Boc-PGGGG-OCH2Ph | 874306-13-5

• 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: Boc-PGGGG-OCH2Ph
• CAS: 874306-13-5
• 化学式: C₂₅H₃₅N₅O₈
• 分子量: 533.582
• InChiKey: NCVRGNWOLWUOLK-SFHVURJKSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.41
• 重原子数：
  38.0
• 可旋转键数：
  11.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.52
• 拓扑面积：
  172.24
• 氢给体数：
  4.0
• 氢受体数：
  8.0

反应信息

• 作为反应物：
  描述：

  Boc-PGGGG-OCH2Ph 在 盐酸 、 1-羟基苯并三唑一水物 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 、 三乙胺 作用下， 以 1,4-二氧六环 、 二氯甲烷 为溶剂， 反应 49.0h， 生成 [2-(2-{2-[(1-{2-[2-(2-dioctadecylcarbamoylmethoxyacetylamino)acetylamino]acetyl}pyrrolidine-2-carbonyl)amino]acetylamino}acetylamino)acetylamino]acetic acid benzyl ester
  参考文献：
  名称：

  Cation Dependence of Chloride Ion Complexation by Open-Chained Receptor Molecules in Chloroform Solution

  摘要：

  Seventeen peptides, most having the sequence GGGPGGG, but differing in the C- and N-terminal ends, have been studied as anion-complexing agents. These relatively simple, open-chained peptide systems interact with both chloride and the associated cation. Changes, in the N- and C-terminal side chains appear to make little difference in the efficacy of binding. NMR studies suggest that the primary interactions involve amide NH contacts with the chloride anion, and CD spectral analyses suggest a concomitant conformational change upon binding. Changes in binding constants, which are expected in different solvents, also suggest selective solvent interactions with the unbound host that helps to preorganize the open-chained peptide system. Significant differences are apparent in complexation strengths when the heptapeptide chain is shortened or lengthened or when the relative position of proline within the heptapeptide is varied.

  DOI：

  10.1021/ja0558894
• 作为产物：
  描述：

  Boc-GGGG-OCH2Ph 在 盐酸 、 1-羟基苯并三唑一水物 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 、 N,N-二异丙基乙胺 作用下， 以 1,4-二氧六环 、 二氯甲烷 为溶剂， 反应 49.0h， 生成 Boc-PGGGG-OCH2Ph
  参考文献：
  名称：

  Cation Dependence of Chloride Ion Complexation by Open-Chained Receptor Molecules in Chloroform Solution

  摘要：

  Seventeen peptides, most having the sequence GGGPGGG, but differing in the C- and N-terminal ends, have been studied as anion-complexing agents. These relatively simple, open-chained peptide systems interact with both chloride and the associated cation. Changes, in the N- and C-terminal side chains appear to make little difference in the efficacy of binding. NMR studies suggest that the primary interactions involve amide NH contacts with the chloride anion, and CD spectral analyses suggest a concomitant conformational change upon binding. Changes in binding constants, which are expected in different solvents, also suggest selective solvent interactions with the unbound host that helps to preorganize the open-chained peptide system. Significant differences are apparent in complexation strengths when the heptapeptide chain is shortened or lengthened or when the relative position of proline within the heptapeptide is varied.

  DOI：

  10.1021/ja0558894