Peer-Reviewed Journal Details
Mandatory Fields
Ahmed, MH;Keyes, TE;Byrne, JA
2013
February
Journal of Photochemistry and Photobiology A: Chemistry
The photocatalytic inactivation effect of Ag-TiO2 on beta-amyloid peptide (1-42)
Published
20 ()
Optional Fields
ATOMIC-FORCE MICROSCOPY ENHANCED RAMAN-SPECTROSCOPY HUMAN SERUM-ALBUMIN SILVER SURFACE TIO2 PROTEIN FILMS AG ADSORPTION DEGRADATION
254
1
11
Due to its low toxicity and excellent biocompatibility, titanium dioxide and its alloyed are widely used in biomedical applications. Furthermore, TiO2 can be excited by UV light to create charge carriers giving rise to photocatalytic redox reactions at its surface and photo-induced super-hydrophilicity. In this work, TiO2 films were modified with silver (Ag-TiO2) by the photocatalytic reduction of Ag+ from solution. The films and the adsorption of beta-amyloid (1-42), were studied using Raman spectroscopy, X-ray photoelectron spectroscopy (XPS), X-ray diffraction (XRD), and atomic force microscopy (AFM). These films were confirmed to contain mainly anatase crystallites and the photo-reduced Ag was predominantly Ag-0 (>0%). Ag loading of the TiO2 markedly enhanced the Raman signal (ca. 15-fold), but caused significant changes to the protein spectrum indicating non-specific binding of beta-amyloid side chain residues to the silver. The amide modes remained well-resolved and were used to estimate the conformational change induced in the protein by the silver. Raman analysis showed an increase in the intensity of the band at similar to 1665 cm(-1) assigned to the disordered conformation of the beta-amyloid, suggesting that the adsorption to the silver sites induces conformational changes. Contaminated surfaces were exposed to UVB irradiation, caused further conformational changes in the beta-amyloid, which mildly inhibited amyloid fibril formation, thought to be induced through a photocatalytic mechanism. (C) 2012 Elsevier B.V. All rights reserved.
LAUSANNE
1010-6030
10.1016/j.jphotochem.2012.12.019
Grant Details