N-(1,10-phenanthrolin-5-yl)octanamide

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 菲咯啉
• 英文名称: N-(1,10-phenanthrolin-5-yl)octanamide
• 化学式: C₂₀H₂₃N₃O
• 分子量: 321.422
• InChiKey: BHRAFZFVNVWLMZ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.6
• 重原子数：
  24
• 可旋转键数：
  7
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.35
• 拓扑面积：
  54.9
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  1,10-菲罗啉-5-氨基 、 辛酰氯 在 碳酸氢钠 作用下， 以 水 为溶剂， 反应 3.0h， 生成 N-(1,10-phenanthrolin-5-yl)octanamide
  参考文献：
  名称：

  Role of amphiphilic [metal:chelator] complexes in a non-chromatographic antibody purification platform

  摘要：

  We have recently introduced a non-chromatographic alternative for antibody (Ab) purification, one which does not require the use of Protein A. With this approach, polyclonal human or mouse immtmoglobulins (IgG's) are captured almost quantitatively by Tween-20 micelles conjugated with a [chelator:divalent metal cation] complex. Target IgG structure remains native even following extraction from the surfactant aggregate. In the present work, we explore the effect of varying both components of the [metal:chelator] pair on the yield of purified Ab. Capture efficiency is observed to correlate with the formation of sufficiently large detergent aggregates, as determined by dynamic light scattering (DLS) and polyacrylamide gel electrophoresis (PAGE). This, in turn, depends on the rigidity and aromaticity of the chelator. Detergent aggregates are stable over a wide range of pH values (pH = 3-9). Under acidic conditions (3-3.8) they lead to good IgG recovery yields (70-78%) with purity similar to that obtained with Protein A chromatography while maintaining the monomeric state of the IgG's. Finally, the influence of the environment and the presence of various water-soluble chelators (e.g. EDTA, histidine, imidazole) on process efficiency, is described.

  DOI：

  10.1016/j.jchromb.2019.121830

文献信息

• METHODS OF ANALYZING CELL MEMBRANES
  申请人：Ariel-University Research and Development Company Ltd.

  公开号：US20170121668A1

  公开（公告）日：2017-05-04

  A method of precipitating cell membrane fragments from a cell lysate is disclosed. The method comprises contacting the cell lysate with a hydrophobic chelator and a metal ion under conditions that allow precipitation of the cell membrane fragments. Kits for precipitating cell membrane fragments are also disclosed.

  本发明公开了一种从细胞裂解液中沉淀细胞膜碎片的方法。该方法包括在允许细胞膜碎片沉淀的条件下，将细胞裂解液与疏水螯合剂和金属离子接触。此外，本发明还公开了用于沉淀细胞膜碎片的试剂盒。
• Methods of analyzing cell membranes
  申请人：Ariel-University Research and Development Company Ltd.

  公开号：US10030224B2

  公开（公告）日：2018-07-24

  A method of precipitating cell membrane fragments from a cell lysate is disclosed. The method comprises contacting the cell lysate with a hydrophobic chelator and a metal ion under conditions that allow precipitation of the cell membrane fragments. Kits for precipitating cell membrane fragments are also disclosed.

  本发明公开了一种从细胞裂解液中沉淀细胞膜片段的方法。该方法包括在允许细胞膜片段沉淀的条件下，将细胞裂解液与疏水螯合剂和金属离子接触。还公开了用于沉淀细胞膜片段的试剂盒。
• METHODS OF PURIFYING ANTIBODIES
  申请人：Ariel Scientific Innovations Ltd.

  公开号：US20200102372A1

  公开（公告）日：2020-04-02

  A method of isolating an antibody is disclosed. The method comprises contacting a hydrophobic chelator, a non-ionic detergent and metal ions so as to generate an aggregate comprising the hydrophobic chelator, the detergent and the metal ions; and contacting the aggregate with a medium comprising the antibody under conditions that allow partitioning of the antibody into the aggregate. Kits for isolating the antibody are also disclosed.
• Role of amphiphilic [metal:chelator] complexes in a non-chromatographic antibody purification platform
  作者：Gunasekaran Dhandapani、Divya K. Nair、Raju R. Kale、Ellen Wachtel、Irishi N.N. Namboothiri、Guy Patchornik

  DOI：10.1016/j.jchromb.2019.121830

  日期：2019.12

  We have recently introduced a non-chromatographic alternative for antibody (Ab) purification, one which does not require the use of Protein A. With this approach, polyclonal human or mouse immtmoglobulins (IgG's) are captured almost quantitatively by Tween-20 micelles conjugated with a [chelator:divalent metal cation] complex. Target IgG structure remains native even following extraction from the surfactant aggregate. In the present work, we explore the effect of varying both components of the [metal:chelator] pair on the yield of purified Ab. Capture efficiency is observed to correlate with the formation of sufficiently large detergent aggregates, as determined by dynamic light scattering (DLS) and polyacrylamide gel electrophoresis (PAGE). This, in turn, depends on the rigidity and aromaticity of the chelator. Detergent aggregates are stable over a wide range of pH values (pH = 3-9). Under acidic conditions (3-3.8) they lead to good IgG recovery yields (70-78%) with purity similar to that obtained with Protein A chromatography while maintaining the monomeric state of the IgG's. Finally, the influence of the environment and the presence of various water-soluble chelators (e.g. EDTA, histidine, imidazole) on process efficiency, is described.