(S)-4-tert-Butoxycarbonylamino-6-diazo-5-oxo-hexanoic acid tert-butyl ester | 61389-58-0

• 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)-4-tert-Butoxycarbonylamino-6-diazo-5-oxo-hexanoic acid tert-butyl ester
• CAS: 61389-58-0
• 化学式: C₁₅H₂₅N₃O₅
• 分子量: 327.381
• InChiKey: FYSMMDPQFFDRFM-JTQLQIEISA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.87
• 重原子数：
  23.0
• 可旋转键数：
  6.0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.73
• 拓扑面积：
  118.1
• 氢给体数：
  1.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  甲醇 、 (S)-4-tert-Butoxycarbonylamino-6-diazo-5-oxo-hexanoic acid tert-butyl ester 在 silver benzoate 、 三乙胺 作用下， 以 四氢呋喃 为溶剂， 反应 1.0h， 以1.89 g的产率得到(S)-3-tert-Butoxycarbonylamino-hexanedioic acid 6-tert-butyl ester 1-methyl ester
  参考文献：
  名称：

  2,4-Dinitrophenyl 4-Methoxybenzyl Disulfide:  A New Efficient Reagent for the Electrophilic Sulfenylation of β-Amino Ester Enolates

  摘要：

  DOI：

  10.1021/jo9623853
• 作为产物：
  描述：

  重氮甲烷 、 生成 (S)-4-tert-Butoxycarbonylamino-6-diazo-5-oxo-hexanoic acid tert-butyl ester
  参考文献：
  名称：

  Investigation of Subsite Preferences in Aminopeptidase A (EC 3.4.11.7) Led to the Design of the First Highly Potent and Selective Inhibitors of This Enzyme

  摘要：

  The study of the physiological roles of the membrane-bound zinc-aminopeptidase A (glutamyl aminopeptidase, EC 3.4.11.7) needs the design of efficient and selective inhibitors of this enzyme. An acute exploration of aminopeptidase A active site was performed by a combinatorial approach using (3-amino-2-mercapto-acyl)dipeptides able to sc its S-1, S-1', and S-2' subsites. This analysis confirmed that the S-1 subsite is optimally blocked by a glutamate or isosteric residues and demonstrated that the S-1' subsite is hydrophobic whereas the S-2' subsite recognizes preferentially negatively charged residues derived from aspartic acid. The optimization of these structural parameters led to the synthesis of nanomolar and subnanomolar inhibitors of aminopeptidase A such as H3N+CH(CH2CH2SO3-)CH(SH)CO-Ile-(3-COOH)Pro that exhibits a K-i of 0.87 nM. The best compounds were synthesized by a stereochemically controlled route. These first described highly potent inhibitors could allow studies about the role of physiological substrates of APA such as angiotensin II- and cholecystokinin CCK8 in the central nervous system.

  DOI：

  10.1021/jm9903040