Z-Val-Val-Gly-OtBu | 56610-26-5

• 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: Z-Val-Val-Gly-OtBu
• 英文别名: Cbz-Val-Val-Gly-OtBu；tert-butyl 2-[[(2S)-3-methyl-2-[[(2S)-3-methyl-2-(phenylmethoxycarbonylamino)butanoyl]amino]butanoyl]amino]acetate
• CAS: 56610-26-5
• 化学式: C₂₄H₃₇N₃O₆
• 分子量: 463.574
• InChiKey: HFDITGPGAUCUPG-PMACEKPBSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.8
• 重原子数：
  33
• 可旋转键数：
  13
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.58
• 拓扑面积：
  123
• 氢给体数：
  3
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  Z-Val-Val-Gly-OtBu 在 palladium on activated charcoal N-甲基吗啉 、 氢气 、 N-甲基吗啉盐酸盐 、 1-羟基苯并三唑 、 N,N'-二环己基碳二亚胺 作用下， 以 溶剂黄146 、 N,N-二甲基甲酰胺 、 异丙醇 为溶剂， -10.0~25.0 ℃ 、101.33 kPa 条件下， 反应 30.0h， 生成 Cbz-Tyr-D-Ala-Phe-Asp(OtBu)-Val-Val-Gly-OtBu
  参考文献：
  名称：

  Unique sequence in deltorphin C confers structural requirement for δ opioid receptor selectivity

  摘要：

  A series of deltorphin C (H-Tyr-D-Ala-Phe-Asp-Val-Val-Gly-NH2) analogues were synthesized to assess the consequences of changing anionic and hydrophobic residues on delta receptor selectivity. Analogues with altered C-terminal groups, inverted sequences, or esterified with tert-butyl, benzyl, or ethyl groups revealed that high delta selectivity required an unmodified amino acid sequence. Shifts of Asp and hydrophobic residues decreased delta selectivity due to loss in delta affinity (5- to almost-equal-to 700-fold); mu affinity was unchanged or increased 14-fold. Suppression of charge or deamidation diminished delta selectivity through reduced delta and modified mu affinities. Data provide evidence that a negative charge does not a priori guarantee high selectivity and specific alignment of anionic and hydrophobic residues might facilitate optimum spatial configuration which complements the 8 receptor binding site.

  DOI：

  10.1016/0223-5234(92)90113-f
• 作为产物：
  描述：

  甘氨酸叔丁酯 在 palladium on activated charcoal 氢气 、 1-羟基苯并三唑 、 N,N-二异丙基乙胺 作用下， 以 溶剂黄146 、 N,N-二甲基甲酰胺 、 异丙醇 为溶剂， 25.0 ℃ 、101.33 kPa 条件下， 生成 Z-Val-Val-Gly-OtBu
  参考文献：
  名称：

  Unique sequence in deltorphin C confers structural requirement for δ opioid receptor selectivity

  摘要：

  A series of deltorphin C (H-Tyr-D-Ala-Phe-Asp-Val-Val-Gly-NH2) analogues were synthesized to assess the consequences of changing anionic and hydrophobic residues on delta receptor selectivity. Analogues with altered C-terminal groups, inverted sequences, or esterified with tert-butyl, benzyl, or ethyl groups revealed that high delta selectivity required an unmodified amino acid sequence. Shifts of Asp and hydrophobic residues decreased delta selectivity due to loss in delta affinity (5- to almost-equal-to 700-fold); mu affinity was unchanged or increased 14-fold. Suppression of charge or deamidation diminished delta selectivity through reduced delta and modified mu affinities. Data provide evidence that a negative charge does not a priori guarantee high selectivity and specific alignment of anionic and hydrophobic residues might facilitate optimum spatial configuration which complements the 8 receptor binding site.

  DOI：

  10.1016/0223-5234(92)90113-f

文献信息

• Unique sequence in deltorphin C confers structural requirement for δ opioid receptor selectivity
  作者：LH Lazarus、S Salvadori、P Grieco、WE Wilson、R Tomatis

  DOI：10.1016/0223-5234(92)90113-f

  日期：1992.11

  A series of deltorphin C (H-Tyr-D-Ala-Phe-Asp-Val-Val-Gly-NH2) analogues were synthesized to assess the consequences of changing anionic and hydrophobic residues on delta receptor selectivity. Analogues with altered C-terminal groups, inverted sequences, or esterified with tert-butyl, benzyl, or ethyl groups revealed that high delta selectivity required an unmodified amino acid sequence. Shifts of Asp and hydrophobic residues decreased delta selectivity due to loss in delta affinity (5- to almost-equal-to 700-fold); mu affinity was unchanged or increased 14-fold. Suppression of charge or deamidation diminished delta selectivity through reduced delta and modified mu affinities. Data provide evidence that a negative charge does not a priori guarantee high selectivity and specific alignment of anionic and hydrophobic residues might facilitate optimum spatial configuration which complements the 8 receptor binding site.