N-琥珀酰亚胺基 4,4,5,5,6,6,7,7,8,8,9,9,9-十三氟壬酸酯 | 1262770-54-6

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吡咯烷类
• 中文名称: N-琥珀酰亚胺基 4,4,5,5,6,6,7,7,8,8,9,9,9-十三氟壬酸酯
• 中文别名: N-琥珀酰亚胺基4,4,5,5,6,6,7,7,8,8,9,9,9-十三氟壬酸酯
• 英文名称: 2,5-dioxopyrrolidine-1-yl 4,4,5,5,6,6,7,7,8,8,9,9,9-tridecafluorononanoate
• 英文别名: 1-[(4,4,5,5,6,6,7,7,8,8,9,9,9-Tridecafluorononanoyl)oxy]pyrrolidine-2,5-dione；(2,5-dioxopyrrolidin-1-yl) 4,4,5,5,6,6,7,7,8,8,9,9,9-tridecafluorononanoate
• CAS: 1262770-54-6
• 化学式: C₁₃H₈F₁₃NO₄
• 分子量: 489.19
• InChiKey: ATDSDUMFZUDFRA-UHFFFAOYSA-N

物化性质

• 熔点：
  127-131°C

计算性质

• 辛醇/水分配系数(LogP)：
  4
• 重原子数：
  31
• 可旋转键数：
  9
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.77
• 拓扑面积：
  63.7
• 氢给体数：
  0
• 氢受体数：
  17

反应信息

• 作为产物：
  描述：

  O-(N-succinimidyl)-N,N,N',N'-tetramethyluronium tetrafluoroborate 、 4,4,5,5,6,6,7,7,8,8,9,9,9-十三氟壬酸 在 N,N-二异丙基乙胺 作用下， 以 四氢呋喃 为溶剂， 以38%的产率得到N-琥珀酰亚胺基 4,4,5,5,6,6,7,7,8,8,9,9,9-十三氟壬酸酯
  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

• [EN] FLUORINATED HYDROPHOBIN AND USES THEREOF<br/>[FR] HYDROPHOBINE FLUORÉE ET SES UTILISATIONS
  申请人：FOND ISTITUTO ITALIANO DI TECNOLOGIA

  公开号：WO2013080133A1

  公开（公告）日：2013-06-06

  Modified protein comprising a molecule of hydrophobin and at least one fluorocarbon group bound covalently to an amino acid of hydrophobin, obtainable by reaction of a hydrophobin with a fluorinated compound of formula: Y-RH-RF, in which Y is a functional group capable of reacting with an amino acid residue of the hydrophobin forming a covalent bond between the fluorinated compound and said amino acid of the hydrophobin, RH is an optional hydrocarbon group, non-fluorinated, aliphatic and/or aromatic, optionally including heteroatoms, and RF is a fluorinated or perfluorinated hydrocarbon residue, linear, branched or cyclic, optionally including one or more heteroatoms.
• 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.