N-NVOC-L-phenylalanine | 30034-25-4

• 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: N-NVOC-L-phenylalanine
• 英文别名: N-(4,5-dimethoxy-2-nitrobenzyloxycarbonyl)-L-phenylalanine；NVOC-Phe-OH；(2S)-2-[(4,5-dimethoxy-2-nitrophenyl)methoxycarbonylamino]-3-phenylpropanoic acid
• CAS: 30034-25-4
• 化学式: C₁₉H₂₀N₂O₈
• 分子量: 404.376
• InChiKey: QDNREOBCXKMERP-AWEZNQCLSA-N

物化性质

• 沸点：
  636.1±55.0 °C(Predicted)
• 密度：
  1.349±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.8
• 重原子数：
  29
• 可旋转键数：
  9
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.26
• 拓扑面积：
  140
• 氢给体数：
  2
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  N-NVOC-L-phenylalanine 在 三乙胺 作用下， 反应 24.0h， 生成 5'-O-phosphoryl-2'-deoxycytidylyl(3'-5')-<2'-O-(D-phenylalanyl)adenosine>
  参考文献：
  名称：

  转移 RNA 化学氨酰化的通用有效途径

  摘要：

  详述了通过N-保护的α-氨基酸的氰甲基活性酯与pdCpA反应一步高产率制备氨酰基pdCpA。还研究了含有硝基草酰 (NVOC) N 保护氨基酸的氨酰基 pdCpA 衍生物的制备和光脱保护。通过将 NVOC-苯丙氨酰 pdCpA 酶促连接到 tRNA-C OH，然后光解以提供未保护的苯丙氨酰 tRNA，证实了上述制备氨酰 tRNA 的方法的效用。苯丙氨酰 tRNA 被证明在体外蛋白质生物合成系统中是有能力的。这些协议极大地简化了化学错酰化 tRNA 在含有非天然氨基酸的蛋白质合成以及蛋白质生物合成研究中的使用

  DOI：

  10.1021/ja00007a055
• 作为产物：
  描述：

  4,5-二甲氧基-2-硝基苯甲醇 在 碳酸氢钠 、 三乙胺 作用下， 以 四氢呋喃 、 1,4-二氧六环 、 水 为溶剂， 反应 4.0h， 生成 N-NVOC-L-phenylalanine
  参考文献：
  名称：

  Oligonucleotide promoted peptide bond formation using a tRNA mimicking approach

  摘要：

  tRNA在蛋白质翻译中的作用是信息离去基团（ILG）的主要例子。在特定寡核苷酸存在的情况下，一个简化的模型使用修饰的尿嘧啶作为ILG产生寡苯丙氨酸。我们的初步研究有助于弥合肽和核酸之间的差距的混合物种的重要性。

  DOI：

  10.1039/c7cc00831g

文献信息

• Synthesis of Pentafluorophenyl Esters of Nitroveratryloxycarbonyl-Protected Amino Acids
  作者：Yoon-Sik Lee、Dong-Sik Shin

  DOI：10.1055/s-0029-1218369

  日期：2009.12

  For efficient peptide synthesis on a glass chip, 20 kinds of pentafluorophenyl (Pfp) esters of nitroveratryloxycarbonyl (NVOC)-protected amino acids were synthesized by using Pfp tri­fluoroacetate. Simple purification step gave moderate to high yield. The first loading time of each amino acid on glass surface was 30-60 min. The UV cleavage of the NVOC group was completed within 10 minutes.

  为了在玻璃芯片上高效合成肽，通过使用五氟苯基三氟乙酸盐合成了20种硝基藜芦氧羰基（NVOC）保护的氨基酸的五氟苯基（Pfp）酯。简单的纯化步骤提供了中等至高产率。每个氨基酸在玻璃表面上的第一次加载时间为30-60分钟。NVOC基团的紫外光裂解在10分钟内完成。
• Sequentially Photocleavable Protecting Groups in Solid-Phase Synthesis
  作者：Martin Kessler、Ralf Glatthar、Bernd Giese、Christian G. Bochet

  DOI：10.1021/ol027454g

  日期：2003.4.1

  [reaction: see text] A sequential solid-phase peptide synthesis was developed using both photolabile linker and protecting groups. The chromatic sequential lability between a tert-butyl ketone-derived linker (sensitive to irradiation at 305 nm) and a nitroveratryloxycarbonyl (NVOC) group (sensitive at 360 nm) was exploited to prepare Leu-Enkephalin in a 55% overall yield. This new strategy allows the

