Boc-NHPro-Val-Ala-Ala-NHⁱPr | 218455-01-7

• 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: Boc-NHPro-Val-Ala-Ala-NHⁱPr
• 英文别名: tert-butyl N-[(2S)-2-[[(2S)-3-methyl-1-oxo-1-[[(2S)-1-oxo-1-[[(2S)-1-oxo-1-(propan-2-ylamino)propan-2-yl]amino]propan-2-yl]amino]butan-2-yl]carbamoyl]pyrrolidin-1-yl]carbamate
• CAS: 218455-01-7
• 化学式: C₂₄H₄₄N₆O₆
• 分子量: 512.65
• InChiKey: YYFHWPHLBBMXET-XSLAGTTESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.6
• 重原子数：
  36
• 可旋转键数：
  12
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.79
• 拓扑面积：
  158
• 氢给体数：
  5
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  Boc-NHPro-Val-Ala-Ala-NHⁱPr 在 盐酸 、 三乙胺 作用下， 以 乙酸乙酯 、 N,N-二甲基甲酰胺 为溶剂， 反应 48.0h， 生成 Boc-Ala-NHPro-Val-Ala-Ala-NHⁱPr
  参考文献：
  名称：

  Design and Synthesis of Hydrazinopeptides and Their Evaluation as Human Leukocyte Elastase Inhibitors

  摘要：

  The name hydrazinopeptide designates peptidic structures in which one of the native CONH links is replaced by a CONHNH (hydrazido) fragment. In this paper, we report the synthesis of such hydrazinohexapeptides (3-5) analogous to Z-Ala-Ala-Pro-Val-Ala-Ala-(NHPr)-Pr-i (6), a substrate of human leukocyte elastase (HLE; EC 3.4.21.37), cleaved by this serine protease between the Val4 and Ala5 residues. In hydrazinopeptides 3-5, the Ala5, Val4, or Pro3 residue, respectively, of the model peptide, has been replaced by the corresponding alpha-L-hydrazino acid. In 3, the bond likely to be cleaved by HLE is the one involving the CONHNH link, while in 4 and 5, this link is normally shifted away by one or two amino acid units from the catalytic serine. On incubation with HLE, hydrazinopeptide 3 proved to be a substrate and was cleaved between Val4 and NHAla5, like peptide 6. In contrast, 4 and 5 proved to bind to HLE without being cleaved, featuring properties consistent with reversible competitive inhibition. General guidelines for the synthesis of hydrazinopeptides are also reported in this paper. These guidelines take into account the chemical specificity of hydrazino acids, while being fully compatible with the conventional peptide coupling techniques. The utilization of orthogonally bisprotected hydrazino acids 1 where the N-beta and N-alpha atoms bear a Boc and a Bzl group, respectively, is recommended for the easy construction of such hydrazinopeptides.

  DOI：

  10.1021/jm980419o
• 作为产物：
  描述：

  (S)-(-)-N-BOC-L-脯氨酸肼 、 HCl*Val-Ala-Ala-NHⁱPr 在 三乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 48.0h， 生成 Boc-NHPro-Val-Ala-Ala-NHⁱPr
  参考文献：
  名称：

  Design and Synthesis of Hydrazinopeptides and Their Evaluation as Human Leukocyte Elastase Inhibitors

  摘要：

  The name hydrazinopeptide designates peptidic structures in which one of the native CONH links is replaced by a CONHNH (hydrazido) fragment. In this paper, we report the synthesis of such hydrazinohexapeptides (3-5) analogous to Z-Ala-Ala-Pro-Val-Ala-Ala-(NHPr)-Pr-i (6), a substrate of human leukocyte elastase (HLE; EC 3.4.21.37), cleaved by this serine protease between the Val4 and Ala5 residues. In hydrazinopeptides 3-5, the Ala5, Val4, or Pro3 residue, respectively, of the model peptide, has been replaced by the corresponding alpha-L-hydrazino acid. In 3, the bond likely to be cleaved by HLE is the one involving the CONHNH link, while in 4 and 5, this link is normally shifted away by one or two amino acid units from the catalytic serine. On incubation with HLE, hydrazinopeptide 3 proved to be a substrate and was cleaved between Val4 and NHAla5, like peptide 6. In contrast, 4 and 5 proved to bind to HLE without being cleaved, featuring properties consistent with reversible competitive inhibition. General guidelines for the synthesis of hydrazinopeptides are also reported in this paper. These guidelines take into account the chemical specificity of hydrazino acids, while being fully compatible with the conventional peptide coupling techniques. The utilization of orthogonally bisprotected hydrazino acids 1 where the N-beta and N-alpha atoms bear a Boc and a Bzl group, respectively, is recommended for the easy construction of such hydrazinopeptides.

  DOI：

  10.1021/jm980419o

文献信息

• Design and Synthesis of Hydrazinopeptides and Their Evaluation as Human Leukocyte Elastase Inhibitors
  作者：Laure Guy、Joëlle Vidal、André Collet、Augustin Amour、Michèle Reboud-Ravaux

  DOI：10.1021/jm980419o

  日期：1998.11.1

  The name hydrazinopeptide designates peptidic structures in which one of the native CONH links is replaced by a CONHNH (hydrazido) fragment. In this paper, we report the synthesis of such hydrazinohexapeptides (3-5) analogous to Z-Ala-Ala-Pro-Val-Ala-Ala-(NHPr)-Pr-i (6), a substrate of human leukocyte elastase (HLE; EC 3.4.21.37), cleaved by this serine protease between the Val4 and Ala5 residues. In hydrazinopeptides 3-5, the Ala5, Val4, or Pro3 residue, respectively, of the model peptide, has been replaced by the corresponding alpha-L-hydrazino acid. In 3, the bond likely to be cleaved by HLE is the one involving the CONHNH link, while in 4 and 5, this link is normally shifted away by one or two amino acid units from the catalytic serine. On incubation with HLE, hydrazinopeptide 3 proved to be a substrate and was cleaved between Val4 and NHAla5, like peptide 6. In contrast, 4 and 5 proved to bind to HLE without being cleaved, featuring properties consistent with reversible competitive inhibition. General guidelines for the synthesis of hydrazinopeptides are also reported in this paper. These guidelines take into account the chemical specificity of hydrazino acids, while being fully compatible with the conventional peptide coupling techniques. The utilization of orthogonally bisprotected hydrazino acids 1 where the N-beta and N-alpha atoms bear a Boc and a Bzl group, respectively, is recommended for the easy construction of such hydrazinopeptides.