Electrochemical measurements confirm the preferential bonding of the antimetastatic complex [ImH][RuCl4(DMSO)(Im)] (NAMI-A) with proteins and the weak interaction with nucleobases

Mauro Ravera; Sara Baracco; Claudio Cassino; Donato Colangelo; Graziana Bagni; Gianni Sava; Domenico Osella

doi:10.1016/j.jinorgbio.2004.02.015

Electrochemical measurements confirm the preferential bonding of the antimetastatic complex [ImH][RuCl₄(DMSO)(Im)] (NAMI-A) with proteins and the weak interaction with nucleobases

Mauro Ravera
, Sara Baracco
, Claudio Cassino
, Donato Colangelo
, Graziana Bagni
, Gianni Sava
, Domenico Osella

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	984-990
Number of pages	7
Journal	Journal of Inorganic Biochemistry
Volume	98
Issue number	6
DOIs	https://doi.org/10.1016/j.jinorgbio.2004.02.015
Publication status	Published - Jun 2004

Keywords

Antimetastatic compounds
DNA-biosensors
Electrochemistry
Ruthenium

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10.1016/j.jinorgbio.2004.02.015

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Ravera, M., Baracco, S., Cassino, C., Colangelo, D., Bagni, G., Sava, G., & Osella, D. (2004). Electrochemical measurements confirm the preferential bonding of the antimetastatic complex [ImH][RuCl₄(DMSO)(Im)] (NAMI-A) with proteins and the weak interaction with nucleobases. Journal of Inorganic Biochemistry, 98(6), 984-990. https://doi.org/10.1016/j.jinorgbio.2004.02.015

@article{89f8d37e744c45d3a99b59caf70bdc86,

title = "Electrochemical measurements confirm the preferential bonding of the antimetastatic complex [ImH][RuCl4(DMSO)(Im)] (NAMI-A) with proteins and the weak interaction with nucleobases",

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.",

keywords = "Antimetastatic compounds, DNA-biosensors, Electrochemistry, Ruthenium",

author = "Mauro Ravera and Sara Baracco and Claudio Cassino and Donato Colangelo and Graziana Bagni and Gianni Sava and Domenico Osella",

year = "2004",

month = jun,

doi = "10.1016/j.jinorgbio.2004.02.015",

language = "English",

volume = "98",

pages = "984--990",

journal = "Journal of Inorganic Biochemistry",

issn = "0162-0134",

publisher = "Elsevier Inc.",

number = "6",

}

Ravera, M, Baracco, S, Cassino, C, Colangelo, D, Bagni, G, Sava, G & Osella, D 2004, 'Electrochemical measurements confirm the preferential bonding of the antimetastatic complex [ImH][RuCl₄(DMSO)(Im)] (NAMI-A) with proteins and the weak interaction with nucleobases', Journal of Inorganic Biochemistry, vol. 98, no. 6, pp. 984-990. https://doi.org/10.1016/j.jinorgbio.2004.02.015

Electrochemical measurements confirm the preferential bonding of the antimetastatic complex [ImH][RuCl₄(DMSO)(Im)] (NAMI-A) with proteins and the weak interaction with nucleobases. / Ravera, Mauro; Baracco, Sara; Cassino, Claudio et al.
In: Journal of Inorganic Biochemistry, Vol. 98, No. 6, 06.2004, p. 984-990.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Electrochemical measurements confirm the preferential bonding of the antimetastatic complex [ImH][RuCl4(DMSO)(Im)] (NAMI-A) with proteins and the weak interaction with nucleobases

AU - Ravera, Mauro

AU - Baracco, Sara

AU - Cassino, Claudio

AU - Colangelo, Donato

AU - Bagni, Graziana

AU - Sava, Gianni

AU - Osella, Domenico

PY - 2004/6

Y1 - 2004/6

N2 - 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.

AB - 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.

KW - Antimetastatic compounds

KW - DNA-biosensors

KW - Electrochemistry

KW - Ruthenium

UR - https://www.scopus.com/pages/publications/2442473959

U2 - 10.1016/j.jinorgbio.2004.02.015

DO - 10.1016/j.jinorgbio.2004.02.015

M3 - Article

SN - 0162-0134

VL - 98

SP - 984

EP - 990

JO - Journal of Inorganic Biochemistry

JF - Journal of Inorganic Biochemistry

IS - 6

ER -

Electrochemical measurements confirm the preferential bonding of the antimetastatic complex [ImH][RuCl₄(DMSO)(Im)] (NAMI-A) with proteins and the weak interaction with nucleobases

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Keywords

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