4-(hydroxymethyl)phenyl 2-phenylacetate | 192999-56-7

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯酚酯
• 英文名称: 4-(hydroxymethyl)phenyl 2-phenylacetate
• 英文别名: 4-(phenylacetoxy)benzyl alcohol；Benzeneacetic acid, 4-(hydroxymethyl)phenyl ester；[4-(hydroxymethyl)phenyl] 2-phenylacetate
• CAS: 192999-56-7
• 化学式: C₁₅H₁₄O₃
• 分子量: 242.274
• InChiKey: TWIPMPHQFPEIAW-UHFFFAOYSA-N

物化性质

• 沸点：
  422.7±38.0 °C(Predicted)
• 密度：
  1.201±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.4
• 重原子数：
  18
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.13
• 拓扑面积：
  46.5
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  4-(hydroxymethyl)phenyl 2-phenylacetate 在 4-二甲氨基吡啶 、 青霉素(酰胺)酶 、 达卡巴嗪 、 2-乙氧基-1-乙氧碳酰基-1,2-二氢喹啉 作用下， 以 甲醇 、 phosphate buffer 为溶剂， 生成 对羟基苯甲醇
  参考文献：
  名称：

  Synthesis and Membrane-Binding Properties of a Characteristic Lipopeptide from the Membrane-Anchoring Domain of Influenza Virus A Hemagglutinin

  摘要：

  On the trail of the influenza virus! Fluorescent-labeled lipopeptides, such as the characteristic S-palmitoylated partial structure from influenza virus hemagglutinin A, can be synthesized efficiently by employing a new enzymatic protecting-group technique in the key steps. Their binding to model membranes was determined in a kinetic assay, so leading to a first approximation of the membrane-anchoring ability of the corresponding lipopeptide motif in the parent protein.

  DOI：

  10.1002/1521-3773(20010119)40:2<369::aid-anie369>3.0.co;2-7
• 作为产物：
  描述：

  苯乙酰氯 在 4-二甲氨基吡啶 、 sodium sulfide 、 四丁基溴化铵 、 三乙胺 作用下， 以 二氯甲烷 、 水 、 甲苯 为溶剂， 反应 2.0h， 生成 4-(hydroxymethyl)phenyl 2-phenylacetate
  参考文献：
  名称：

  二酰基二硫化物：4-（N，N-二甲基氨基）吡啶催化的苯酚化学选择性酰化试剂

  摘要：

  为了通过DMAP（4-（N，N-二甲基氨基）吡啶）催化实现有效的酯形成，发现了通用且优异的酰化试剂二酰基二硫化物。该方案为酚和伯脂族羟基的位点选择性酰化提供了一个有希望的合成平台，这大大扩展了保护基化学的领域。该试剂的重要性还体现在其出色的耐湿性，高效率以及在合成化学和生物学上有意义的天然产物修饰方面的潜力。

  DOI：

  10.1021/acs.orglett.6b02818

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 and Membrane Binding Properties of a Lipopeptide Fragment from Influenza Virus A Hemagglutinin
  作者：Frank Eisele、Jürgen Kuhlmann、Herbert Waldmann

