Ac-D-Phe-L-Pro-OMe | 78663-61-3

• 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: Ac-D-Phe-L-Pro-OMe
• 英文别名: L-Proline, 1-(N-acetyl-D-phenylalanyl)-, methyl ester；methyl (2S)-1-[(2R)-2-acetamido-3-phenylpropanoyl]pyrrolidine-2-carboxylate
• CAS: 78663-61-3
• 化学式: C₁₇H₂₂N₂O₄
• 分子量: 318.373
• InChiKey: JTLJWLXDBYTJGZ-CABCVRRESA-N

物化性质

• 沸点：
  561.2±50.0 °C(Predicted)
• 密度：
  1.200±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.5
• 重原子数：
  23
• 可旋转键数：
  6
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.47
• 拓扑面积：
  75.7
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  N-乙酰-D-苯丙氨酸 、 L-脯氨酸甲酯盐酸盐 在 2-乙氧基-1-乙氧碳酰基-1,2-二氢喹啉 、 三乙胺 作用下， 以 甲醇 、 N,N-二甲基甲酰胺 为溶剂， 反应 24.0h， 生成 Ac-D-Phe-L-Pro-OMe
  参考文献：
  名称：

  15N NMR spectroscopy. 30—structure/shift relationships of oligopeptides and copolypeptides, including gramicidin S

  摘要：

  AbstractThe 15N NMR spectra of various oligopeptide derivatives of the ZXYYOMe structure, where X and Y are variable amino acids and Z is the benzyloxycarbonyl group, were measured in several protic and aprotic solvents. The shift difference of the 15N of the YY and XY bond (neighbouring residue effect) is discussed with respect to the nature of X and Y with respect to the solvent. Oligopeptides of the ZXYYOH and n̊H3XYYOMe structures were compared with the Z‐pëptide esters to investigate the spectroscopic influence of the protecting groups. The methyl ester hydrochlorides of the 25 most common amino acids were measured in water and DMSO to elucidate the solvent dependence of the substituent effects. Moreover, the methyl ester hydrochlorides were compared with Z‐amino acids and N‐acetyl‐amino acid methyl esters in DMSO to establish whether the substituent effects depend on the nature of the amino acid derivatives. In this connection the assignments of the serine, threonine and glycine signals are discussed with respect to silk proteins. Furthermore, the assignments of the signals of copolypeptides by comparison with oligo‐ and homo‐polypeptides are discussed. Finally, it was demonstrated that intramolecular H bonds cause downfied shifts of 7–10 ppm of the acceptor amide groups.

  DOI：

  10.1002/mrc.1270150211

文献信息

• 15N NMR spectroscopy. 30—structure/shift relationships of oligopeptides and copolypeptides, including gramicidin S
  作者：Hans R. Kricheldorf

  DOI：10.1002/mrc.1270150211

  日期：1981.2

  AbstractThe 15N NMR spectra of various oligopeptide derivatives of the ZXYYOMe structure, where X and Y are variable amino acids and Z is the benzyloxycarbonyl group, were measured in several protic and aprotic solvents. The shift difference of the 15N of the YY and XY bond (neighbouring residue effect) is discussed with respect to the nature of X and Y with respect to the solvent. Oligopeptides of the ZXYYOH and n̊H3XYYOMe structures were compared with the Z‐pëptide esters to investigate the spectroscopic influence of the protecting groups. The methyl ester hydrochlorides of the 25 most common amino acids were measured in water and DMSO to elucidate the solvent dependence of the substituent effects. Moreover, the methyl ester hydrochlorides were compared with Z‐amino acids and N‐acetyl‐amino acid methyl esters in DMSO to establish whether the substituent effects depend on the nature of the amino acid derivatives. In this connection the assignments of the serine, threonine and glycine signals are discussed with respect to silk proteins. Furthermore, the assignments of the signals of copolypeptides by comparison with oligo‐ and homo‐polypeptides are discussed. Finally, it was demonstrated that intramolecular H bonds cause downfied shifts of 7–10 ppm of the acceptor amide groups.