3,4-Bis(4-fluorophenoxy)cyclobut-3-ene-1,2-dione | 1253286-59-7

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 3,4-Bis(4-fluorophenoxy)cyclobut-3-ene-1,2-dione
• 英文别名: 3,4-bis(4-fluorophenoxy)cyclobut-3-ene-1,2-dione
• CAS: 1253286-59-7
• 化学式: C₁₆H₈F₂O₄
• 分子量: 302.234
• InChiKey: YVXATDQMBWFKTG-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.2
• 重原子数：
  22
• 可旋转键数：
  4
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  52.6
• 氢给体数：
  0
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  3,4-Bis(4-fluorophenoxy)cyclobut-3-ene-1,2-dione 、 单-6-O-氨基-Β-环糊精 以 水 、 N,N-二甲基甲酰胺 、 丙酮 为溶剂， 生成 3-(4-fluorophenoxy)-4-[[(1S,3R,5R,6S,8R,10R,11S,13R,15R,16S,18R,20R,21S,23R,25R,26S,28R,30R,31S,33R,35R,36R,37R,38R,39R,40R,41R,42R,43R,44R,45R,46R,47R,48R,49R)-36,37,38,39,40,41,42,43,44,45,46,47,48,49-tetradecahydroxy-10,15,20,25,30,35-hexakis(hydroxymethyl)-2,4,7,9,12,14,17,19,22,24,27,29,32,34-tetradecaoxaoctacyclo[31.2.2.23,6.28,11.213,16.218,21.223,26.228,31]nonatetracontan-5-yl]methylamino]cyclobut-3-ene-1,2-dione
  参考文献：
  名称：

  Modification of Proteins with Cyclodextrins Prevents Aggregation and Surface Adsorption and Increases Thermal Stability

  摘要：

  This work describes a general approach for preventing protein aggregation and surface adsorption by modifying proteins with beta-cyclodextrins (beta CD) via an efficient water-driven ligation. As compared to native unmodified proteins, the cyclodextrin-modified proteins (lysozyme and RNase A) exhibit significant reduction in aggregation, surface adsorption and increase in thermal stability. These results reveal a new chemistry for preventing protein aggregation and surface adsorption that is likely of different mechanisms than that by modifying proteins with poly(ethylene glycol).

  DOI：

  10.1021/la203271u
• 作为产物：
  描述：

  3,4-二氯-3-环丁烯-1,2-二酮 、 4-氟苯酚 在 三乙胺 作用下， 以 苯 为溶剂， 生成 3,4-Bis(4-fluorophenoxy)cyclobut-3-ene-1,2-dione
  参考文献：
  名称：

  Modification of Proteins with Cyclodextrins Prevents Aggregation and Surface Adsorption and Increases Thermal Stability

  摘要：

  This work describes a general approach for preventing protein aggregation and surface adsorption by modifying proteins with beta-cyclodextrins (beta CD) via an efficient water-driven ligation. As compared to native unmodified proteins, the cyclodextrin-modified proteins (lysozyme and RNase A) exhibit significant reduction in aggregation, surface adsorption and increase in thermal stability. These results reveal a new chemistry for preventing protein aggregation and surface adsorption that is likely of different mechanisms than that by modifying proteins with poly(ethylene glycol).

  DOI：

  10.1021/la203271u

文献信息

• METHOD OF COVALENTLY MODIFYING PROTEINS WITH ORGANIC MOLECULES TO PREVENT AGGREGATION
  申请人：Luk Yan-Yeung

  公开号：US20100273991A1

  公开（公告）日：2010-10-28

  A system and method for preventing protein aggregation is developed by covalent modification of proteins with organic molecules that can preserve the native protein folding. Proteins are covalently modified with sugar alcohols or cyclodextrins (organic Kosmotropes) or other small molecule drugs by water-driven bioorganic reactions in water. In the water-driven bioorganic reactions, the reagent is stable in water and can modify lysine residues or cysteine residue of a protein at physiological conditions with high yield and fast rate. Proteins and antibodies will be modified by non-natural sugar alcohols. As a result, the efficacy of protein drugs (reduction in aggregation and enzymatic degradation, and increase in blood stream life time) may be improved.
• Modification of Proteins with Cyclodextrins Prevents Aggregation and Surface Adsorption and Increases Thermal Stability
  作者：Deepali Prashar、DaWei Cui、Debjyoti Bandyopadhyay、Yan-Yeung Luk

  DOI：10.1021/la203271u

  日期：2011.11.1

  This work describes a general approach for preventing protein aggregation and surface adsorption by modifying proteins with beta-cyclodextrins (beta CD) via an efficient water-driven ligation. As compared to native unmodified proteins, the cyclodextrin-modified proteins (lysozyme and RNase A) exhibit significant reduction in aggregation, surface adsorption and increase in thermal stability. These results reveal a new chemistry for preventing protein aggregation and surface adsorption that is likely of different mechanisms than that by modifying proteins with poly(ethylene glycol).