  [反应：见正文]使用光不稳定的连接基和保护基团开发了顺序的固相肽合成方法。利用叔丁基酮衍生的连接基（对305 nm的辐射敏感）和硝基过碳酰氧羰基（NVOC）基团（对360 nm敏感）之间的色序不稳定性来制备亮氨酸-脑啡肽，总产率为55％。通过避免使用常见的脱保护试剂（例如三氟乙酸或哌啶），该新策略允许在基本中性的介质中制备肽。
• Photocaged Competitor Guests: A General Approach Toward Light-Activated Cargo Release From Cucurbiturils
  作者：Miguel A. Romero、Nuno Basílio、Artur J. Moro、Mara Domingues、José A. González-Delgado、Jesús F. Arteaga、Uwe Pischel

  DOI：10.1002/chem.201702185

  日期：2017.9.21

  light‐induced guest release from cucurbit[7]uril by means of a photoactivatable competitor was devised. An o‐nitrobenzyl‐caged competitor is photolyzed to generate a competitive guest that can displace cargo from the host macrocycle solely based on considerations of chemical equilibrium. With this method the release of terpene guests from inclusion complexes with cucurbit[7]uril was demonstrated. The binding

  设计了一种通过光活化竞争剂从葫芦[7]脲中光诱导客体释放的一般方法。仅基于化学平衡的考虑，邻硝基苄基笼竞争者被光解以产生竞争性客体，该客体可以从宿主大环中置换货物。用这种方法证明了从与葫芦[7]脲的包合物中释放萜客体。本文研究的萜烯（都是精油中的铅芳香成分）的结合首次得到了表征。它们的结合常数高达 10 8  L mol -1和高差异结合选择性（对于特定萜烯组的结合常数跨越四个数量级）。通过微调可光激活的竞争客体，实现了萜烯的选择性和顺序释放。
• Automated Maskless Photolithography System for Peptide Microarray Synthesis on a Chip
  作者：Dong-Sik Shin、Kook-Nyung Lee、Byung-Wook Yoo、Jaehi Kim、Mira Kim、Yong-Kweon Kim、Yoon-Sik Lee

  DOI：10.1021/cc100009g

  日期：2010.7.12

  Maskless photolithographic peptide synthesis was performed on a glass chip using an automated peptide array synthesizer system. The peptide array synthesizer was built in a closed box, which contained optical and fluidic systems. The conditions for peptide synthesis were fully controlled by a computer program. For the peptide synthesis on a glass chip, 20 NVOC-protected amino acids were synthesized. The coupling efficiencies of two model peptide sequences were examined on ACA/APTS and PEG/CHI/GPTS chips. PEG/CHI/GPIS chip gave higher average stepwise yields of GIYWHHY (94%) and YIYGSFK (98%) than those of ACA/APTS chip. To quantify peptide-protein binding affinity, HPQ- or HPM-containing pentapeptides were synthesized on a PEG/CHI/GPTS chip and the binding event of Cy3 labeled-streptavidin was quantified. The peptide sequence of IQHPQ showed highest binding affinity with Cy3 labeled-streptavidin. The results demonstrated that the photolithographic peptide array synthesis method efficiently quantified the binding activities of protein-peptide interactions and it can be used for additional biological assay applications.
• Specificity of Translation for <i>N</i>-Alkyl Amino Acids
  作者：Baolin Zhang、Zhongping Tan、Lucas Gartenmann Dickson、Madhavi N. L. Nalam、Virginia W. Cornish、Anthony C. Forster

  DOI：10.1021/ja073487l

  日期：2007.9.1

  We examine the specificity of translation for various primary and secondary amino acid analogues. A synthetase-free, pure, E. coli translation system is used to prevent competing reactions, and three different tRNA adaptor:codon pairs are used to control for tRNA- and codon-specific effects. Surprisingly, N -butyl amino acids fail to incorporate, N -methyl amino acid incorporation efficiencies are dependent on the tRNA adaptor, yet hydroxyPro, Pro, Phe, and Ala incorporate near quantitatively from all adaptors. This suggests that Pro is a privileged N -alkyl amino acid for incorporation by the translation apparatus and establishes that very efficient N -methyl amino acid incorporation is possible if matched with an optimal tRNA adaptor. Results support exploration of Pro analogues and N -methyl amino acids as substrates for engineering ribosomal synthesis of genetically selectable libraries of protease-resistant, N -alkyl peptide ligands.