[(1R,6S)-8-oxo-7-azabicyclo[4.2.0]octan-7-yl]methyl butanoate | 285560-90-9

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: [(1R,6S)-8-oxo-7-azabicyclo[4.2.0]octan-7-yl]methyl butanoate
• CAS: 285560-90-9
• 化学式: C₁₂H₁₉NO₃
• 分子量: 225.288
• InChiKey: QULRZOUZEZTQEU-ZJUUUORDSA-N

物化性质

• 沸点：
  366.4±25.0 °C(Predicted)
• 密度：
  1.120±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.7
• 重原子数：
  16
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.83
• 拓扑面积：
  46.6
• 氢给体数：
  0
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  [(1R,6S)-8-oxo-7-azabicyclo[4.2.0]octan-7-yl]methyl butanoate 在 盐酸 作用下， 反应 2.0h， 以0.07 g的产率得到2-氨基-(1R,2S)-环己烷羧酸
  参考文献：
  名称：

  Enzymatic resolution of alicyclic β-lactams

  摘要：

  Racemates of N-hydroxymethylated beta-lactams 4-6 were resolved through the lipase-catalyzed asymmetric acylation of the primary hydroxy group at the 6S stereogenic centre. High enantioselectivity (E > 200) was observed when the enzymatic reactions were performed in acetone with lipase PS as catalyst and vinyl butyrate as acyl donor. The hydrolysis of the enantiomeric azetidinones 4a-6a and 4b-6b resulted in the enantiomerically pure alicyclic beta-amino acids 4c-6c and 4d-6d. When the less reactive enantiomers 4b-6b were treated with NH4OH/MeOH, enantiomerically pure beta-lactams 4e-6e were formed. (C) 2000 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0957-4166(00)00070-7
• 作为产物：
  描述：

  环己烯 在 potassium carbonate 作用下， 以 二氯甲烷 、 水 、 丙酮 为溶剂， 反应 36.0h， 生成 [(1R,6S)-8-oxo-7-azabicyclo[4.2.0]octan-7-yl]methyl butanoate
  参考文献：
  名称：

  Hairpin Folding Behavior of Mixed α/β-Peptides in Aqueous Solution

  摘要：

  The invention of new strategies for the design of protein-mimetic oligomers that manifest the folding encoded in natural amino acid sequences is a significant challenge. In contrast to the a-helix, mimicry of protein beta-sheets is less understood. We report here the aqueous folding behavior of a prototype alpha-peptide hairpin model sequence varied at cross-strand positions by incorporation of 16 different beta-amino acid monomers. Our results provide a folding propensity scale for beta-residues in a protein beta-sheet context as well as high-resolution structures of several mixed-backbone alpha/beta-peptide hairpins in water.

  DOI：

  10.1021/ja2002346