Electrochemical measurements confirm the preferential bonding of the antimetastatic complex [ImH][RuCl(4)(DMSO)(Im)] (NAMI-A) with proteins and the weak interaction with nucleobases

J Inorg Biochem. 2004 Jun;98(6):984-90. doi: 10.1016/j.jinorgbio.2004.02.015.

Abstract

An electrochemical and biological study of interaction between the prototypical antimetastatic drug imidazolium trans-tetrachlorodimethylsulfoxideimidazoleruthenate (III) complex, [ImH][RuCl(4)(DMSO)(Im)] (DMSO = dimethylsulfoxide, Im = imidazole), nicknamed NAMI-A, and several biomolecules, namely DNA, bovine (BSA) and human (HSA) serum albumin, is reported. Electrochemistry offers great advantages over the existing devices based on optical techniques, since it provides rapid, simple, and low-cost information whether the interaction occurs or not. Moreover, we describe some biochemical assays to test the interaction of NAMI-A with ribonucleoprotein telomerase and protein Taq polymerase. All the data confirm the preferential interaction of NAMI-A with proteins with respect to nucleotides, especially when compared with the behaviour of the well-known alkylating drug cisplatin in the presence of the same targets.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antineoplastic Agents, Alkylating / chemistry*
  • Dimethyl Sulfoxide / analogs & derivatives*
  • Dimethyl Sulfoxide / chemistry*
  • Electrochemistry
  • Molecular Conformation
  • Molecular Structure
  • Nucleotides / chemistry*
  • Organometallic Compounds / chemistry*
  • Ruthenium Compounds
  • Taq Polymerase / chemistry*
  • Telomerase / chemistry*

Substances

  • Antineoplastic Agents, Alkylating
  • Nucleotides
  • Organometallic Compounds
  • Ruthenium Compounds
  • imidazolium-bis(imidazole)dimethylsulfoxideimidazotetrachlororuthenate(III)
  • Taq Polymerase
  • Telomerase
  • Dimethyl Sulfoxide