{N'-[3-(3,4-dimethoxyphenyl)-2-(9H-fluoren-9-ylmethoxycarbonylamino)propionyl]hydrazino}-4,4,4-trifluorobutyrylamino)-3-phenylpropionic acid methyl ester | 1123546-35-9

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 肽模拟物
• 英文名称: 2-(3-{N'-[3-(3,4-dimethoxyphenyl)-2-(9H-fluoren-9-ylmethoxycarbonylamino)propionyl]hydrazino}-4,4,4-trifluorobutyrylamino)-3-phenylpropionic acid methyl ester
• CAS: 1123546-35-9
• 化学式: C₄₀H₄₁F₃N₄O₈
• 分子量: 762.783
• InChiKey: YTUPDZXVPDAYDW-SVYHFPLZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.0
• 重原子数：
  55.0
• 可旋转键数：
  16.0
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.3
• 拓扑面积：
  153.32
• 氢给体数：
  4.0
• 氢受体数：
  9.0

反应信息

• 作为反应物：
  描述：

  2-(3-{N'-[3-(3,4-dimethoxyphenyl)-2-(9H-fluoren-9-ylmethoxycarbonylamino)propionyl]hydrazino}-4,4,4-trifluorobutyrylamino)-3-phenylpropionic acid methyl ester 在 哌啶 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 1.3h， 以84%的产率得到2-(3-{N'-[2-amino-3-(3,4-dimethoxyphenyl)propionyl]hydrazino}-4,4,4-trifluorobutyrylamino)-3-phenylpropionic acid methyl ester
  参考文献：
  名称：

  Novel fluorinated pseudopeptides as proteasome inhibitors

  摘要：

  We have designed novel small inhibitors of rabbit 20S proteasome using a trifluoromethyl-beta-hydrazino acid scaffold. Structural variations influenced their inhibition of the three types of active sites. Proteasome inhibition at the micromolar level was selective, calpain I and cathepsin B were not inhibited. (C) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2008.11.012
• 作为产物：
  描述：

  3-phenyl-2-(4,4,4-trifluoro-3-hydrazinobutyrylamino)propionic acid methyl ester trifluoroacetic acid salt 、 FMOC-L-3,4-二甲氧基苯基丙氨酸 在 2,4,6-三甲基吡啶 、 1-羟基苯并三唑 、 O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 21.0h， 以22%的产率得到2-(3-{N'-[3-(3,4-dimethoxyphenyl)-2-(9H-fluoren-9-ylmethoxycarbonylamino)propionyl]hydrazino}-4,4,4-trifluorobutyrylamino)-3-phenylpropionic acid methyl ester
  参考文献：
  名称：

  Novel fluorinated pseudopeptides as proteasome inhibitors

  摘要：

  We have designed novel small inhibitors of rabbit 20S proteasome using a trifluoromethyl-beta-hydrazino acid scaffold. Structural variations influenced their inhibition of the three types of active sites. Proteasome inhibition at the micromolar level was selective, calpain I and cathepsin B were not inhibited. (C) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2008.11.012