diethyl 2-<<(2,2,2-trichloroethoxy)carbonyl>amino>-2-(2-propenyl)malonate | 146395-30-4

• 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: diethyl 2-<<(2,2,2-trichloroethoxy)carbonyl>amino>-2-(2-propenyl)malonate
• CAS: 146395-30-4
• 化学式: C₁₃H₁₈Cl₃NO₆
• 分子量: 390.648
• InChiKey: YJAIMIIQVFKTAQ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.52
• 重原子数：
  23.0
• 可旋转键数：
  8.0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.62
• 拓扑面积：
  90.93
• 氢给体数：
  1.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  diethyl 2-<<(2,2,2-trichloroethoxy)carbonyl>amino>-2-(2-propenyl)malonate 在 N-甲基吗啉 、 4-二甲氨基吡啶 、 sodium hydroxide 、 三氯化铁 、 N,N'-二环己基碳二亚胺 、 锌 作用下， 以 四氢呋喃 、 乙醇 、 二氯甲烷 、 xylene 为溶剂， 反应 66.0h， 生成 oxy>-4-pentenoate>>glycyl>-(R)-alanine methyl ester
  参考文献：
  名称：

  Synthesis of modified partial structures of the bacterial cell wall. 1. Lipopeptides containing nonproteinogenic amino acids

  摘要：

  Two stereoisomeric lipopeptides 1 and 2 which can be regarded as modified peptidoglycans have been synthesized by using three different reaction sequences. The ene reaction of the alpha-allylated dipeptide 12 with butyl glyoxylate was used as a key step. The required enantiomerically pure substrates 9, 10, and 23 were obtained by enzymatic hydrolysis of the corresponding racemic alpha-allylated esters. The absolute configuration of both stereoisomers 1 and 2 was assigned by oxidative cleavage of the double bond in 18 and 19 followed by comparison of the esterified degradation products 28 and 29 with samples of authentic configuration, derived from (R)- and (S)-malic acid.

  DOI：

  10.1021/jo00055a022
• 作为产物：
  描述：

  氨基丙二酸二乙酯盐酸盐 在 N-甲基吗啉 、 sodium 作用下， 以 四氢呋喃 、 乙醇 为溶剂， 反应 6.0h， 生成 diethyl 2-<<(2,2,2-trichloroethoxy)carbonyl>amino>-2-(2-propenyl)malonate
  参考文献：
  名称：

  Synthesis of modified partial structures of the bacterial cell wall. 1. Lipopeptides containing nonproteinogenic amino acids

  摘要：

  Two stereoisomeric lipopeptides 1 and 2 which can be regarded as modified peptidoglycans have been synthesized by using three different reaction sequences. The ene reaction of the alpha-allylated dipeptide 12 with butyl glyoxylate was used as a key step. The required enantiomerically pure substrates 9, 10, and 23 were obtained by enzymatic hydrolysis of the corresponding racemic alpha-allylated esters. The absolute configuration of both stereoisomers 1 and 2 was assigned by oxidative cleavage of the double bond in 18 and 19 followed by comparison of the esterified degradation products 28 and 29 with samples of authentic configuration, derived from (R)- and (S)-malic acid.

  DOI：

  10.1021/jo00055a022