ethyl 4-(4-acetyl-3-hydroxyphenoxy)butanoate | 1608463-36-0

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: ethyl 4-(4-acetyl-3-hydroxyphenoxy)butanoate
• 英文别名: Ethyl 4-(4-acetyl-3-hydroxyphenoxy)butanoate
• CAS: 1608463-36-0
• 化学式: C₁₄H₁₈O₅
• 分子量: 266.294
• InChiKey: FGSFTNPZKSCWNV-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.32
• 重原子数：
  19.0
• 可旋转键数：
  7.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.43
• 拓扑面积：
  72.83
• 氢给体数：
  1.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  ethyl 4-(4-acetyl-3-hydroxyphenoxy)butanoate 在 (1,1'-bis(diphenylphosphino)ferrocene)palladium(II) dichloride 、 sodium acetate 、 三乙胺 、 三氟乙酸 作用下， 以 1,4-二氧六环 、 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 9.0h， 生成
  参考文献：
  名称：

  Targeting cancer cells with folic acid–iminoboronate fluorescent conjugates

  摘要：

  在此我们展示了荧光2-乙酰基苯硼酸的合成，这些化合物与溶菌酶和N-(2-氨基乙基)叶酸（EDA-FA）发生B-N促进的缔合，生成的缔合物可被过度表达叶酸受体的癌细胞特异性识别和内化。

  DOI：

  10.1039/c3cc47534d
• 作为产物：
  描述：

  2,4-二羟基苯乙酮 、 4-溴丁酸乙酯 在 potassium carbonate 、 sodium iodide 作用下， 以 丙酮 为溶剂， 反应 28.0h， 以68%的产率得到ethyl 4-(4-acetyl-3-hydroxyphenoxy)butanoate
  参考文献：
  名称：

  Aldehydes can switch the chemoselectivity of electrophiles in protein labeling

  摘要：

  电荷亲合物的衍生化可以改变其化学选择性。醛共轭环氧化物和磺酸酯提供了原则证明，并提供了N-末端标记的蛋白质。

  DOI：

  10.1039/c8ob02897d

文献信息

• Single-Site Labeling of Native Proteins Enabled by a Chemoselective and Site-Selective Chemical Technology
  作者：Srinivasa Rao Adusumalli、Dattatraya Gautam Rawale、Usha Singh、Prabhanshu Tripathi、Rajesh Paul、Neetu Kalra、Ram Kumar Mishra、Sanjeev Shukla、Vishal Rai

  DOI：10.1021/jacs.8b10490

  日期：2018.11.7

  Chemical biology research often requires precise covalent attachment of labels to the native proteins. Such methods are sought after to probe, design, and regulate the properties of proteins. At present, this demand is largely unmet due to the lack of empowering chemical technology. Here, we report a chemical platform that enables site-selective labeling of native proteins. Initially, a reversible intermolecular reaction places the "chemical linchpins" globally on all the accessible Lys residues. These linchpins have the capability to drive site-selective covalent labeling of proteins. The linchpin detaches within physiological conditions and capacitates the late-stage installation of various tags. The chemical platform is modular, and the reagent design regulates the site of modification. The linchpin is a multitasking group and facilitates purification of the labeled protein eliminating the requirement of additional chromatography tag. The methodology allows the labeling of a single protein in a mixture of proteins. The precise modification of an accessible residue in protein ensures that their structure remains unaltered. The enzymatic activity of myoglobin, cytochrome C, aldolase, and lysozyme C remains conserved after labeling. Also, the cellular uptake of modified insulin and its downstream signaling process remain unperturbed. The linchpin directed modification (LDM) provides a convenient route for the conjugation of a fluorophore and drug to a Fab and monoclonal antibody. It delivers trastuzumab-doxorubicin and trastuzumab-emtansine conjugates with selective antiproliferative activity toward Her-2 positive SKBR-3 breast cancer cells.