(E)-3-((2-(pyridin-2-yl)ethyl)imino)-1λ2-indolin-2-one

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: (E)-3-((2-(pyridin-2-yl)ethyl)imino)-1λ2-indolin-2-one
• 英文别名: 3-(2-pyridin-2-ylethylimino)-1H-indol-2-one
• 化学式: C₁₅H₁₃N₃O
• 分子量: 251.288
• InChiKey: TXGIIBFUWKSDFJ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.8
• 重原子数：
  19
• 可旋转键数：
  3
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.13
• 拓扑面积：
  54.4
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  (E)-3-((2-(pyridin-2-yl)ethyl)imino)-1λ2-indolin-2-one 、 zinc(II) chloride 在 sodium hydroxide 作用下， 以 水 为溶剂， 以90%的产率得到[Zn((E)-3-((2-(pyridin-2-yl)ethyl)imino)-1λ²-indolin-2-one)Cl₂]
  参考文献：
  名称：

  Comparative studies of oxindolimine-metal complexes as inhibitors of human DNA topoisomerase IB

  摘要：

  Copper(II) and zinc(II) complexes with oxindolimine ligands, obtained by a condensation reaction between isatin (1H-indole-2,3-dione) and 2-(2-aminoethyl)pyridine, have been previously shown to activate apoptosis very efficiently in different cancer cell lines. Here, we show that these compounds inhibit human DNA topoisomerase IB (Topo I) activity, and this characteristic may be implicated in its pro-apoptotic and potential antitumor properties. The studied metal complexes prevent DNA relaxation and cleavage reaction, whilst they do not have any effect on the religation process. The protein inhibition occurs in two different ways since the copper compound does not permit the enzyme-DNA complex formation, while the zinc analogue permits this complex formation but inhibits the catalytic cleavage reaction. Other related copper and zinc complexes, one with an asymmetric imine ligand derived from isatin, 1,3-diaminopropane, and salicyladehyde, and another one previously reported, derived from isatin and 1,3-diaminopropane, had their corresponding inhibition results towards Topo I compared. These data demonstrated that such complexes can act as good catalytic inhibitors of Topo I, in a process modulated by the ligand features and the nature of the metal ion. Computational studies complemented and supported experimental data, showing three different characteristics of the metal complexes that influence its interaction and consequent inhibition of Topo I. The ligand planarity when bound to the protein increases the occurring interactions in different binding sites, the total charge of the complex modulates the preferential region of interaction, and the copper(II) complexes are expected to be more efficient inhibitors compared to analogous zinc(II), as verified experimentally.

  DOI：

  10.1016/j.jinorgbio.2018.05.012
• 作为产物：
  描述：

  2-(2-氨乙基)吡啶 、 靛红 在 盐酸 作用下， 以 乙醇 、 水 为溶剂， 生成 (E)-3-((2-(pyridin-2-yl)ethyl)imino)-1λ2-indolin-2-one
  参考文献：
  名称：

  Comparative studies of oxindolimine-metal complexes as inhibitors of human DNA topoisomerase IB

  摘要：

  Copper(II) and zinc(II) complexes with oxindolimine ligands, obtained by a condensation reaction between isatin (1H-indole-2,3-dione) and 2-(2-aminoethyl)pyridine, have been previously shown to activate apoptosis very efficiently in different cancer cell lines. Here, we show that these compounds inhibit human DNA topoisomerase IB (Topo I) activity, and this characteristic may be implicated in its pro-apoptotic and potential antitumor properties. The studied metal complexes prevent DNA relaxation and cleavage reaction, whilst they do not have any effect on the religation process. The protein inhibition occurs in two different ways since the copper compound does not permit the enzyme-DNA complex formation, while the zinc analogue permits this complex formation but inhibits the catalytic cleavage reaction. Other related copper and zinc complexes, one with an asymmetric imine ligand derived from isatin, 1,3-diaminopropane, and salicyladehyde, and another one previously reported, derived from isatin and 1,3-diaminopropane, had their corresponding inhibition results towards Topo I compared. These data demonstrated that such complexes can act as good catalytic inhibitors of Topo I, in a process modulated by the ligand features and the nature of the metal ion. Computational studies complemented and supported experimental data, showing three different characteristics of the metal complexes that influence its interaction and consequent inhibition of Topo I. The ligand planarity when bound to the protein increases the occurring interactions in different binding sites, the total charge of the complex modulates the preferential region of interaction, and the copper(II) complexes are expected to be more efficient inhibitors compared to analogous zinc(II), as verified experimentally.

