Binding of Oxovanadium(IV) complexes to blood serum albumins

Enoch Cobbina, Sameena Mehtab, Isabel Correia, Gisela Gonçalves, Isabel Tomaz, Isabel Cavaco, T. Jakusch, E. Enyedy, T. Kiss, João Costa Pessoa

Research output: Contribution to journalArticle

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Abstract

In this work the binding of VIVO2+ and VIVO-complexes to serum albumins {human serum albumin (HSA), bovine serum albumin (BSA) and porcine serum albumin (PSA)} are studied using circular dichroism (CD), electron paramagnetic resonance (EPR) and visible absorption spectroscopy. The results confirm previous findings that VIVO2+ occupies at least two types of binding sites on albumin: 'the strong vanadium binding site' (designated by VBS1) and 'the weak vanadium binding sites' (designated by VBS2). VBS1 binds 1 mol equivalent of VIVO2+. On the other hand VBS2 correspond to binding of several mol equivalents of VIVO, and studies done with PSA in the presence of excess ZnII ions indicate that VSB2 corresponds to two distinct types of sites. The hyperfine coupling constant Az for VIVO2+ binding at VBS2 on HSA and BSA are all very similar (~168 × 10-4 cm-1) but differ slightly on PSA (~166 × 10-4 cm-1) due to differences in the binding sets. When (VIVO)-HSA systems are titrated with maltol ternary species of (maltol)m(VIVO)mHSA and (maltol)2m(VIVO)mHSA stoichiometry form which are clearly distinguishable from the binary (VIVO)-HSA system by the type and intensity of the CD spectra recorded. Changes are also observable in the intensity of the X-band EPR spectra, but not much in the hyperfine coupling constants Az, which are all in the range 166-167 × 10-4 cm-1. The results further demonstrate that the presence of maltol may enhance the binding of VIVO to albumin.

Original languageEnglish
Pages (from-to)180-191
Number of pages12
JournalJournal of the Mexican Chemical Society
Volume57
Issue number3
Publication statusPublished - Jul 2013

Fingerprint

Serum Albumin
Blood
Vanadium
Binding Sites
Bovine Serum Albumin
Paramagnetic resonance
Albumins
Absorption spectroscopy
Stoichiometry
oxovanadium IV
Ions
maltol

Keywords

  • Bovine serum albumin
  • Circular dichroism
  • Electron paramagnetic resonance
  • Human serum albumin
  • Maltol
  • Oxovanadium(IV)
  • Porcine serum albumin

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Cobbina, E., Mehtab, S., Correia, I., Gonçalves, G., Tomaz, I., Cavaco, I., ... Costa Pessoa, J. (2013). Binding of Oxovanadium(IV) complexes to blood serum albumins. Journal of the Mexican Chemical Society, 57(3), 180-191.

Binding of Oxovanadium(IV) complexes to blood serum albumins. / Cobbina, Enoch; Mehtab, Sameena; Correia, Isabel; Gonçalves, Gisela; Tomaz, Isabel; Cavaco, Isabel; Jakusch, T.; Enyedy, E.; Kiss, T.; Costa Pessoa, João.

In: Journal of the Mexican Chemical Society, Vol. 57, No. 3, 07.2013, p. 180-191.

Research output: Contribution to journalArticle

Cobbina, E, Mehtab, S, Correia, I, Gonçalves, G, Tomaz, I, Cavaco, I, Jakusch, T, Enyedy, E, Kiss, T & Costa Pessoa, J 2013, 'Binding of Oxovanadium(IV) complexes to blood serum albumins', Journal of the Mexican Chemical Society, vol. 57, no. 3, pp. 180-191.
Cobbina E, Mehtab S, Correia I, Gonçalves G, Tomaz I, Cavaco I et al. Binding of Oxovanadium(IV) complexes to blood serum albumins. Journal of the Mexican Chemical Society. 2013 Jul;57(3):180-191.
Cobbina, Enoch ; Mehtab, Sameena ; Correia, Isabel ; Gonçalves, Gisela ; Tomaz, Isabel ; Cavaco, Isabel ; Jakusch, T. ; Enyedy, E. ; Kiss, T. ; Costa Pessoa, João. / Binding of Oxovanadium(IV) complexes to blood serum albumins. In: Journal of the Mexican Chemical Society. 2013 ; Vol. 57, No. 3. pp. 180-191.
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abstract = "In this work the binding of VIVO2+ and VIVO-complexes to serum albumins {human serum albumin (HSA), bovine serum albumin (BSA) and porcine serum albumin (PSA)} are studied using circular dichroism (CD), electron paramagnetic resonance (EPR) and visible absorption spectroscopy. The results confirm previous findings that VIVO2+ occupies at least two types of binding sites on albumin: 'the strong vanadium binding site' (designated by VBS1) and 'the weak vanadium binding sites' (designated by VBS2). VBS1 binds 1 mol equivalent of VIVO2+. On the other hand VBS2 correspond to binding of several mol equivalents of VIVO, and studies done with PSA in the presence of excess ZnII ions indicate that VSB2 corresponds to two distinct types of sites. The hyperfine coupling constant Az for VIVO2+ binding at VBS2 on HSA and BSA are all very similar (~168 × 10-4 cm-1) but differ slightly on PSA (~166 × 10-4 cm-1) due to differences in the binding sets. When (VIVO)-HSA systems are titrated with maltol ternary species of (maltol)m(VIVO)mHSA and (maltol)2m(VIVO)mHSA stoichiometry form which are clearly distinguishable from the binary (VIVO)-HSA system by the type and intensity of the CD spectra recorded. Changes are also observable in the intensity of the X-band EPR spectra, but not much in the hyperfine coupling constants Az, which are all in the range 166-167 × 10-4 cm-1. The results further demonstrate that the presence of maltol may enhance the binding of VIVO to albumin.",
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AB - In this work the binding of VIVO2+ and VIVO-complexes to serum albumins {human serum albumin (HSA), bovine serum albumin (BSA) and porcine serum albumin (PSA)} are studied using circular dichroism (CD), electron paramagnetic resonance (EPR) and visible absorption spectroscopy. The results confirm previous findings that VIVO2+ occupies at least two types of binding sites on albumin: 'the strong vanadium binding site' (designated by VBS1) and 'the weak vanadium binding sites' (designated by VBS2). VBS1 binds 1 mol equivalent of VIVO2+. On the other hand VBS2 correspond to binding of several mol equivalents of VIVO, and studies done with PSA in the presence of excess ZnII ions indicate that VSB2 corresponds to two distinct types of sites. The hyperfine coupling constant Az for VIVO2+ binding at VBS2 on HSA and BSA are all very similar (~168 × 10-4 cm-1) but differ slightly on PSA (~166 × 10-4 cm-1) due to differences in the binding sets. When (VIVO)-HSA systems are titrated with maltol ternary species of (maltol)m(VIVO)mHSA and (maltol)2m(VIVO)mHSA stoichiometry form which are clearly distinguishable from the binary (VIVO)-HSA system by the type and intensity of the CD spectra recorded. Changes are also observable in the intensity of the X-band EPR spectra, but not much in the hyperfine coupling constants Az, which are all in the range 166-167 × 10-4 cm-1. The results further demonstrate that the presence of maltol may enhance the binding of VIVO to albumin.

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