(S)-3-Amino-6-(2,5-dimethyl-phenyl)-4-oxo-hexanoic acid tert-butyl ester | 863667-07-6

• 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)-3-Amino-6-(2,5-dimethyl-phenyl)-4-oxo-hexanoic acid tert-butyl ester
• CAS: 863667-07-6
• 化学式: C₁₈H₂₇NO₃
• 分子量: 305.417
• InChiKey: JKWNFPAYMYAQNO-HNNXBMFYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.86
• 重原子数：
  22.0
• 可旋转键数：
  6.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.56
• 拓扑面积：
  69.39
• 氢给体数：
  1.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  (S)-3-Amino-6-(2,5-dimethyl-phenyl)-4-oxo-hexanoic acid tert-butyl ester 在 benzotriazol-1-yloxyl-tris-(pyrrolidino)-phosphonium hexafluorophosphate 、 N,N-二异丙基乙胺 、 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 2.17h， 生成 (S)-3-{(S)-2-[(S)-2-((S)-2-Acetylamino-3-carboxy-propionylamino)-4-carboxy-butyrylamino]-3-methyl-butyrylamino}-6-(2,5-dimethyl-phenyl)-4-oxo-hexanoic acid
  参考文献：
  名称：

  Using Peptidic Inhibitors to Systematically Probe the S1‘ Site of Caspase-3 and Caspase-7

  摘要：

  Fifteen ketone-containing peptides were designed, synthesized, and used to probe the effect of substitution at the P1' position on caspase-3 and -7 inhibition. Even with the large bias of Ac-Asp-Glu-Val-Asp at the P4-P1 positions, certain peptides with cyclic functionality in the P1' position show a dramatically reduced ability to inhibit these caspases. Additionally, trends toward isozyme selectivity were also uncovered for particular P1' substituents. The data indicate that substitution in the P1' position can drastically affect both caspase inhibition and selectivity.

  DOI：

  10.1021/ol051287d
• 作为产物：
  描述：

  tert-butyl (3S)-3-(9H-fluoren-9-ylmethoxycarbonylamino)-4-oxo-4-pyridin-2-ylsulfanylbutanoate 在 哌啶 、 copper(l) iodide 作用下， 以 四氢呋喃 、 N,N-二甲基甲酰胺 为溶剂， 反应 0.33h， 生成 (S)-3-Amino-6-(2,5-dimethyl-phenyl)-4-oxo-hexanoic acid tert-butyl ester
  参考文献：
  名称：

  Using Peptidic Inhibitors to Systematically Probe the S1‘ Site of Caspase-3 and Caspase-7

  摘要：

  Fifteen ketone-containing peptides were designed, synthesized, and used to probe the effect of substitution at the P1' position on caspase-3 and -7 inhibition. Even with the large bias of Ac-Asp-Glu-Val-Asp at the P4-P1 positions, certain peptides with cyclic functionality in the P1' position show a dramatically reduced ability to inhibit these caspases. Additionally, trends toward isozyme selectivity were also uncovered for particular P1' substituents. The data indicate that substitution in the P1' position can drastically affect both caspase inhibition and selectivity.

  DOI：

  10.1021/ol051287d