(2R)-2-(2-(acetylamino)acetylamino)-N-benzyl-3-phenylpropionamide

• 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: (2R)-2-(2-(acetylamino)acetylamino)-N-benzyl-3-phenylpropionamide
• 英文别名: 2(R)-(2-acetylamino-acetylamino)-N-benzyl-3-phenyl-propionamide；(2R)-2-[(2-acetamidoacetyl)amino]-N-benzyl-3-phenylpropanamide
• 化学式: C₂₀H₂₃N₃O₃
• 分子量: 353.421
• InChiKey: YDOXEZCTWBZHKM-GOSISDBHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.3
• 重原子数：
  26
• 可旋转键数：
  8
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.25
• 拓扑面积：
  87.3
• 氢给体数：
  3
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  D-苯丙氨酸 在 copper(I) sulfate 、 triflic azide 、 1-羟基苯并三唑 、 N,N'-二环己基碳二亚胺 作用下， 以 四氢呋喃 、 二氯甲烷 、 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 15.0h， 生成 (2R)-2-(2-(acetylamino)acetylamino)-N-benzyl-3-phenylpropionamide
  参考文献：
  名称：

  Staudinger Ligation of α-Azido Acids Retains Stereochemistry

  摘要：

  The Staudinger ligation of peptides with a C-terminal phosphinothioester and N-terminal azide is an emerging method in protein chemistry. Here, the first Staudinger ligations of nonglycyl azides are reported and shown to proceed both in nearly quantitative yield and with no detectable effect on the stereochemistry at the a-carbon of the azide. These results demonstrate further the potential of the Staudinger ligation as a general method for the total synthesis of proteins from peptide fragments.

  DOI：

  10.1021/jo025631l

文献信息

• [EN] CHEMICAL SYNTHESIS OF REAGENTS FOR PEPTIDE COUPLING<br/>[FR] SYNTHESE CHIMIQUE DE REACTIFS POUR COUPLAGE PEPTIDIQUE
  申请人：WISCONSIN ALUMNI RES FOUND

  公开号：WO2003104243A1

  公开（公告）日：2003-12-18

  The present invention provides improved methods for synthesis of phosphinothiol reagents, as well as novel protected reagents, for use in formation of amide bonds, and particularly for peptide ligation. The invention provides phosphineborane complexes useful as reagents in the formation of amide bonds, particularly for the formation of an amide bond between any two of an amino acid, a peptide, or a protein.

  本发明提供了改进的磷硫脂试剂合成方法，以及用于形成酰胺键的新型保护试剂，特别是用于肽连接的。该发明提供了磷硼烷络合物，可用作形成酰胺键的试剂，特别是用于在氨基酸、肽或蛋白质中的任意两者之间形成酰胺键。
• Staudinger Ligation of α-Azido Acids Retains Stereochemistry
  作者：Matthew B. Soellner、Bradley L. Nilsson、Ronald T. Raines

  DOI：10.1021/jo025631l

  日期：2002.7.1

  The Staudinger ligation of peptides with a C-terminal phosphinothioester and N-terminal azide is an emerging method in protein chemistry. Here, the first Staudinger ligations of nonglycyl azides are reported and shown to proceed both in nearly quantitative yield and with no detectable effect on the stereochemistry at the a-carbon of the azide. These results demonstrate further the potential of the Staudinger ligation as a general method for the total synthesis of proteins from peptide fragments.