  DOI：

  10.1016/j.jinorgbio.2018.05.012

文献信息

• Kinetic studies of carbohydrate oxidation catalyzed by novel isatin–Schiff base copper(II) complexes
  作者：Giselle Cerchiaro、Gustavo A. Micke、Marina Franco Maggi Tavares、Ana Maria da Costa Ferreira

  DOI：10.1016/j.molcata.2004.06.017

  日期：2004.11

  With the aim of elucidating the mechanism of oxidative processes initiated by copper(II)-carbohydrate interactions, new isatin-Schiff base copper(II) complexes, [Cu(isaen)H2O]ClO(4)(.)2H(2)O (1), and [Cu(isaepy)(2)](ClO4)(2)(.)2H(2)O (2), where isaen = N-[(3-indolin-2-one)]-1,3-ethylenediamine and isaepy = N-[(3-indolin-2-one)]-2-aminoethyl pyridine were isolated, and characterized by elemental analyses, UV-vis, FTIR, EPR, and molar conductivity measurements. These imine ligands are capable of modifying selectively the environment of the copper(II) ion in a pH controlled process, through keto-enolic equilibria similar to those occurring with carbohydrates. Therefore, the obtained complexes had their catalytic activity in the oxidation of common carbohydrates (glucose, fructose and galactose) by molecular oxygen, compared to that of an analogous complex [Cu(isapn)](ClO4)(2) (3), previously reported. The determined rate law, from kinetic curves of oxygen consumption, showed a pseudo-first-order dependence both on the catalyst and substrate concentrations, followed by a saturation effect, for all the compounds studied. Further, the pH profile indicated that reaction occurs significantly only in very alkaline medium (pH greater than or equal to 10), and some influence of ionic strength (controlled by carbonate buffer) was also verified. The participation of very reactive intermediates in the oxidative degradation of the substrates was monitored by EPR spin trapping, while final products were identified by capillary electrophoresis. An extensive mechanism is proposed, explaining new kinetic studies as well as earlier data. (C) 2004 Elsevier B.V. All rights reserved.
• Comparative studies of oxindolimine-metal complexes as inhibitors of human DNA topoisomerase IB
  作者：Silvia Castelli、Marcos Brown Gonçalves、Prafulla Katkar、Gabriela Cristina Stuchi、Ricardo Alexandre Alves Couto、Helena Maria Petrilli、Ana Maria da Costa Ferreira

  DOI：10.1016/j.jinorgbio.2018.05.012

  日期：2018.9

  Copper(II) and zinc(II) complexes with oxindolimine ligands, obtained by a condensation reaction between isatin (1H-indole-2,3-dione) and 2-(2-aminoethyl)pyridine, have been previously shown to activate apoptosis very efficiently in different cancer cell lines. Here, we show that these compounds inhibit human DNA topoisomerase IB (Topo I) activity, and this characteristic may be implicated in its pro-apoptotic and potential antitumor properties. The studied metal complexes prevent DNA relaxation and cleavage reaction, whilst they do not have any effect on the religation process. The protein inhibition occurs in two different ways since the copper compound does not permit the enzyme-DNA complex formation, while the zinc analogue permits this complex formation but inhibits the catalytic cleavage reaction. Other related copper and zinc complexes, one with an asymmetric imine ligand derived from isatin, 1,3-diaminopropane, and salicyladehyde, and another one previously reported, derived from isatin and 1,3-diaminopropane, had their corresponding inhibition results towards Topo I compared. These data demonstrated that such complexes can act as good catalytic inhibitors of Topo I, in a process modulated by the ligand features and the nature of the metal ion. Computational studies complemented and supported experimental data, showing three different characteristics of the metal complexes that influence its interaction and consequent inhibition of Topo I. The ligand planarity when bound to the protein increases the occurring interactions in different binding sites, the total charge of the complex modulates the preferential region of interaction, and the copper(II) complexes are expected to be more efficient inhibitors compared to analogous zinc(II), as verified experimentally.