  DOI：10.1002/1521-3765(20020802)8:15<3362::aid-chem3362>3.0.co;2-0

  日期：2002.8.2

  Hemagglutinin from influenza virus A is a S-palmitoylated lipoglycoprotein in which the lipid groups are thought to influence the interaction between cell membrane and capsid during budding of viral offspring as well as fusion processes of the viral membrane with the endosome after entry of the viral particle into the cell. The paper describes the development of a method for the synthesis of characteristic lipidated hemagglutinin derived peptides which additionally carry the fluorescent 7-nitrobenz-2oxa-1,3-diazole (NBD) group. To achieve this goal the enzyme-sensitive para-phenylacetoxybenzyloxycarbonyl (PAOB) ester was developed. It is cleaved from the peptides and lipidated peptides under very mild conditions and with complete selectivity by treatment with the enzyme penicillin G acylase; this results in the formation of a phenolate. This intermediate spontaneously undergoes fragmentation thereby releasing the desired carboxylates. The combined use of this enzymelabile fragmenting ester with the acidlabile Boc group, the Pd-0-sensitive allyl ester and the corresponding Aloc urethane gave access to a mono-S-palmitoylated and a doubly S-palmitoylated NBD-labelled hemagglutinin peptide. The binding of these lipopeptides to model membranes was analyzed in a biophysical setup monitoring the transfer of fluorescent-labelled lipopeptide from vesicles containing the non-ex-changeable fluorescence quencher Rho-DHPE to quencher-free vesicles. The experiments demonstrate that one lipid group is not sufficient for quasi-irreversible membrane insertion of lipidated peptides. This is, however, achieved by introduction of the bis-palmitoyl anchor. The intervesicle transfer always implies release of peptides localized at the outer face of the vesicles into solution followed by diffusion to and insertion into acceptor vesicles. For peptides bound at the inner face of the vesicle membrane, however, an additional flip-flop diffusion to the outer face has to occur beforehand. The kinetics of these processes were estimated by fast chemical quench of the outside fluorophores by sodium dithionite.
• Formulating a new basis for the treatment against botulinum neurotoxin intoxication: 3,4-Diaminopyridine prodrug design and characterization
  作者：Joseph S. Zakhari、Isao Kinoyama、Mark S. Hixon、Antonia Di Mola、Daniel Globisch、Kim D. Janda

  DOI：10.1016/j.bmc.2011.09.019

  日期：2011.11

  Botulism is a disease characterized by neuromuscular paralysis and is produced from botulinum neurotoxins (BoNTs) found within the Gram positive bacterium Clostridium botulinum. This bacteria produces the most deadliest toxin known, with lethal doses as low as 1 ng/kg. Due to the relative ease of production and transport, the use of these agents as potential bioterrorist weapons has become of utmost concern. No small molecule therapies against BoNT intoxication have been approved to date. However, 3,4-diaminopyridine (3,4-DAP), a potent reversible inhibitor of voltage-gated potassium channels, is an effective cholinergic agonist used in the treatment of neuromuscular degenerative disorders that require cholinergic enhancement. 3,4-DAP has also been shown to facilitate recovery of neuromuscular action potential post botulinum intoxication by blocking K(+) channels. Unfortunately, 3,4-DAP displays toxicity largely due to blood-brain-barrier (BBB) penetration. As a dual-action prodrug approach to cholinergic enhancement we have designed carbamate and amide conjugates of 3,4-DAP. The carbamate prodrug is intended to be a slowly reversible inhibitor of acetylcholinesterase (AChE) along the lines of the stigmines thereby allowing increased persistence of released acetylcholine within the synaptic cleft. As a secondary activity, cleavage of the carbamate prodrug by AChE will afford the localized release of 3,4-DAP, which in turn, will enhance the pre-synaptic release of additional acetylcholine. Being a competitive inhibitor with respect to acetylcholine, the activity of the prodrug will be greatest at the synaptic junctions most depleted of acetylcholine. Here we report upon the synthesis and biochemical characterization of three new classes of prodrugs intended to limit previously reported stability and toxicity issues. Of the prodrugs examined, compound 32, demonstrated the most clinically relevant half-life of 2.76 h, while selectively inhibiting AChE over butyrylcholinesterase-a plasma-based high activity esterase. Future in vivo studies could provide validation of prodrug 32 as a potential treatment against BoNT intoxication as well as other neuromuscular disorders. (C) 2011 Elsevier Ltd. All rights reserved.
• Chemoenzymatic Synthesis of a Characteristic Phosphorylated and Glycosylated Peptide Fragment of the Large Subunit of Mammalian RNA Polymerase II
  作者：Torsten Pohl、Herbert Waldmann

  DOI：10.1021/ja970709e

  日期：1997.7.1

  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.
• Braun; Kuhl, Pharmazie, 2002, vol. 57, # 5, p. 310 - 312
  作者：Braun、Kuhl

  DOI：——

  日期：——