AHH

• 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: AHH
• 英文别名: Ala-His-His；(2S)-2-[[(2S)-2-[[(2S)-2-aminopropanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]-3-(1H-imidazol-5-yl)propanoic acid
• 化学式: C₁₅H₂₁N₇O₄
• 分子量: 363.376
• InChiKey: ATAKEVCGTRZKLI-UWJYBYFXSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -4
• 重原子数：
  26
• 可旋转键数：
  9
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.4
• 拓扑面积：
  179
• 氢给体数：
  6
• 氢受体数：
  7

反应信息

• 作为产物：
  描述：

  2-trimethylsilylethyl (2S)-3-iodo-2-(tritylamino)propanoate 、 Fmoc-L-丙氨酸 、 N-Fmoc-N'-三苯甲基-L-组氨酸 在 4-甲基哌啶 、 N,N-二异丙基乙胺 、 N-[(dimethylamino)-3-oxo-1H-1,2,3-triazolo[4,5-b]pyridin-1-yl-methylene]-N-methylmethanaminium hexafluorophosphate 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 0.83h， 生成 AHH
  参考文献：
  名称：

  Cu(II) Binding to the Peptide Ala-His-His, a Chimera of the Canonical Cu(II)-Binding Motifs Xxx-His and Xxx-Zzz-His

  摘要：

  Peptides and proteins with the N-terminal motifs NH2-Xxx-His and NH2-Xxx-Zzz-His form well-established Cu(II) complexes. The canonical peptides are Gly-His-Lys and Asp-Ala-His-Lys (from the wound healing factor and human serum albumin, respectively). Cu(II) is bound to NH2-Xxx-His via three nitrogens from the peptide and an external ligand in the equatorial plane (called 3N form here). In contrast, Cu(II) is bound to NH2-Xxx-Zzz-His via four nitrogens from the peptide in the equatorial plane (called 4N form here). These two motifs are not mutually exclusive, as the peptides with the sequence NH2-Xxx-His-His contain both of them. However, this chimera has never been fully explored. In this work, we use a multispectroscopic approach to analyze the Cu(II) binding to the chimeric peptide Ala His-His (AHH). AHH is capable of forming the 3N- and 4N-type complexes in a pH dependent manner. The 3N form predominates at pH similar to 4-6.5 and the 4N form at similar to pH 6.5-10. NMR experiments showed that at pH 8.5, where Cu(II) is almost exclusively bound in the 4N form, the Cu(II)-exchange between AHH or the amidated AHH-NH2 is fast, in comparison to the nonchimeric 4N form (AAH). Together, the results show that the chimeric AHH can access both Cu(II) coordination types, that minor changes in the second (or further) coordination sphere can impact considerably the equilibrium between the forms, and that Cu kinetic exchange is fast even when Cu-AHH is mainly in the 4N form.

  DOI：

  10.1021/acs.inorgchem.7b01996

文献信息

• Cu(II) Binding to the Peptide Ala-His-His, a Chimera of the Canonical Cu(II)-Binding Motifs Xxx-His and Xxx-Zzz-His
  作者：Paulina Gonzalez、Bertrand Vileno、Karolina Bossak、Youssef El Khoury、Petra Hellwig、Wojciech Bal、Christelle Hureau、Peter Faller

  DOI：10.1021/acs.inorgchem.7b01996

  日期：2017.12.18

  Peptides and proteins with the N-terminal motifs NH2-Xxx-His and NH2-Xxx-Zzz-His form well-established Cu(II) complexes. The canonical peptides are Gly-His-Lys and Asp-Ala-His-Lys (from the wound healing factor and human serum albumin, respectively). Cu(II) is bound to NH2-Xxx-His via three nitrogens from the peptide and an external ligand in the equatorial plane (called 3N form here). In contrast, Cu(II) is bound to NH2-Xxx-Zzz-His via four nitrogens from the peptide in the equatorial plane (called 4N form here). These two motifs are not mutually exclusive, as the peptides with the sequence NH2-Xxx-His-His contain both of them. However, this chimera has never been fully explored. In this work, we use a multispectroscopic approach to analyze the Cu(II) binding to the chimeric peptide Ala His-His (AHH). AHH is capable of forming the 3N- and 4N-type complexes in a pH dependent manner. The 3N form predominates at pH similar to 4-6.5 and the 4N form at similar to pH 6.5-10. NMR experiments showed that at pH 8.5, where Cu(II) is almost exclusively bound in the 4N form, the Cu(II)-exchange between AHH or the amidated AHH-NH2 is fast, in comparison to the nonchimeric 4N form (AAH). Together, the results show that the chimeric AHH can access both Cu(II) coordination types, that minor changes in the second (or further) coordination sphere can impact considerably the equilibrium between the forms, and that Cu kinetic exchange is fast even when Cu-AHH is mainly in the 4N form.