N-t-Boc-Leu-(p-MeOBzl)Cys-OMe | 97721-57-8

• 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-t-Boc-Leu-(p-MeOBzl)Cys-OMe
• CAS: 97721-57-8
• 化学式: C₂₃H₃₆N₂O₆S
• 分子量: 468.615
• InChiKey: QYQONQADCHKQEM-OALUTQOASA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.53
• 重原子数：
  32.0
• 可旋转键数：
  11.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.61
• 拓扑面积：
  102.96
• 氢给体数：
  2.0
• 氢受体数：
  7.0

反应信息

• 作为反应物：
  描述：

  N-t-Boc-Leu-(p-MeOBzl)Cys-OMe 在 N-甲基吗啉 、 氨 作用下， 以 甲醇 、 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 120.75h， 生成 N-Z-(S-Bzl)Cys-Gln-Phe-Phe-Gly-Leu-(p-MeOBzl)Cys-NH2
  参考文献：
  名称：

  Conformationally restricted C-terminal peptides of substance P. Synthesis, mass spectral analysis and pharmacological properties

  摘要：

  Four cyclic analogues of the C-terminal hepta- or hexapeptide of substance P were prepared by the solution method. The cyclizations were obtained by substituting with cysteine the residues normally present in positions 5 or 6 or 11 of substance P and by subsequent disulfide bond formation. The final products were identified by ordinary analytical procedures and advanced mass spectroscopy. The biological activities were determined on three bioassays: the guinea pig ileum, the guinea pig trachea and the rabbit mesenteric vein. Results obtained with these assays indicate that all peptides with a disulfide bridgehead in position 11 are inactive and that a cycle between positions 5 and 6 already strongly reduces the biological activity. The acyclic precursors containing thiol protection groups display weak biological activities. These results further underline the importance of the side chain in position 11 of substance P and suggest that optimal biological activities may require a linear peptide sequence.

  DOI：

  10.1021/jm00148a029
• 作为产物：
  描述：

  BOC-L-亮氨酸 、 S-<(4-methoxyphenyl)methyl>-L-cysteine methyl ester hydrochloride 在 N-甲基吗啉 、 N,N'-二环己基碳二亚胺 作用下， 以 二氯甲烷 为溶剂， 以66%的产率得到N-t-Boc-Leu-(p-MeOBzl)Cys-OMe
  参考文献：
  名称：

  Conformationally restricted C-terminal peptides of substance P. Synthesis, mass spectral analysis and pharmacological properties

  摘要：

  Four cyclic analogues of the C-terminal hepta- or hexapeptide of substance P were prepared by the solution method. The cyclizations were obtained by substituting with cysteine the residues normally present in positions 5 or 6 or 11 of substance P and by subsequent disulfide bond formation. The final products were identified by ordinary analytical procedures and advanced mass spectroscopy. The biological activities were determined on three bioassays: the guinea pig ileum, the guinea pig trachea and the rabbit mesenteric vein. Results obtained with these assays indicate that all peptides with a disulfide bridgehead in position 11 are inactive and that a cycle between positions 5 and 6 already strongly reduces the biological activity. The acyclic precursors containing thiol protection groups display weak biological activities. These results further underline the importance of the side chain in position 11 of substance P and suggest that optimal biological activities may require a linear peptide sequence.

  DOI：

  10.1021/jm00148a029