Z-Gly 2,2,2-trifluoroethyl ester | 203640-50-0

• 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: Z-Gly 2,2,2-trifluoroethyl ester
• 英文别名: Cbz-Gly-OTfe；2,2,2-Trifluoroethyl 2-(phenylmethoxycarbonylamino)acetate；2,2,2-trifluoroethyl 2-(phenylmethoxycarbonylamino)acetate
• CAS: 203640-50-0
• 化学式: C₁₂H₁₂F₃NO₄
• 分子量: 291.227
• InChiKey: VWKXFODDKNSPNR-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.5
• 重原子数：
  20
• 可旋转键数：
  7
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  64.6
• 氢给体数：
  1
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  Z-Gly 2,2,2-trifluoroethyl ester 在 L-苯丙氨酸 、 sodium chloride 、 calcium chloride 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 以5.7%的产率得到N-苄氧羰基甘氨酸
  参考文献：
  名称：

  酶特异性激活与离开组能力

  摘要：

  由酶激活还是只是一个好的离去基团？胍基苯基 (OGp) 酯是底物模拟物和化学酶促肽键形成中的关键激活基团。我们表明酯的离去基团能力在这个过程中至少与激活基团与酶的特定相互作用一样重要。

  DOI：

  10.1002/cbic.201200227
• 作为产物：
  描述：

  2,2,2-三氟乙醇 、 N-苄氧羰基甘氨酸 在 4-二甲氨基吡啶 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 作用下， 以 二氯甲烷 为溶剂， 生成 Z-Gly 2,2,2-trifluoroethyl ester
  参考文献：
  名称：

  在动态控制的肽合成中，通过使用氨基甲酰基甲酯作为酰基供体，扩大了α-胰凝乳蛋白酶的底物耐受性

  摘要：

  在动力学控制方法中 肽 通过α-胰凝乳蛋白酶介导的合成，可通过切换蛋白酶来实现蛋白酶底物耐受性的扩大。 酰基供体从常规的甲酯到氨基甲酰基甲酯。因此，作为典型实例，通过使用固有不良的甲基酯获得极低的偶联效率。氨基酸 基质， 翼，通过使用此特殊功能得到了显着改善 酯。在其他氨基酸残基如Gly和Ser的偶联中也观察到其改善作用。羧基 成分。

  DOI：

  10.1039/b004180g

文献信息

• Papain-Specific Activating Esters in Aqueous Dipeptide Synthesis
  作者：Roseri J. A. C. de Beer、Barbara Zarzycka、Michiel Mariman、Helene I. V. Amatdjais-Groenen、Marc J. Mulders、Peter J. L. M. Quaedflieg、Floris L. van Delft、Sander B. Nabuurs、Floris P. J. T. Rutjes

  DOI：10.1002/cbic.201200017

  日期：2012.6.18

  A set of new activating esters was evaluated in an enzymatic, papain‐catalyzed approach to synthesizing dipeptides under aqueous conditions. In particular, benzyl and dimethylaminophenyl esters yielded the corresponding dipeptides in several instances in high yields and with relatively small levels of hydrolysis. These results were also interpreted by computational docking analysis.

  一组新的活化酯是在木瓜蛋白酶催化的水溶液中以酶促法合成的。特别地，苄基和二甲基氨基苯基酯在几种情况下以高产率和相对少量的水解产生相应的二肽。这些结果也可以通过计算对接分析来解释。
• Remarkable effects of donor esters on the α-chymotrypsin-catalyzed couplings of inherently poor amino acid substrates
  作者：Toshifumi Miyazawa、Kayoko Tanaka、Eiichi Ensatsu、Ryoji Yanagihara、Takashi Yamada

  DOI：10.1016/s0040-4039(97)10798-5

  日期：1998.2

  The extremely low efficiency during the α-chymotrypsin-catalyzed coupling of an inherently poor amino acid substrate, e.g., alanine, using the methyl ester as an acyl donor was significantly improved using esters such as the 2,2,2-trifluoroethyl or carbamoylmethyl ester. The ameliorating effect of the latter ester was especially significant.

