A spectroscopy approach for the study of the interactions of bioactive vanadium species with bovine serum albumin

Ferrer, Evelina G.; Bosch, Alejandra; Yantorno, Osvaldo; Baran, Enrique J.

doi:10.1016/j.bmc.2008.01.060

Cited by 106 publications

(64 citation statements)

References 68 publications

(97 reference statements)

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“…It has the outstanding property of binding to a huge amount of drugs reversibly (Ferrer et al, 2008). The interaction between BSA and drugs has attracted great interest among researchers because of its structural homology with human serum albumin.…”

Section: Introductionmentioning

confidence: 99%

Study of nobiletin binding to bovine serum albumin by capillary electrophoresis–frontal analysis and circular dichroism

Deng

et al. 2010

Biomedical Chromatography

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A very recent epidemiological study provided strong support for nobiletin (NOB) as a potential candidate chemopreventive agent against cancer. From the pharmacology point of view, drug-protein interactions are determining factors in therapeutic, pharmacodynamic and toxicological drug properties. In this work, for the first time, detection of NOB at near-physiological conditions was accomplished by means of capillary electrophoresis-frontal analysis (CE-FA), and then the binding constants of NOB with bovine serum albumin (BSA) at the same conditions were determined. Complexation of NOB-BSA led to a decrease of the height for free NOB with increasing concentration of BSA. These results revealed the presence of a single class of binding site on BSA, and provided the binding constant of 10(3)/m, showing the strong affinity of NOB for BSA. Furthermore, circular dichroism spectra showed that, when the molar ratio of NOB to BSA was up to 2:1, NOB did not affect the overall protein conformation significantly and the protein thus retained a native-like structure. These results may provide important information for preclinical studies of nobiletin in pharmaceutical research.

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Section: Introductionmentioning

confidence: 99%

Study of nobiletin binding to bovine serum albumin by capillary electrophoresis–frontal analysis and circular dichroism

Deng

et al. 2010

Biomedical Chromatography

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“…3) 13 Other studies performed with ferritin described a stoichiometry of 16 vanadyl cations to one protein molecule, 26 this cation being recognized to bind to several proteins, at the same and higher orders of magnitude than the one described for actin. [27][28][29][30] Similarly as it was described above for decavanadate, the presence of ATP in the assay medium prevents the interaction between vanadyl and actin, hence no EPR signals are detected. 13 Recently reviewed decavanadate insights into biological systems have pointed out that this oligovanadate is either more or less efficient than the corresponding simple oxovanadates in targeting proteins, particularly at the nucleotide binding site.…”

Section: Introductionmentioning

confidence: 99%

Recent advances into vanadyl, vanadate and decavanadate interactions with actin

2012

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Although the number of papers about ''vanadium'' has doubled in the last decade, the studies about ''vanadium and actin'' are scarce. In the present review, the effects of vanadyl, vanadate and decavanadate on actin structure and function are compared. Decavanadate 51 V NMR signals, at À516 ppm, broadened and decreased in intensity upon actin titration, whereas no effects were observed for vanadate monomers, at À560 ppm. Decavanadate is the only species inducing actin cysteine oxidation and vanadyl formation, both processes being prevented by the natural ligand of the protein, ATP. Vanadyl titration with monomeric actin (G-actin), analysed by EPR spectroscopy, reveals a 1 : 1 binding stoichiometry and a K d of 7.5 mM À1 . Both decavanadate and vanadyl inhibited G-actin polymerization into actin filaments (F-actin), with a IC 50 of 68 and 300 mM, respectively, as analysed by light scattering assays, whereas no effects were detected for vanadate up to 2 mM. However, only vanadyl (up to 200 mM) induces 100% of G-actin intrinsic fluorescence quenching, whereas decavanadate shows an opposite effect, which suggests the presence of vanadyl high affinity actin binding sites. Decavanadate increases (2.6-fold) the actin hydrophobic surface, evaluated using the ANSA probe, whereas vanadyl decreases it (15%). Both vanadium species increased the e-ATP exchange rate (k = 6.5 Â 10 À3 s À1 and 4.47 Â 10 À3 s À1 for decavanadate and vanadyl, respectively). Finally, 1 H NMR spectra of G-actin treated with 0.1 mM decavanadate clearly indicate that major alterations occur in protein structure, which are much less visible in the presence of ATP, confirming the preventive effect of the nucleotide on the decavanadate interaction with the protein. Putting it all together, it is suggested that actin, which is involved in many cellular processes, might be a potential target not only for decavanadate but above all for vanadyl. By affecting actin structure and function, vanadium can regulate many cellular processes of great physiological significance.

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“…V(V) species, as suggested by Kiss et al (2012), bind to transferrin in form of VO 2 + without requiring bicarbonate (Harris and Carrano 1984;Heinemann et al 2002;Jakusch et al 2009;Saponja and Vogel 1996). VO 2+ and VO 3 À are shown to bind to serum albumin as well (Ahmed-Ouameur et al 2006;Ferrer et al 2008). Human serum albumin binds VO 2+ stronger than VO 3 À , with two binding sites, one strong and one weak, whereas VO 3 À binds by only one weak site (Purcell et al 2001).…”

Section: Coordination Reactions Of Vanadatementioning

confidence: 91%

Chemical, Biochemical, and Biological Behaviors of Vanadate and Its Oligomers

Wang

2013

Biomedical Inorganic Polymers

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Vanadate is widely used as an inhibitor of protein tyrosine phosphatases (PTPase) and is routinely applied in cell lysis buffers or immunoprecipitations of phosphotyrosyl proteins. Additionally, vanadate has been extensively studied for its antidiabetic and anticancer effects. In most studies, orthovanadate or metavanadate was used as the starting compound, whereas these "vanadate" solutions may contain more or less oligomerized species. Whether and how different species of vanadium compounds formed in the biological media exert specific biological effect is still a mystery. In the present commentary, we focus on the chemical, biochemical, and biological behaviors of vanadate. On the basis of species formation of vanadate in chemical and biological systems, we compared the biological effects and working mechanism of monovanadate with that of its oligomers, especially the decamer. We propose that different oligomers may exert a specific biological effect, which depends on their structures and the context of the cell types, by different modes of action.

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A spectroscopy approach for the study of the interactions of bioactive vanadium species with bovine serum albumin

Cited by 106 publications

References 68 publications

Study of nobiletin binding to bovine serum albumin by capillary electrophoresis–frontal analysis and circular dichroism

Study of nobiletin binding to bovine serum albumin by capillary electrophoresis–frontal analysis and circular dichroism

Recent advances into vanadyl, vanadate and decavanadate interactions with actin

Chemical, Biochemical, and Biological Behaviors of Vanadate and Its Oligomers

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