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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
- Source :
- Journal of inorganic biochemistry. 98(6)
- Publication Year :
- 2003
-
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.
- Subjects :
- Stereochemistry
Serum albumin
Molecular Conformation
Biochemistry
Nucleobase
Inorganic Chemistry
Chemical models
chemistry.chemical_compound
Electrochemistry
Organometallic Compounds
Imidazole
NAMI-A
Protein binding
Nucleotide
Dimethyl Sulfoxide
Taq Polymerase
Antimetastatic
Antineoplastic Agents, Alkylating
Telomerase
Ribonucleoprotein
chemistry.chemical_classification
biology
Chemical model
Molecular Structure
Nucleotides
Biomolecule
chemistry
biology.protein
Ruthenium Compounds
DNA
Subjects
Details
- ISSN :
- 01620134
- Volume :
- 98
- Issue :
- 6
- Database :
- OpenAIRE
- Journal :
- Journal of inorganic biochemistry
- Accession number :
- edsair.doi.dedup.....b950bfce51b85794693e0ddde6ee1a49