Metal-bioorganic compounds of vanadium pentoxide and bovine serum albumin (BSA) (Fraction V) were obtained by using sol-gel method. Series of the samples (BSA)xV2O5?nH2O, where x=0, 0.01 and 0.001, were originally produced by the synthesis of vanadium pentoxide xerogels and subsequent blending with water-dissolved BSA in appropriate molar ratios. It was evident that the gelation process does not occur for x>0.01. For the X-ray photoelectron spectroscopy (XPS) studies, the thin layers of these materials were prepared by drying the gel onto the glass and mica substrates. The surface morphology of the samples was characterized by scanning electron microscopy (SEM) and atomic force microscopy (AFM) techniques. It follows from the analysis of experimental XPS spectra of (BSA)xV2O5?nH2O that the nitrogen ions in pure albumin and in (BSA)0.01V2O5?nH2O are present in imine, amine and protonated amine groups. The additional protonated amine arises when the concentration of albumin in (BSA)xV2O5?nH2O is low (x=0.001). Increasing the amount of albumin results in decrease of the number of oxygen ions bonded to vanadium. At the same time (with increase of albumin), the component of oxygen bounded to carbon and nitrogen is increasing. In the samples with greater amount of albumin, the reduction of vanadium ions occurs. This means that the trivalent and tetravalent vanadium ions are present together with pentavalent ones.

CHEMICAL COMPOSITION STUDY OF VANADIUM PENTOXIDE XEROGELS DOPED BY BOVINE ALBUMIN

S KACIULIS;A MEZZI;M BRUCALE
2016

Abstract

Metal-bioorganic compounds of vanadium pentoxide and bovine serum albumin (BSA) (Fraction V) were obtained by using sol-gel method. Series of the samples (BSA)xV2O5?nH2O, where x=0, 0.01 and 0.001, were originally produced by the synthesis of vanadium pentoxide xerogels and subsequent blending with water-dissolved BSA in appropriate molar ratios. It was evident that the gelation process does not occur for x>0.01. For the X-ray photoelectron spectroscopy (XPS) studies, the thin layers of these materials were prepared by drying the gel onto the glass and mica substrates. The surface morphology of the samples was characterized by scanning electron microscopy (SEM) and atomic force microscopy (AFM) techniques. It follows from the analysis of experimental XPS spectra of (BSA)xV2O5?nH2O that the nitrogen ions in pure albumin and in (BSA)0.01V2O5?nH2O are present in imine, amine and protonated amine groups. The additional protonated amine arises when the concentration of albumin in (BSA)xV2O5?nH2O is low (x=0.001). Increasing the amount of albumin results in decrease of the number of oxygen ions bonded to vanadium. At the same time (with increase of albumin), the component of oxygen bounded to carbon and nitrogen is increasing. In the samples with greater amount of albumin, the reduction of vanadium ions occurs. This means that the trivalent and tetravalent vanadium ions are present together with pentavalent ones.
2016
Istituto per lo Studio dei Materiali Nanostrutturati - ISMN
Chemical synthesis; oxides; atomic force microscopy; electron microscopy; X-ray photo-emission spectroscopy
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/320987
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