Boc-DProΨPhe-methyl ester | 153484-02-7

• 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-DProΨPhe-methyl ester
• 英文别名: Boc-DProΨ(CH2NH)Phe-methyl ester；tert-butyl (2R)-2-[[[(2S)-1-methoxy-1-oxo-3-phenylpropan-2-yl]amino]methyl]pyrrolidine-1-carboxylate
• CAS: 153484-02-7
• 化学式: C₂₀H₃₀N₂O₄
• 分子量: 362.469
• InChiKey: JNEYLKCCAODZEK-SJORKVTESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.1
• 重原子数：
  26
• 可旋转键数：
  9
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.6
• 拓扑面积：
  67.9
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  Boc-DProΨPhe-methyl ester 在 sodium hydroxide 作用下， 以 四氢呋喃 、 甲醇 、 水 为溶剂， 反应 0.5h， 以60%的产率得到Boc-DProΨPhe-OH
  参考文献：
  名称：

  Potent Gastrin-Releasing Peptide (GRP) Antagonists Derived from GRP(19-27) with a C-Terminal DPro.PSI.[CH2NH]Phe-NH2 and N-Terminal Aromatic Residues

  摘要：

  We have previously reported that octapeptides with a -DPro Psi[CH2NH]Phe-NH2 C-terminus are potent GRP antagonists and have greatly enhanced in vivo stability. Now we report the detailed syntheses of such peptides and additional attempts to further increase metabolic stability. Replacement of the -DPro Psi[CH2NH]Phe-NH2 with a ''DPro-statine''-Phe-NH2 led to less potent antagonistic activity. The introduction of ThiAla and BzthAla, to replace His and Trp, respectively, did not increase activity. A series of analogs having different aromatic residues at the N-terminal, other than 3-phenylpropionic acid, are equally potent. These residues show increased activity when hydrophilic substitutions are added to the aromatic ring, Replacement of the C-terminal Phe by DPhe and D2Nal is tolerated. Even though none of these peptides have higher activity than the original lead peptide, they are potentially more metabolically stable.

  DOI：

  10.1021/jm00030a002
• 作为产物：
  描述：

  L-苯丙氨酸甲酯 在 platinum(IV) oxide 4 A molecular sieve 、 氢气 作用下， 以 甲醇 为溶剂， 反应 18.0h， 生成 Boc-DProΨPhe-methyl ester
  参考文献：
  名称：

  Potent Gastrin-Releasing Peptide (GRP) Antagonists Derived from GRP(19-27) with a C-Terminal DPro.PSI.[CH2NH]Phe-NH2 and N-Terminal Aromatic Residues

  摘要：

  We have previously reported that octapeptides with a -DPro Psi[CH2NH]Phe-NH2 C-terminus are potent GRP antagonists and have greatly enhanced in vivo stability. Now we report the detailed syntheses of such peptides and additional attempts to further increase metabolic stability. Replacement of the -DPro Psi[CH2NH]Phe-NH2 with a ''DPro-statine''-Phe-NH2 led to less potent antagonistic activity. The introduction of ThiAla and BzthAla, to replace His and Trp, respectively, did not increase activity. A series of analogs having different aromatic residues at the N-terminal, other than 3-phenylpropionic acid, are equally potent. These residues show increased activity when hydrophilic substitutions are added to the aromatic ring, Replacement of the C-terminal Phe by DPhe and D2Nal is tolerated. Even though none of these peptides have higher activity than the original lead peptide, they are potentially more metabolically stable.

  DOI：

  10.1021/jm00030a002

文献信息

• Potent Gastrin-Releasing Peptide (GRP) Antagonists Derived from GRP(19-27) with a C-Terminal DPro.PSI.[CH2NH]Phe-NH2 and N-Terminal Aromatic Residues
  作者：Johann J. Leban、Antonio Landavazo、John D. McDermed、Emanuel J. Diliberto、Marilyn Jansen、Beth Stockstill、Frederick C. Kull

  DOI：10.1021/jm00030a002

  日期：1994.2

  We have previously reported that octapeptides with a -DPro Psi[CH2NH]Phe-NH2 C-terminus are potent GRP antagonists and have greatly enhanced in vivo stability. Now we report the detailed syntheses of such peptides and additional attempts to further increase metabolic stability. Replacement of the -DPro Psi[CH2NH]Phe-NH2 with a ''DPro-statine''-Phe-NH2 led to less potent antagonistic activity. The introduction of ThiAla and BzthAla, to replace His and Trp, respectively, did not increase activity. A series of analogs having different aromatic residues at the N-terminal, other than 3-phenylpropionic acid, are equally potent. These residues show increased activity when hydrophilic substitutions are added to the aromatic ring, Replacement of the C-terminal Phe by DPhe and D2Nal is tolerated. Even though none of these peptides have higher activity than the original lead peptide, they are potentially more metabolically stable.