H-Gly-Val-NH2 | 89315-03-7

• 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: H-Gly-Val-NH2
• 英文别名: N-glycyl-L-valine amide；Glycyl-valine amide；(2S)-2-[(2-aminoacetyl)amino]-3-methylbutanamide
• CAS: 89315-03-7
• 化学式: C₇H₁₅N₃O₂
• 分子量: 173.215
• InChiKey: LHEGGRARBGJKNS-LURJTMIESA-N

物化性质

• 沸点：
  429.5±30.0 °C(Predicted)
• 密度：
  1.115±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -1.5
• 重原子数：
  12
• 可旋转键数：
  4
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.71
• 拓扑面积：
  98.2
• 氢给体数：
  3
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  H-Gly-Val-NH2 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-二异丙基乙胺 、 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 Boc-Tyr-D-Ala-Phe-Asp(OtBu)(OtBu)-Val-Gly-Val-NH2
  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：

  L-缬氨酸酰胺 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 H-Gly-Val-NH2
  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

• Enzymatic Fragment Condensation of Side Chain-Protected Peptides using Subtilisin A in Anhydrous Organic Solvents: A General Strategy for Industrial Peptide Synthesis
  作者：Timo Nuijens、Annette H. M. Schepers、Claudia Cusan、John A. W. Kruijtzer、Dirk T. S. Rijkers、Rob M. J. Liskamp、Peter J. L. M. Quaedflieg

  DOI：10.1002/adsc.201200694

  日期：2013.1.4

  Herein, the enzymatic condensation of side chain-protected peptide fragments using subtilisin A in anhydrous organic solvents is described. A screening with dipeptide Cbz-Val-Xxx carboxamidomethyl esters with H-Xxx-Val-NH2 nucleophiles was performed, wherein Xxx stands for every (side chain-protected) amino acid residue. Finally, it was demonstrated that it is feasible to enzymatically condense larger

  在此，描述了在无水有机溶剂中使用枯草杆菌蛋白酶A对侧链保护的肽片段进行酶促缩合。用具有H-Xxx-Val-NH 2亲核试剂的二肽Cbz-Val-Xxx羧酰胺甲基酯进行了筛选，其中Xxx代表每个（侧链保护的）氨基酸残基。最后，证明了用酶法以很高的转化率缩合带有多个侧链保护基团的较大的肽片段（至多10个聚合物的水平）是可行的。
• Engelfried,C. et al., Liebigs Annalen der Chemie, 1979, p. 973 - 985
  作者：Engelfried,C. et al.

  DOI：——

  日期：——
• 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.