Boc-Dmaa-D-pro-Aic-Ser(Bn)-NMe₂ | 1562416-55-0

• 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: Boc-Dmaa-D-pro-Aic-Ser(Bn)-NMe₂
• CAS: 1562416-55-0
• 化学式: C₃₇H₅₂N₆O₇
• 分子量: 692.856
• InChiKey: LNUZLSOZUYSSFB-OIFRRMEBSA-N

物化性质

• 沸点：
  912.1±65.0 °C(Predicted)
• 密度：
  1.24±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.88
• 重原子数：
  50.0
• 可旋转键数：
  13.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.54
• 拓扑面积：
  149.62
• 氢给体数：
  3.0
• 氢受体数：
  8.0

反应信息

• 作为产物：
  描述：

  N-BOC-O-苄基-L-丝氨酸 在 盐酸 、 1-羟基苯并三唑 、 O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 、 N,N-二异丙基乙胺 作用下， 以 1,4-二氧六环 、 二氯甲烷 为溶剂， 反应 139.0h， 生成 Boc-Dmaa-D-pro-Aic-Ser(Bn)-NMe₂
  参考文献：
  名称：

  Peptide-Catalyzed Conversion of Racemic Oxazol-5(4H)-ones into Enantiomerically Enriched α-Amino Acid Derivatives

  摘要：

  We report the development and optimization of a tetrapeptide that catalyzes the methanolytic dynamic kinetic resolution of oxazol-5(4H)-ones (azlactones) with high levels of enantioinduction. Oxazolones possessing benzylic-type substituents were found to perform better than others, providing methyl ester products in 88:12 to 98:2 er. The mechanism of this peptide-catalyzed process was investigated through truncation studies and competition experiments. High-field NOESY analysis was performed to elucidate the solution-phase structure of the peptide, and we present a plausible model for catalysis.

  DOI：

  10.1021/jo402828f
• 作为试剂：
  描述：

  N-苯甲酰-N-缬氨酸 在 Boc-Dmaa-D-pro-Aic-Ser(Bn)-NMe₂ 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 作用下， 以 二氯甲烷 、 甲苯 为溶剂， 反应 24.0h， 生成 (2R)-2-(benzoylamino)-3-methylbutyric acid methyl ester 、 N-benzoyl-L-valine methyl ester
  参考文献：
  名称：

  Peptide-Catalyzed Conversion of Racemic Oxazol-5(4H)-ones into Enantiomerically Enriched α-Amino Acid Derivatives

  摘要：

  We report the development and optimization of a tetrapeptide that catalyzes the methanolytic dynamic kinetic resolution of oxazol-5(4H)-ones (azlactones) with high levels of enantioinduction. Oxazolones possessing benzylic-type substituents were found to perform better than others, providing methyl ester products in 88:12 to 98:2 er. The mechanism of this peptide-catalyzed process was investigated through truncation studies and competition experiments. High-field NOESY analysis was performed to elucidate the solution-phase structure of the peptide, and we present a plausible model for catalysis.

  DOI：

  10.1021/jo402828f