  使用酯类（例如2,2,2-三氟乙基或氨基甲酰基甲基酯）可显着改善α-胰凝乳蛋白酶催化的固有不良氨基酸底物（如丙氨酸）在使用甲基酯作为酰基供体时的极低效率。后一种酯的改善作用特别显着。
• Improving the carboxyamidomethyl ester for subtilisin A-catalysed peptide synthesis
  作者：Roseri J. A. C. de Beer、Timo Nuijens、Lotte Wiermans、Peter J. L. M. Quaedflieg、Floris P. J. T. Rutjes

  DOI：10.1039/c2ob25662b

  日期：——

  A series of novel glycine esters was evaluated for efficiency in subtilisin A-CLEA-catalysed peptide synthesis. The reactivity of the easily accessible carboxyamidomethyl (Cam) ester was further enhanced by elongating it with an amino acid residue, thereby creating more recognition space for subtilisin A.

  我们评估了一系列新型甘氨酸酯在枯草酶 A-CLEA 催化肽合成中的效率。通过将羧酰胺甲基（Cam）酯与一个氨基酸残基拉长，进一步提高了这种容易获得的酯的反应活性，从而为枯草蛋白 A 创造了更多的识别空间。
• Enzymatic synthesis of activated esters and their subsequent use in enzyme-based peptide synthesis
  作者：Timo Nuijens、Claudia Cusan、Annette C.H.M. Schepers、John A.W. Kruijtzer、Dirk T.S. Rijkers、Rob M.J. Liskamp、Peter J.L.M. Quaedflieg

  DOI：10.1016/j.molcatb.2011.03.012

  日期：2011.8

  Chemoenzymatic peptide synthesis is potentially the most cost-efficient technology for the synthesis of short and medium-sized peptides. However, there are still some limitations when challenging peptides, e.g. containing sterically demanding acyl donors, non-proteinogenic amino acids or proline residues, are to be synthesized. To remedy these limitations, special ester moieties have been used that are specifically recognized by the enzyme, e.g. guanidinophenyl, carboxamidomethyl (Cam) or trifluoroethyl (Tfe) esters, which, unfortunately, are notoriously difficult to synthesize chemically. Herein, we demonstrate that Cam and Tfe esters are very useful for Alcalase-CLEA mediated peptide synthesis using sterically demanding and non-proteinogenic acyl donors as well as poor nucleophiles, and combinations thereof. Furthermore, these esters can be efficiently synthesized by using the lipase Cal-B or Alcalase-CLEA. Finally, it is shown that the ester synthesis by Cal-B and subsequent peptide synthesis by Alcalase-CLEA can be performed simultaneously using a two-enzyme-one-pot approach with glycolamide or 2,2,2-trifluoroethanol as additive. (C) 2011 Elsevier B.V. All rights reserved.
• Enzyme-Specific Activation versus Leaving Group Ability
  作者：Roseri J. A. C. de Beer、Berry Bögels、Gijs Schaftenaar、Barbara Zarzycka、Peter J. L. M. Quaedflieg、Floris L. van Delft、Sander B. Nabuurs、Floris P. J. T. Rutjes

  DOI：10.1002/cbic.201200227

  日期：2012.8.13

  Activation by the enzyme or just a good leaving group? The guanidinophenyl (OGp) ester is a key activating group in substrate mimetics and chemoenzymatic peptide bond formation. We show that the leaving group ability of the ester is at least as important in this process as the specific interactions of the activating group with the enzyme.

  由酶激活还是只是一个好的离去基团？胍基苯基 (OGp) 酯是底物模拟物和化学酶促肽键形成中的关键激活基团。我们表明酯的离去基团能力在这个过程中至少与激活基团与酶的特定相互作用一样重要。