2-(2-(2-(prop-2-yn-1-yloxy)ethoxy)ethoxy)ethyl 4-chloro-3-nitrobenzoate | 1448620-78-7

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: 2-(2-(2-(prop-2-yn-1-yloxy)ethoxy)ethoxy)ethyl 4-chloro-3-nitrobenzoate
• CAS: 1448620-78-7
• 化学式: C₁₆H₁₈ClNO₇
• 分子量: 371.774
• InChiKey: ILYZFRCMHCOTPX-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.09
• 重原子数：
  25.0
• 可旋转键数：
  12.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.44
• 拓扑面积：
  97.13
• 氢给体数：
  0.0
• 氢受体数：
  7.0

反应信息

• 作为反应物：
  描述：

  谷胱甘肽 、 2-(2-(2-(prop-2-yn-1-yloxy)ethoxy)ethoxy)ethyl 4-chloro-3-nitrobenzoate 在 glutathione S-transferase 作用下， 以 甲醇 、 aq. phosphate buffer 为溶剂， 以45%的产率得到
  参考文献：
  名称：

  Synthesis of a Suite of Bioorthogonal Glutathione S-Transferase Substrates and Their Enzymatic Incorporation for Protein Immobilization

  摘要：

  Label-free protein immobilization allows precise detection of biomolecular events. Preserving enzyme function is intrinsically challenging for these strategies. Considering that glutathione S-transferase (GST) is a broadly employed enzymatic fusion tag, we reported a label-free self-catalyzed immobilization for Schistosoma japonicum GST. We now report the synthesis, structure, and enzymology of a set of 20 smSNAREs (small molecule SNAr-electrophiles). These smSNAREs mimic (electronically) the canonical GST substrate 1-chloro-2,4-dinitrobenzene (CDNB), and bear a wide variety of bioorthogonal functionalities such as alkynes, aldehydes, acetals, and azides. Sixteen analogues including the chloro- and nitro substituted 1, 3, 5, 6, 7, 11, 12, and 13 participated in the GST-catalyzed conjugation, indicating the substrate tolerance of the enzymatic H-site of SjGST. Using UV-vis spectroscopy, we estimate the efficiency of conjugation as a function of substrate diversity. Using LC-MS, we characterized the conjugates formed under each enzymatic transformation. Significant deviations from the canonical CDNB architecture are tolerated. Relative rates between nitro and chloro substituents indicate the nucleophilic addition step is rate determining. Enzyme immobilization on glass slides is affected by additional surface interactions and therefore does not reflect kinetic profiles observed in solution. This new class of heterobifunctional linkers enables a single-step and uniform protein capture on designer surfaces.

  DOI：

  10.1021/jo401278x
• 作为产物：
  描述：

  三乙二醇 在 偶氮二甲酸二异丙酯 、 三苯基膦 作用下， 以 四氢呋喃 为溶剂， 反应 5.0h， 生成 2-(2-(2-(prop-2-yn-1-yloxy)ethoxy)ethoxy)ethyl 4-chloro-3-nitrobenzoate
  参考文献：
  名称：

  Synthesis of a Suite of Bioorthogonal Glutathione S-Transferase Substrates and Their Enzymatic Incorporation for Protein Immobilization

  摘要：

  Label-free protein immobilization allows precise detection of biomolecular events. Preserving enzyme function is intrinsically challenging for these strategies. Considering that glutathione S-transferase (GST) is a broadly employed enzymatic fusion tag, we reported a label-free self-catalyzed immobilization for Schistosoma japonicum GST. We now report the synthesis, structure, and enzymology of a set of 20 smSNAREs (small molecule SNAr-electrophiles). These smSNAREs mimic (electronically) the canonical GST substrate 1-chloro-2,4-dinitrobenzene (CDNB), and bear a wide variety of bioorthogonal functionalities such as alkynes, aldehydes, acetals, and azides. Sixteen analogues including the chloro- and nitro substituted 1, 3, 5, 6, 7, 11, 12, and 13 participated in the GST-catalyzed conjugation, indicating the substrate tolerance of the enzymatic H-site of SjGST. Using UV-vis spectroscopy, we estimate the efficiency of conjugation as a function of substrate diversity. Using LC-MS, we characterized the conjugates formed under each enzymatic transformation. Significant deviations from the canonical CDNB architecture are tolerated. Relative rates between nitro and chloro substituents indicate the nucleophilic addition step is rate determining. Enzyme immobilization on glass slides is affected by additional surface interactions and therefore does not reflect kinetic profiles observed in solution. This new class of heterobifunctional linkers enables a single-step and uniform protein capture on designer surfaces.

  DOI：

  10.1021/jo401278x

文献信息

• Self-Catalyzed Immobilization of GST-Fusion Proteins for Genome-Encoded Biochips
  作者：Alden E. Voelker、Rajesh Viswanathan

  DOI：10.1021/bc400128g

  日期：2013.8.21

  conjugation products with 5 in the presence of the enzyme. As an application of this protein capture technology, we printed alkaloid biosynthesis enzyme, isonitrile synthase (IsnA), to result in a biochip. Because proteins bearing a GST-fusion purification tag are commonly created through the pGEX expression system, these findings show broad potential applicability to genome-wide studies and proteomic platforms

  随着近年来从基因组测序项目中获得的蛋白质组学信息激增，用于制造蛋白质生物芯片的选择性和鲁棒性技术已变得越来越受欢迎。在这里，我们描述了小分子SNAr亲电试剂（smSNAREs）的发展，这是一类新型的捕获探针，可对蛋白质生物芯片进行选择性的单步固定。这种酶学驱动的方法依赖于Sj GST的结合和催化机制。我们设计并合成了基于机制的底物类似物3，4，和5作为谷胱甘肽S-转移酶（GST）或其任何融合蛋白结合的亲电前体。当在存在这些探针缀合评价谷胱甘肽Sj的通过紫外可见分光法（UV-VIS）和LC-MS技术GST，我们发现，3，4，和5分别转移到GSH。通过将炔5作为smSNARE探针锚定在玻璃表面上，我们证明了Sj GST的单步自催化固定化。荧光成像定量显示Sj的选择性结合增加了18倍GST超过蛋白质的随机方向（由于非特异性结合）。GST和smSNARE表面之间的结合牢固，在加至100 mM GS