[Cu(npmp)2] | 84821-33-0

• 英文名称: [Cu(npmp)2]
• 英文别名: [Cu(npmp)₂]
• CAS: 84821-33-0
• 化学式: C₂₆H₁₈CuN₄O₆
• 分子量: 545.998
• InChiKey: VCTIAUIAYSYLMZ-ZNVPEIAMSA-L

计算性质

• 辛醇/水分配系数(LogP)：
  None
• 重原子数：
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• 可旋转键数：
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• 环数：
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• sp3杂化的碳原子比例：
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• 拓扑面积：
  None
• 氢给体数：
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• 氢受体数：
  None

反应信息

• 作为产物：
  描述：

  在 吡啶 、 苯胺 作用下， 以 氯仿 为溶剂， 生成 [Cu(npmp)2]
  参考文献：
  名称：

  Talzi, E. P.; Nekipelov, V. M.; Zamaraev, K. I., Russian Journal of Physical Chemistry, 1984, vol. 58, p. 165 - 178

  摘要：

  DOI：

文献信息

• 2-Phenyliminomethylphenols, 2-phenylaminomethylphenols and their copper(II) complexes
  作者：H.J. Harries、B.F. Orford、J. Burgess

  DOI：10.1016/s0020-1693(00)88934-3

  日期：1983.1

  2-phenyliminomethylphenols (I) and 2-phenylaminomethylphenols (II) are described. Acid dissociation constants, determined potentiometrically, for the amines (II) are related to substituent constants; values are not obtained for Schiff bases(I) due to their hydrolysis. IR spectra of the amines (II) indicate chelate ring formation via OH⋯N hydrogen bonding. NMR spectra for Schiff bases (I) are consistent

  摘要描述了2-苯基亚氨基甲基苯酚（I）和2-苯基氨基甲基苯酚（II）的合成。电位测定的胺（II）的酸解离常数与取代基常数有关。由于席夫碱（I）的水解作用，因此无法获得这些值。胺（II）的红外光谱表明通过OH⋯N氢键形成螯合环。Schiff碱（I）的NMR光谱与酚亚胺互变异构体一致，而不与酮胺互变异构体一致。配体（I）与铜（II）形成双配合物，而胺（II）在乙酸根阴离子存在下形成铜（II）配合物；这些材料的磁测量表明在固态下没有金属与金属的相互作用。
• Synthesis and evaluation of copper complexes of Schiff-base condensates from 5-substituted-2-hydroxybenzaldehyde and 2-substituted-benzenamine as selective inhibitors of protein tyrosine phosphatases
  作者：Ruiting Zhu、Liping Lu、Miaoli Zhu、Hong Han、Caixia Yuan、Shu Xing、Xueqi Fu

  DOI：10.1016/j.ica.2013.05.018

  日期：2013.8

  Five copper complexes, [Cu(bhbb,chbb,ohbb)(H2O)(n)] (tridentate-ligands: H(2)bhbb = 2-(5-bromo-2-hydroxylbenzylideneamino)benzoic acid, 1; H(2)chbb = 2-(5-chloro-2-hydroxylbenzylideneamino)benzoic acid, 2; H(2)nhbb = 2-(5-nitro-2-hydroxyl-benzylideneamino)benzoic acid, 3) and [Cu(cpmp,npmp)(2)] (bidentate-ligands: Hcpmp = 4-chloro-2-((phenylimino)methyl)phenol, 4; Hnpmp = 4-bromo-2-((phenyl-imino)methyl)phenol, 5) have been prepared and characterized by EA, IR, EPR UV-Vis, and ESI-MS. Structure-activity relationship of copper complexes in inhibiting protein tyrosine phosphatases (protein tyrosine phosphatase 1B, PTP1B; T-cell protein tyrosine phosphatase, TCPTP; megakaryocyte protein-tyrosine phosphatase, PTP-MEG2; Src homology phosphatase 1, SHP-1 and Src homology phosphatase 2, SHP-2) is investigated. Inhibitory activities of complexes against the five PTPs indicate that they potently inhibit PTP1B, TCPTP, PTP-MEG2 and SHP-1, but do not inhibit SHP-2. In the complexes, 5 exhibits very strong inhibition (IC50, 0.059 mu M) and better selectivity against PTP1B while 1 and 2 show very strong inhibition (IC50 = 0.089 and 0.067 mu M) and a little selectivity against TCPTP. Compared with the oxovanadium(IV) complexes of same ligands, the copper complexes increase the inhibitory ability against TCPTP, PTP-MEG2 and SHP-1 but decrease the inhibition against SHP-2. For complex 5, the inhibition over PTP1B, TCPTP, PTP-MEG2 and SHP-1 are all improved about 5- to 15-fold compared with the oxovanadium(IV) complex. The results demonstrate that both the ligand structures and the center metals influence the inhibition and selectivity against different PTPs. (C) 2013 Elsevier B.V. All rights reserved.