4-(phenylacetoxy)benzyl chloroformate | 192999-58-9

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯酚酯
• 英文名称: 4-(phenylacetoxy)benzyl chloroformate
• 英文别名: [4-(Carbonochloridoyloxymethyl)phenyl] 2-phenylacetate
• CAS: 192999-58-9
• 化学式: C₁₆H₁₃ClO₄
• 分子量: 304.73
• InChiKey: PQZPELKMZDOETK-UHFFFAOYSA-N

物化性质

• 沸点：
  440.5±45.0 °C(Predicted)
• 密度：
  1.294±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  4
• 重原子数：
  21
• 可旋转键数：
  7
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.12
• 拓扑面积：
  52.6
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  4-(phenylacetoxy)benzyl chloroformate 在 吗啉 、 四(三苯基膦)钯 、 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 四氢呋喃 、 二氯甲烷 为溶剂， 反应 5.0h， 生成 (2S,3R)-3-hydroxy-2-[[(2S)-1-[[4-(2-phenylacetyl)oxyphenyl]methoxycarbonyl]pyrrolidine-2-carbonyl]amino]butanoic acid
  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-formylphenyl 2-phenylacetate 在 sodium tetrahydroborate 作用下， 以 异丙醇 、 甲苯 为溶剂， 反应 3.0h， 生成 4-(phenylacetoxy)benzyl chloroformate
  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

• Selective activation of organocatalysts by specific signals
  作者：Chandan Maity、Fanny Trausel、Rienk Eelkema

  DOI：10.1039/c8sc02019a

  日期：——

  development of catalysts that can be activated by different signals. To demonstrate the versatility of that concept, we synthesized organocatalysts that can be activated by three different signals and that can be used to control two different reactions. In this way the organocatalyst proline is designed as a pro-catalyst that is activated either by the chemical signal H2O2, by light or by the enzyme penicillin

  让人想起生物系统中的信号转导，可以通过物理或化学信号控制其活性的人工催化剂将在设计能够响应其环境的化学系统中引起极大的兴趣。自焚化学为开发可被不同信号活化的催化剂提供了一种通用方法。为了证明该概念的多功能性，我们合成了可以被三种不同信号激活并可以用来控制两种不同反应的有机催化剂。这样，有机催化剂脯氨酸被设计为被化学信号H 2 O 2活化的前催化剂。，通过光照或青霉素酰基转移酶。助催化剂用于对醛醇缩合反应和迈克尔反应的速率进行时间控制。
• 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
• Braun; Kuhl, Pharmazie, 2002, vol. 57, # 5, p. 310 - 312
  作者：Braun、Kuhl

  DOI：——

  日期：——
• Mapping Concentration Profiles within the Diffusion Layer of an Electrode: Application to Redox Catalysis
  作者：Christian Amatore、Cécile Pebay、Onofrio Scialdone、Sabine Szunerits、Laurent Thouin

  DOI：10.1002/1521-3765(20010702)7:13<2940::aid-chem2940>3.0.co;2-u

  日期：2001.7.2

  Catalytic reductions of some aromatic halides were performed at a millimetric electrode with several redox mediators. The resulting concentration profiles were monitored amperometrically by placing an ultramicroelectrode inside the diffusion layer produced at the former electrode. The features of redox catalysis and the subsequent structuring of the diffusion layer were investigated experimentally under steady-state conditions imposed by the spontaneous convection of the solution. The concentration profiles established from the probe measurements were in agreement with our theoretical predictions, based on fast kinetics of redox catalysis. Under these conditions, very similar to preparative electrosynthesis, the diffusion layer separates into two domains where pure diffusion takes place and the concentration profiles therein are mainly linear. We demonstrate that the limit between these two zones does not depend on kinetics, but is rather fixed by the product of the ratio of the bulk concentrations of each species and the ratio of their diffusion coefficients.