3,3'-bis[(2,2'-dipicolylamino)methyl]biphenyl | 879088-98-9

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: 3,3'-bis[(2,2'-dipicolylamino)methyl]biphenyl
• 英文别名: 1-[3-[3-[[bis(pyridin-2-ylmethyl)amino]methyl]phenyl]phenyl]-N,N-bis(pyridin-2-ylmethyl)methanamine
• CAS: 879088-98-9
• 化学式: C₃₈H₃₆N₆
• 分子量: 576.744
• InChiKey: VUFFJNOCRFCYSW-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.1
• 重原子数：
  44
• 可旋转键数：
  13
• 环数：
  6.0
• sp3杂化的碳原子比例：
  0.16
• 拓扑面积：
  58
• 氢给体数：
  0
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  3,3'-bis[(2,2'-dipicolylamino)methyl]biphenyl 、 zinc(II) nitrate 以 水 、 乙腈 为溶剂， 以66%的产率得到[Zn2(3,3'-bis[(2,2'-dipicolylamino)methyl]biphenyl](NO3)4
  参考文献：
  名称：

  Effective Disruption of Phosphoprotein−Protein Surface Interaction Using Zn(II) Dipicolylamine-Based Artificial Receptors via Two-Point Interaction

  摘要：

  Protein phosphorylation is ubiquitously involved in living cells, and it is one of the key events controlling protein-protein surface interactions, which are essential in signal transduction cascades. We now report that the small molecular receptors bearing binuclear Zn(ll)-Dpa can strongly bind to a bisphosphorylated peptide in a cross-linking manner under neutral aqueous conditions when the distance between the two Zn(ll) centers can appropriately fit in that of the two phosphate groups of the phosphorylated peptide. The binding property was quantitatively determined by ITC (isothermal titration calorimetry), induced CD (circular dichroism), and NMR. On the basis of these findings, we demonstrated that these types of small molecules were able to effectively disrupt the phosphoprotein-protein interaction in a phosphorylated CTD peptide and the Pin1 WW domain, a phosphoprotein binding domain, at a micromolar level. The strategy based on a small molecular disruptor that directly interacts with phosphoprotein is unique and should be promising in developing a designer inhibitor for phosphoprotein-protein interaction.

  DOI：

  10.1021/ja056585k
• 作为产物：
  描述：

  3,3'-双溴甲基联苯 、 二甲基吡啶胺 在 potassium carbonate 、 potassium iodide 作用下， 以 乙腈 为溶剂， 反应 5.0h， 以48%的产率得到3,3'-bis[(2,2'-dipicolylamino)methyl]biphenyl
  参考文献：
  名称：

  金属离子在人工磷酸二酯酶的催化活性中诱导了变构转变。

  摘要：

  带有两种类型的金属结合位点，催化位点和调节联吡啶位点的人工磷酸二酯酶（）在针对金属浓度的催化活性中表现出独特的变构转变。评估2-羟基丙基-对-硝基苯基磷酸酯（HPNP）和RNA二聚体（ApA）在有或没有效应金属离子的条件下的水解反应速率常数；。（Zn（2 +））（3）（2.0 x 10（-4）s（-1））的HPNP水解的k（obs）值是。（Zn（2+））的HPNP水解的k（obs）值大3.3倍。 （2）。在和Cu（2+）的情况下，。（Cu（2 +））（3）（1.2 x 10（-3）s（-1））对的k（obs）值大19.4倍。 （Cu（2 +））（2）。催化活性的增加归因于效应金属离子与Bpy部分的配位所诱导的构构构象转变。

  DOI：

  10.1039/b716196d

文献信息

• Metal ion induced allosteric transition in the catalytic activity of an artificial phosphodiesterase
  作者：Shinji Takebayashi、Seiji Shinkai、Masato Ikeda、Masayuki Takeuchi

  DOI：10.1039/b716196d

  日期：——

  two types of metal binding sites, a catalytic site and a regulatory bipyridine site showed a unique allosteric transition in the catalytic activity against the metal concentration. The rate constants for the hydrolysis reaction of 2-hydroxypropyl-p-nitrophenyl phosphate (HPNP) and RNA dimer (ApA) with and without an effector metal ion were evaluated; the k(obs) value of HPNP hydrolysis for .(Zn(2+))(3)

  带有两种类型的金属结合位点，催化位点和调节联吡啶位点的人工磷酸二酯酶（）在针对金属浓度的催化活性中表现出独特的变构转变。评估2-羟基丙基-对-硝基苯基磷酸酯（HPNP）和RNA二聚体（ApA）在有或没有效应金属离子的条件下的水解反应速率常数；。（Zn（2 +））（3）（2.0 x 10（-4）s（-1））的HPNP水解的k（obs）值是。（Zn（2+））的HPNP水解的k（obs）值大3.3倍。 （2）。在和Cu（2+）的情况下，。（Cu（2 +））（3）（1.2 x 10（-3）s（-1））对的k（obs）值大19.4倍。 （Cu（2 +））（2）。催化活性的增加归因于效应金属离子与Bpy部分的配位所诱导的构构构象转变。
• Effective Disruption of Phosphoprotein−Protein Surface Interaction Using Zn(II) Dipicolylamine-Based Artificial Receptors via Two-Point Interaction
  作者：Akio Ojida、Masa-aki Inoue、Yasuko Mito-oka、Hiroshi Tsutsumi、Kazuki Sada、Itaru Hamachi

  DOI：10.1021/ja056585k

  日期：2006.2.1

  Protein phosphorylation is ubiquitously involved in living cells, and it is one of the key events controlling protein-protein surface interactions, which are essential in signal transduction cascades. We now report that the small molecular receptors bearing binuclear Zn(ll)-Dpa can strongly bind to a bisphosphorylated peptide in a cross-linking manner under neutral aqueous conditions when the distance between the two Zn(ll) centers can appropriately fit in that of the two phosphate groups of the phosphorylated peptide. The binding property was quantitatively determined by ITC (isothermal titration calorimetry), induced CD (circular dichroism), and NMR. On the basis of these findings, we demonstrated that these types of small molecules were able to effectively disrupt the phosphoprotein-protein interaction in a phosphorylated CTD peptide and the Pin1 WW domain, a phosphoprotein binding domain, at a micromolar level. The strategy based on a small molecular disruptor that directly interacts with phosphoprotein is unique and should be promising in developing a designer inhibitor for phosphoprotein-protein interaction.