2H,2H,3H,3H-perfluoro-10-methylundecanoic acid | 1353722-00-5

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: 2H,2H,3H,3H-perfluoro-10-methylundecanoic acid
• CAS: 1353722-00-5
• 化学式: C₁₂H₅F₁₉O₂
• 分子量: 542.14
• InChiKey: ZATDISOCOGDWST-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  6.5
• 重原子数：
  33.0
• 可旋转键数：
  9.0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.92
• 拓扑面积：
  37.3
• 氢给体数：
  1.0
• 氢受体数：
  1.0

反应信息

• 作为反应物：
  描述：

  2H,2H,3H,3H-perfluoro-10-methylundecanoic acid 、 O-(N-succinimidyl)-N,N,N',N'-tetramethyluronium tetrafluoroborate 在 N,N-二异丙基乙胺 作用下， 以 四氢呋喃 为溶剂， 以52%的产率得到2,5-dioxopyrrolidine-1-yl 4,4,5,5,6,6,7,7,8,8,9,9,10,11,11,11-hexadecafluoro-10-(trifluoromethyl)undecanoate
  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

• 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.