2,5-dioxopyrrolidine-1-yl 4,4,5,5,6,6,7,7,7-nonafluoroheptanoate | 852527-43-6

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吡咯烷类
• 英文名称: 2,5-dioxopyrrolidine-1-yl 4,4,5,5,6,6,7,7,7-nonafluoroheptanoate
• 英文别名: 1-[(4,4,5,5,6,6,7,7,7-Nonafluoroheptanoyl)oxy]pyrrolidine-2,5-dione；(2,5-dioxopyrrolidin-1-yl) 4,4,5,5,6,6,7,7,7-nonafluoroheptanoate
• CAS: 852527-43-6
• 化学式: C₁₁H₈F₉NO₄
• 分子量: 389.174
• InChiKey: LNFNFGXVSPNQIW-UHFFFAOYSA-N

物化性质

• 沸点：
  286.5±50.0 °C(Predicted)
• 密度：
  1.60±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.6
• 重原子数：
  25
• 可旋转键数：
  7
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.73
• 拓扑面积：
  63.7
• 氢给体数：
  0
• 氢受体数：
  13

反应信息

• 作为产物：
  描述：

  O-(N-succinimidyl)-N,N,N',N'-tetramethyluronium tetrafluoroborate 、 4,4,5,5,6,6,7,7,7-九氟庚酸 在 N,N-二异丙基乙胺 作用下， 以 四氢呋喃 为溶剂， 以34%的产率得到2,5-dioxopyrrolidine-1-yl 4,4,5,5,6,6,7,7,7-nonafluoroheptanoate
  参考文献：
  名称：

  Perfluoroalkyl Chains Direct Novel Self-Assembly of Insulin

  摘要：

  The self-assembly of biopharmaceutical peptides into multimeric, nanoscale objects, as well as their disassembly to monomers, is central for their mode of action. Here, we describe a bioorthogonal strategy, using a non-native recognition principle, for control of protein self-assembly based on intermolecular fluorous interactions and demonstrate it for the small protein insulin. Perfluorinated alkyl chains of varying length were attached to desB30 human insulin by acylation of the E-amine of the side-chain of LysB29. The insulin analogues were formulated with Zn-II and phenol to form hexamers. The self-segregation of fluorous groups directed the insulin hexamers to self-assemble. The structures of the systems were investigated by circular dichroism I (CD) spectroscopy and synchrotron small-angle X-ray scattering. Also, the binding affinity to the 4 insulin receptor was measured. Interestingly, varying the length of the perfluoroalkyl chain provided three different scenarios for self-assembly; the short chains hardly affected the native hexameric structure, the medium-length chains induced fractal-like structures with the insulin hexamer as the fundamental building block, while the longest chains lead to the formation of structures with local cylindrical geometry. This hierarchical self-assembly system, which combines Zn-II mediated hexamer formation with fluorous interactions, is a promising tool to control the formation of high molecular weight complexes of insulin and potentially other proteins.

  DOI：

  10.1021/la203042c

文献信息

• FLUOROUS LABELING FOR SELECTIVE PROCESSING OF BIOLOGICALLY-DERIVED SAMPLES
  申请人：IRM, LLC

  公开号：EP1687643A1

  公开（公告）日：2006-08-09
• Fluorous labeling for selective processing of biologically-derived samples
  申请人：Peters Eric

  公开号：US20060263886A1

  公开（公告）日：2006-11-23

  This invention provides fluorous-based methods and compositions for preparation, separation and analysis of complex biologically-derived samples, such as proteomic and metabolomic samples.
• [EN] FLUOROUS LABELING FOR SELECTIVE PROCESSING OF BIOLOGICALLY-DERIVED SAMPLES<br/>[FR] MARQUAGE FLUORESCENT DESTINE A UN TRAITEMENT SELECTIF D'ECHANTILLONS DERIVES BIOLOGIQUEMENT
  申请人：IRM LLC

  公开号：WO2005050226A1

  公开（公告）日：2005-06-02

  This invention provides fluorous-based methods and compositions for preparation, separation and analysis of complex biologically-derived samples, such as proteomic and metabolomic samples.
• Perfluoroalkyl Chains Direct Novel Self-Assembly of Insulin
  作者：Leila Malik、Jesper Nygaard、Rasmus Hoiberg-Nielsen、Lise Arleth、Thomas Hoeg-Jensen、Knud J. Jensen

  DOI：10.1021/la203042c

  日期：2012.1.10

  The self-assembly of biopharmaceutical peptides into multimeric, nanoscale objects, as well as their disassembly to monomers, is central for their mode of action. Here, we describe a bioorthogonal strategy, using a non-native recognition principle, for control of protein self-assembly based on intermolecular fluorous interactions and demonstrate it for the small protein insulin. Perfluorinated alkyl chains of varying length were attached to desB30 human insulin by acylation of the E-amine of the side-chain of LysB29. The insulin analogues were formulated with Zn-II and phenol to form hexamers. The self-segregation of fluorous groups directed the insulin hexamers to self-assemble. The structures of the systems were investigated by circular dichroism I (CD) spectroscopy and synchrotron small-angle X-ray scattering. Also, the binding affinity to the 4 insulin receptor was measured. Interestingly, varying the length of the perfluoroalkyl chain provided three different scenarios for self-assembly; the short chains hardly affected the native hexameric structure, the medium-length chains induced fractal-like structures with the insulin hexamer as the fundamental building block, while the longest chains lead to the formation of structures with local cylindrical geometry. This hierarchical self-assembly system, which combines Zn-II mediated hexamer formation with fluorous interactions, is a promising tool to control the formation of high molecular weight complexes of insulin and potentially other proteins.