N-<1(S)-carbethoxybutyl>glycine | 130933-18-5

• 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: N-<1(S)-carbethoxybutyl>glycine
• 英文别名: 2-[[(2S)-1-ethoxy-1-oxopentan-2-yl]amino]acetic acid
• CAS: 130933-18-5
• 化学式: C₉H₁₇NO₄
• 分子量: 203.238
• InChiKey: WSWYYPYBBOZPPK-ZETCQYMHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.3
• 重原子数：
  14
• 可旋转键数：
  8
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.78
• 拓扑面积：
  75.6
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  N-<1(S)-carbethoxybutyl>glycine 在 palladium on activated charcoal sodium hydroxide 、 氢气 、 1-羟基苯并三唑 、 三乙胺 、 N,N'-二环己基碳二亚胺 作用下， 以 乙醇 、 N,N-二甲基甲酰胺 为溶剂， 25.0 ℃ 、294.18 kPa 条件下， 反应 110.0h， 生成 (2S,3aS,7aS)-1-glycinyl>-2-carboxyperhydroindole
  参考文献：
  名称：

  Configuration and preferential solid-state conformations of perindoprilat (S-9780). Comparison with the crystal structures of other ACE inhibitors and conclusions related to structure-activity relationships

  摘要：

  The conformation of perindoprilat, an antihypertensive drug, is studied in the solid state by X-ray analysis. The resolution of its structure reveals important analogies between its observed conformation and that of several ACE inhibitors of the same family. This comparison points out a constant relative orientation of the functional groups, regardless of the molecular environment. This angular constancy appears to us as not being accidental and is a good argument for the spatial design of the ACE binding site. Although ACE is a carboxydipeptidase, the binding site may not contain two but one unique hydrophobic pocket receiving the C-terminal end of the inhibitors.

  DOI：

  10.1021/jm00106a030
• 作为产物：
  描述：

  L-正缬氨酸乙酯盐酸盐 、 溴乙酸 在 三乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 6.0h， 生成 N-<1(S)-carbethoxybutyl>glycine 、 (S)-2-(Carboxymethyl-amino)-pentanoic acid ethyl ester; compound with ammonia
  参考文献：
  名称：

  Configuration and preferential solid-state conformations of perindoprilat (S-9780). Comparison with the crystal structures of other ACE inhibitors and conclusions related to structure-activity relationships

  摘要：

  The conformation of perindoprilat, an antihypertensive drug, is studied in the solid state by X-ray analysis. The resolution of its structure reveals important analogies between its observed conformation and that of several ACE inhibitors of the same family. This comparison points out a constant relative orientation of the functional groups, regardless of the molecular environment. This angular constancy appears to us as not being accidental and is a good argument for the spatial design of the ACE binding site. Although ACE is a carboxydipeptidase, the binding site may not contain two but one unique hydrophobic pocket receiving the C-terminal end of the inhibitors.

  DOI：

  10.1021/jm00106a030

文献信息

• Process for the preparation of high purity perindopril
  申请人：Simig Guyla

  公开号：US20070197821A1

  公开（公告）日：2007-08-23

  The invention relates to 1-2(S)-[1(S)-(ethoxycarbonyl)butylamino]propionyl}-(3aS,7aS)octahydroindol-2(S)-carboxylic acid of the Formula I and the t-butylamine salt of the Formula I′ thereof free of contaminations derivable from dicyclohexyl carbodiimide, and a process for the preparation thereof. The invention also relates to new intermediates of the general Formula III (wherein R stands for lower alkyl or aryl lower alkyl). The compound of the Formula I—perindopril—is a known ACE inhibitor.

  本发明涉及公式I的1-2(S)-[1(S)-(ethoxycarbonyl)butylamino]propionyl}-(3aS,7aS)八氢吲哚-2(S)-羧酸及其不含二环己基氨基甲酸酯污染物的t-丁基胺盐的制备方法。本发明还涉及一般公式III的新中间体（其中R代表低碳基或芳基低碳基）。公式I化合物perindopril是一种已知的ACE抑制剂。
• US7279595B2
  申请人：——

  公开号：US7279595B2

  公开（公告）日：2007-10-09
• Configuration and preferential solid-state conformations of perindoprilat (S-9780). Comparison with the crystal structures of other ACE inhibitors and conclusions related to structure-activity relationships
  作者：Claudine Pascard、Jean Guilhem、Michel Vincent、Georges Remond、Bernard Portevin、Michel Laubie

  DOI：10.1021/jm00106a030

  日期：1991.2

  The conformation of perindoprilat, an antihypertensive drug, is studied in the solid state by X-ray analysis. The resolution of its structure reveals important analogies between its observed conformation and that of several ACE inhibitors of the same family. This comparison points out a constant relative orientation of the functional groups, regardless of the molecular environment. This angular constancy appears to us as not being accidental and is a good argument for the spatial design of the ACE binding site. Although ACE is a carboxydipeptidase, the binding site may not contain two but one unique hydrophobic pocket receiving the C-terminal end of the inhibitors.