Binding of vanadate to human albumin in infusion solutions, to proteins in human fresh frozen plasma, and to transferrin

Heinemann, G.; Fichtl, B.; Mentler, Matthias; Vogt, Wolfgang

doi:10.1016/s0162-0134(02)00399-9

Cited by 32 publications

(24 citation statements)

References 19 publications

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“…41 In a recent comparative study of the binding of vanadate to HSA, human fresh frozen plasma and human transferrin, it was demonstrated that the binding capacity of HSA is about one thousandth of those of the other two systems. 43 …”

Section: Transferrin and Serum Albumin Complexesmentioning

confidence: 99%

Model studies related to vanadium biochemistry: recent advances and perspectives

Baran¹

2003

J. Braz. Chem. Soc.

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Nos ultimos anos, vêm se acumulando as evidências sobre a necessidade de vanádio dos organismos mais evoluídos. Estudos de compostos modelos constituem-se numa importante ferramenta para o entendimento dos diferentes aspectos da bioquímica deste bioelemento. Neste artigo, apresentamos os resultados dos nossos estudos, assim como os de outros grupos de pesquisa, sobre compostos modelos relacionados a vários aspectos do metabolismo e detoxificação do vanádio e a haloperoxidasas dependentes do vanádio. São também apresentadas informações sobre as interações do cátion oxovanádio(IV), relevante do ponto de vista biológico, com bioligantes importantes, tais como nucleotideos, carboidratos, fosfatos e outros sistemas correlatos.Increasing evidence on the need of the higher forms of life for vanadium has accumulated during recent years. Model studies have become a very important tool to attain a better understanding of different aspects of the biochemistry of this bioelement. In this account we present the results of our own studies, as well as those of other research groups, on models related to different aspects of its metabolism and detoxification and to vanadium dependent haloperoxidases. Additional information about the interaction of the biologically relevant oxovanadium(IV) cation with important bioligands, such as nucleotides, carbohydrates, phosphates and related systems are also presented.

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Section: Transferrin and Serum Albumin Complexesmentioning

confidence: 99%

Model studies related to vanadium biochemistry: recent advances and perspectives

Baran¹

2003

J. Braz. Chem. Soc.

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“…Like Fe 3+ , two VO 2+ ions bind to the two iron-binding sites by the aid of HCO 3 À to stabilize the binding (Cannon and Chasteen 1975). 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).…”

Section: Coordination Reactions Of Vanadatementioning

confidence: 97%

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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“…The cancertargeting property of VO(acac) 2 due to its intercellular interaction with glycolytic enzymes is reinforced by formation of macromolecular complexes with serum albumin [47]. The binding interactions of vanadyl complexes with serum proteins are not well understood, and studies have been carried out to investigate binding interactions of serum proteins with vanadate(VO 3 − ) and vanadyl cations [48,49]. EPR and ENDOR spectral results demonstrated that VO(acac) 2 binds albumin with 1:1 stoichiometry [50].…”

Section: Introductionmentioning

confidence: 99%

A Spectroscopy Approach for the Study of the Interaction of Oxovanadium(IV)-Salen Complexes with Proteins

2015

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Oxovanadium(IV)-salen complexes bind with bovine serum albumin (BSA) and ovalbumin (OVA) strongly with binding constant in the range 10(4)-10(7) M(-1) at physiological pH (7.4) confirmed using UV-visible absorption, fluorescence spectral and circular dichroism (CD) study. CD results show that the binding of oxovanadium(IV) complexes induces the conformational change with the loss of α-helicity in the proteins. Docking studies indicate that mode of binding of oxovanadium(IV)-salen complexes with proteins is hydrophobic in nature.

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Binding of vanadate to human albumin in infusion solutions, to proteins in human fresh frozen plasma, and to transferrin

Cited by 32 publications

References 19 publications

Model studies related to vanadium biochemistry: recent advances and perspectives

Model studies related to vanadium biochemistry: recent advances and perspectives

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

A Spectroscopy Approach for the Study of the Interaction of Oxovanadium(IV)-Salen Complexes with Proteins

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