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Adsorption and photocatalytic degradation of human serum albumin on TiO2 and Ag–TiO2 films

Biomedical Sciences Research Institute Computer Science Research Institute Environmental Sciences Research Institute Nanotechnology & Advanced Materials Research Institute

Byrne, JA and Hamilton, JWJ (2011) Adsorption and photocatalytic degradation of human serum albumin on TiO2 and Ag–TiO2 films. Journal of Photochemistry and Photobiology A: Chemistry, 222 (1). p. 123. [Journal article]

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URL: http://dx.doi.org/10.1016/j.jphotochem.2011.05.011

DOI: doi:10.1016/j.jphotochem.2011.05.011

Abstract

Titanium dioxide is a useful material in the biomedical field as it has excellent biocompatibility based on its non-toxicity and non-inflammatory properties. Furthermore, TiO2 can be excited by UV light to create charge carriers giving rise to photocatalytic redox reactions at the surface and photo-induced superhydrophilicity. These properties might be exploited for surface decontamination of medical devices and implants. With this in mind, titanium dioxide TiO2 films were prepared on stainless steel substrates using magnetron sputtering. Silver loaded (Ag–TiO2) films were prepared by the photocatalytic reduction of Ag+ from solution. The adsorption of human serum albumin (HSA) was studied. Surface analysis methods used included X-ray diffraction (XRD), X-ray photoelectron spectroscopy (XPS), Raman spectroscopy and atomic force microscopy (AFM). The TiO2 films were predominantly anatase crystal phase and thephotoreduced Ag was present at greater than 90% of the silver content as Ag0 on the surface. Ag loading of the TiO2 markedly enhanced the Raman signal (ca. 15-fold), but caused significant changes to the spectrum indicating non-specific binding of protein side chain residues to the Ag. The amide I and III modes remained well-resolved and were used to estimate the conformational change induced by the Ag. Raman analysis showed an increase in the intensity of the band at ∼1665 cm−1 assigned to the disordered conformation, suggesting that the adsorption to the Ag sites induces conformational changes in the protein. UVB irradiation of the protein contaminated surfaces caused further changes in the protein conformation, consistent with denaturation and enhanced binding and oxidation, thought to be induced through a photocatalytic mechanism.

Item Type:Journal article
Faculties and Schools:Faculty of Computing & Engineering
Faculty of Computing & Engineering > School of Engineering
Research Institutes and Groups:Engineering Research Institute
Engineering Research Institute > Nanotechnology & Integrated BioEngineering Centre (NIBEC)
ID Code:21780
Deposited By:Professor John Byrne
Deposited On:03 Apr 2012 10:34
Last Modified:03 Apr 2012 10:34

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