trans-(dimethylsulfoxide-S)(imidazole)tetrachlororuthenate(II) | 335375-85-4

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 唑类
• 英文名称: trans-(dimethylsulfoxide-S)(imidazole)tetrachlororuthenate(II)
• 英文别名: trans-imidazole(dimethylsulfoxide)tetrachlororuthenate(II)；trans-tetrachloro(dimethylsulfoxide)imidazoleruthenate(II)；[trans-ruthenium(II)Cl4(dimethylsulfoxide)(imidazole)]；trans-[Ru(II)Cl4(dimethyl sulfoxide)(imidazole)](2-)；trans-[Ru(II)Cl4(DMSO)(Im)](2-)；[trans-Ru(II)Cl4(DMSO)(Im)]；1H-imidazole;methylsulfinylmethane;ruthenium(2+);tetrachloride
• CAS: 335375-85-4
• 化学式: C₅H₁₀Cl₄N₂ORuS
• 分子量: 389.095
• InChiKey: YOHXXPYNSPICNN-UHFFFAOYSA-J

计算性质

• 辛醇/水分配系数(LogP)：
  -11.58
• 重原子数：
  14
• 可旋转键数：
  0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.4
• 拓扑面积：
  65
• 氢给体数：
  1
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  trans-(dimethylsulfoxide-S)(imidazole)tetrachlororuthenate(II) 、 水 以 水 为溶剂， 生成 [Ru(II)(H2O)Cl4(dimethyl sulfoxide)](2-)
  参考文献：
  名称：

  Appraisal of the redox behaviour of the antimetastatic ruthenium(iii) complex [ImH][RuCl4(DMSO)(Im)], NAMI-A

  摘要：

  咪唑铵转型四氯（亚砜）咪唑钌（III）复合物[ImH][Ru(III)Cl4(DMSO)(Im)]，NAMI-A，表现出一种有趣的抗转移活性。由于钌（III）复合物在配位上比相应的钌（II）衍生物更为惰性，提出了一种“还原激活”机制来解释NAMI-A的生物活性，因此其行为类似于前药。我们在此报告了对NAMI-A在水溶液中的电化学研究，强调了伴随简单的Ru(III)/Ru(II)电子转移的结构和化学后果（例如，在循环伏安法的短时间尺度内，酸性溶液中发生轴向咪唑/水交换，随后在宏电解的较长时间尺度内发生赤道氯/水交换）。

  DOI：

  10.1039/b400952e
• 作为产物：
  描述：

  NAMI-A 在 L-半胱氨酸 作用下， 以 水 为溶剂， 生成 trans-(dimethylsulfoxide-S)(imidazole)tetrachlororuthenate(II)
  参考文献：
  名称：

  Influence of redox activation of NAMI-A on affinity to serum proteins: transferrin and albumin

  摘要：

  Imidazolium trans-tetrachloridodimethylsulfoxideimidazoleruthenate(III), NAMI-A, is a ruthenium drug exhibiting unique properties under clinical studies such as ability to inhibit the process of metastases without exerting tumor toxicity. Its place of action is concentrated at the extracellular level, therefore, the transformation and fate of this drug upon injection is of great importance. This study focuses on evaluation of the reducing potency of blood stream on interaction with two serum proteins: albumin and transferrin. It was investigated by applying various simplified serum models preserving physiological concentration of proteins and the amount of Ru complex as found in patients. It was shown that ruthenation of albumin is slightly increased while transferrin decreased upon addition of reductant in blood stream (ascorbate, glutathione, and cysteine) at physiological concentration. Interestingly, in serum models comprising low-molecular-mass components the amount of the reductant in the solution had a pronounced effect on the Ru content, in particular in transferrin. Supplementation of serum models with glutathione at concentration enough for complete reduction of NAMI-A selectively enhanced the binding of Ru complex to transferrin while ruthenation of albumin was almost unchanged. Spectrofluorimetric studies revealed that reduction has a marginal effect on binding affinity, therefore, both Ru(III) and (II) derivatives equally can compete for binding to transferrin.

  DOI：

  10.1080/00958972.2015.1067692

文献信息

• Appraisal of the redox behaviour of the antimetastatic ruthenium(iii) complex [ImH][RuCl4(DMSO)(Im)], NAMI-A
  作者：Mauro Ravera、Sara Baracco、Claudio Cassino、Piero Zanello、Domenico Osella

  DOI：10.1039/b400952e

  日期：——

  The imidazolium trans-tetrachloro(dimethylsulfoxide)imidazoleruthenate(III) complex [ImH][Ru(III)Cl4(DMSO)(Im)], NAMI-A, has shown an interesting antimetastatic activity. Since Ru(III) complexes are coordinatively more inert than the corresponding Ru(II) derivatives, an “activation by reduction” mechanism has been proposed to explain the biological activity of NAMI-A, thus acting as a pro-drug. We report here an electrochemical study on NAMI-A in aqueous solutions which emphasizes the structural and chemical consequences accompanying the easy Ru(III)/Ru(II) electron transfer (e.g., axial imidazole/water exchange in acidic solution in the short timescale of cyclic voltammetry followed by equatorial chloride/water exchange in the longer timescale of macroelectrolysis).

  咪唑铵转型四氯（亚砜）咪唑钌（III）复合物[ImH][Ru(III)Cl4(DMSO)(Im)]，NAMI-A，表现出一种有趣的抗转移活性。由于钌（III）复合物在配位上比相应的钌（II）衍生物更为惰性，提出了一种“还原激活”机制来解释NAMI-A的生物活性，因此其行为类似于前药。我们在此报告了对NAMI-A在水溶液中的电化学研究，强调了伴随简单的Ru(III)/Ru(II)电子转移的结构和化学后果（例如，在循环伏安法的短时间尺度内，酸性溶液中发生轴向咪唑/水交换，随后在宏电解的较长时间尺度内发生赤道氯/水交换）。
• Influence of redox activation of NAMI-A on affinity to serum proteins: transferrin and albumin
  作者：K. Śpiewak、G. Stochel、M. Brindell

  DOI：10.1080/00958972.2015.1067692

  日期：2015.9.17

  Imidazolium trans-tetrachloridodimethylsulfoxideimidazoleruthenate(III), NAMI-A, is a ruthenium drug exhibiting unique properties under clinical studies such as ability to inhibit the process of metastases without exerting tumor toxicity. Its place of action is concentrated at the extracellular level, therefore, the transformation and fate of this drug upon injection is of great importance. This study focuses on evaluation of the reducing potency of blood stream on interaction with two serum proteins: albumin and transferrin. It was investigated by applying various simplified serum models preserving physiological concentration of proteins and the amount of Ru complex as found in patients. It was shown that ruthenation of albumin is slightly increased while transferrin decreased upon addition of reductant in blood stream (ascorbate, glutathione, and cysteine) at physiological concentration. Interestingly, in serum models comprising low-molecular-mass components the amount of the reductant in the solution had a pronounced effect on the Ru content, in particular in transferrin. Supplementation of serum models with glutathione at concentration enough for complete reduction of NAMI-A selectively enhanced the binding of Ru complex to transferrin while ruthenation of albumin was almost unchanged. Spectrofluorimetric studies revealed that reduction has a marginal effect on binding affinity, therefore, both Ru(III) and (II) derivatives equally can compete for binding to transferrin.