PhAcOZ-Ala-OH | 182485-55-8

• 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: PhAcOZ-Ala-OH
• 英文别名: (2S)-2-[[4-(2-phenylacetyl)oxyphenyl]methoxycarbonylamino]propanoic acid
• CAS: 182485-55-8
• 化学式: C₁₉H₁₉NO₆
• 分子量: 357.363
• InChiKey: PDISYRZRMLVPNA-ZDUSSCGKSA-N

物化性质

• 沸点：
  592.4±50.0 °C(Predicted)
• 密度：
  1.288±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.8
• 重原子数：
  26
• 可旋转键数：
  9
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.21
• 拓扑面积：
  102
• 氢给体数：
  2
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  L-亮氨酸叔丁酯盐酸盐 、 PhAcOZ-Ala-OH 在 1-羟基苯并三唑 、 N,N'-二环己基碳二亚胺 作用下， 以 二氯甲烷 为溶剂， 生成 tert-butyl (2S)-4-methyl-2-[[(2S)-2-[[4-(2-phenylacetyl)oxyphenyl]methoxycarbonylamino]propanoyl]amino]pentanoate
  参考文献：
  名称：

  Chemoenzymatic Synthesis of a Characteristic Phosphorylated and Glycosylated Peptide Fragment of the Large Subunit of Mammalian RNA Polymerase II

  摘要：

  The covalent modification of proteins by phosphorylation and addition of GlcNAc residues are important regulatory processes which mediate biological signal transduction. For instance, the cytosolic form of RNA polymerase II is heavily glycosylated but during its transition from an initiating to an elongating complex the carbohydrates are removed and the protein is phosphorylated. For the study of such biological phenomena, characteristic peptides which embody both types of modifications may serve as efficient tools. However, their synthesis is complicated by their pronounced acid and base lability as well as their multifunctionality. These properties make the application of protecting groups necessary which can be removed under the mildest conditions. For the construction of such peptide conjugates the enzyme labile PhAcOZ urethane blocking group was developed. This protecting group embodies (a) a functional group (a phenylacetate) that is recognized by the biocatalyst (penicillin G acylase) and that is bound by an enzyme labile linkage (an ester) to (b) a functional group (a p-hydroxybenzyl urethane) that undergoes a spontaneous fragmentation upon cleavage of the enzyme-sensitive bond resulting in (c) the liberation of a carbamic acid derivative which decarboxylates to give the desired peptide or peptide conjugate. When this enzymatic protecting group technique was combined with classical chemical methods, a complex phosphoglycohexapeptide was built up, which embodies two glycosylated, one phosphorylated, and one underivatized hydroxyamino acid. This peptide represents a characteristic partial structure of the repeat sequence of the large subunit of RNA polymerase II which becomes glycosylated or phosphorylated while the enzyme carries out its biological functions. The conditions under which the enzymatic deprotections proceed are so mild that no undesired side reaction is observed (i.e., no rupture or anomerization of the glycosidic bonds and no beta-elimination of the phosphate or a carbohydrate occur). In addition, the specificity of the biocatalyst guarantees that the peptide bonds and the other protecting groups present are not attacked either.

  DOI：

  10.1021/ja970709e
• 作为产物：
  描述：

  4-(hydroxymethyl)phenyl 2-phenylacetate 在 N,N-二异丙基乙胺 作用下， 以 二氯甲烷 、 甲苯 为溶剂， 反应 5.5h， 生成 PhAcOZ-Ala-OH
  参考文献：
  名称：

  Chemoenzymatic Synthesis of a Characteristic Phosphorylated and Glycosylated Peptide Fragment of the Large Subunit of Mammalian RNA Polymerase II

  摘要：

  The covalent modification of proteins by phosphorylation and addition of GlcNAc residues are important regulatory processes which mediate biological signal transduction. For instance, the cytosolic form of RNA polymerase II is heavily glycosylated but during its transition from an initiating to an elongating complex the carbohydrates are removed and the protein is phosphorylated. For the study of such biological phenomena, characteristic peptides which embody both types of modifications may serve as efficient tools. However, their synthesis is complicated by their pronounced acid and base lability as well as their multifunctionality. These properties make the application of protecting groups necessary which can be removed under the mildest conditions. For the construction of such peptide conjugates the enzyme labile PhAcOZ urethane blocking group was developed. This protecting group embodies (a) a functional group (a phenylacetate) that is recognized by the biocatalyst (penicillin G acylase) and that is bound by an enzyme labile linkage (an ester) to (b) a functional group (a p-hydroxybenzyl urethane) that undergoes a spontaneous fragmentation upon cleavage of the enzyme-sensitive bond resulting in (c) the liberation of a carbamic acid derivative which decarboxylates to give the desired peptide or peptide conjugate. When this enzymatic protecting group technique was combined with classical chemical methods, a complex phosphoglycohexapeptide was built up, which embodies two glycosylated, one phosphorylated, and one underivatized hydroxyamino acid. This peptide represents a characteristic partial structure of the repeat sequence of the large subunit of RNA polymerase II which becomes glycosylated or phosphorylated while the enzyme carries out its biological functions. The conditions under which the enzymatic deprotections proceed are so mild that no undesired side reaction is observed (i.e., no rupture or anomerization of the glycosidic bonds and no beta-elimination of the phosphate or a carbohydrate occur). In addition, the specificity of the biocatalyst guarantees that the peptide bonds and the other protecting groups present are not attacked either.

  DOI：

  10.1021/ja970709e

文献信息

• Synthesis of Nucleopeptides by Employing an Enzyme-Labile Urethane Protecting Group
  作者：Duraiswamy A. Jeyaraj、Heino Prinz、Herbert Waldmann

  DOI：10.1002/1521-3765(20020415)8:8<1879::aid-chem1879>3.0.co;2-5

  日期：2002.4.15

  base lability of nucleopeptides, their synthesis requires the application of a variety of orthogonally stable blocking groups, which can be removed under the mildest conditions. We have developed a new mild enzymatic deprotection method, that is, the penicillin G acylase-catalyzed hydrolysis of the N-phenylacetoxybenzyloxycarbony (PhAcOZ) group, for the synthesis of nucleopeptides. We demonstrate the

  核蛋白是天然存在的生物聚合物，其中丝氨酸，苏氨酸或酪氨酸部分的羟基通过磷酸二酯基连接到核酸的3'-或5'-末端。为了研究其中涉及核蛋白的生物学现象，例如病毒复制，体现肽链和寡核苷酸之间的特征性连接的核苷酸肽可以用作强大的工具。然而，由于核苷酸的多功能性和明显的酸和碱不稳定性，它们的合成需要应用各种正交稳定的保护基团，这些保护基团可以在最温和的条件下除去。我们开发了一种新的温和酶解保护方法，即 青霉素G酰基转移酶催化的N-苯基乙酰氧基苄氧基羰基（PhAcOZ）基团的水解，用于合成核苷酸肽。我们通过将N-末端去保护的核苷酸肽31 ac与PhAcOZ保护的氨基酸偶联，然后从青霉素G酰基转移酶完全保护的核苷酸四肽32 a，b中除去N-PhAcOZ基团，证明了该方法的广泛适用性。反应条件非常温和（pH 6.8），因此未观察到不希望的副反应，例如核苷酸键的断裂或核苷酸的β-消除。我们通过将N-末端去保护的核苷酸肽31
• Pohl, Torsten; Waldmann, Herbert, Angewandte Chemie, 1996, vol. 108, # 15, p. 1829 - 1832
  作者：Pohl, Torsten、Waldmann, Herbert

  DOI：——

  日期：——