SciELO - Scientific Electronic Library Online

 
vol.57 número3Spectroscopic Characterization of an Oxovanadium(IV) Complex of Oxodiacetic Acid and 2,2'-Bipyridine: Bioactivity on Osteoblast-Like Cells in CultureElectrochemical Study of the Complex [Cu(pdto)(H2O)]2+ (pdto =1,8-bis(2-pyridyl)-3,6-dithiaoctane) in the Presence of the Superoxide. Toward an Electrochemical Method to Measure SOD Activity índice de autoresíndice de materiabúsqueda de artículos
Home Pagelista alfabética de revistas  

Servicios Personalizados

Revista

Articulo

Indicadores

Links relacionados

  • No hay artículos similaresSimilares en SciELO

Compartir


Journal of the Mexican Chemical Society

versión impresa ISSN 1870-249X

Resumen

COBBINA, Enoch et al. Binding of Oxovanadium(IV) Complexes to Blood Serum Albumins. J. Mex. Chem. Soc [online]. 2013, vol.57, n.3, pp.180-191. ISSN 1870-249X.

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.

Palabras llave : Oxovanadium(IV); Circular Dichroism; Electron Paramagnetic Resonance; maltol; human serum albumin; bovine serum albumin; porcine serum albumin.

        · resumen en Español     · texto en Inglés

 

Creative Commons License Todo el contenido de esta revista, excepto dónde está identificado, está bajo una Licencia Creative Commons