ZnO NPs immobilized by Alizarin as in vitro predictive and imaging biomarkers for protein amyloidosis

Abstract

Protein amyloidosis represents the main pathological hallmark of many incurable neurodegenerative disorders and protein misfolding diseases. Nanomaterials-based approaches give rise to diagnosis and/or prediction of these proteinopathies, with regards to the multifactorial nature of their pathogenesis. Herein, crystalline truncated hexagonal shaped naked ZnO nanoparticles (mean value 47.4 nm) have been solvothermally prepared and immobilized further with alizarin (Alzn) molecules (54%) to stand up to amyloidosis acting both as inhibitors and imaging agents, as well as antioxidants. Thioflavin-T (ThT) assay revealed that the resulted zinc oxide nanoparticles immobilized with alizarin (ZnO@Alzn NPs) inhibited in vitro insulin amyloids formation in a dose-dependent manner, while the kinetic mechanism of the phenomenon was recorded. In parallel, amyloid oligomers and plaques have been visualized by conventional optical microscopy upon protein co-incubation with ZnO@Alzn NPs, highlighting the imaging ability of the immobilized NPs. The antioxidant activity was monitored by 2,2-diphenyl-1-picrylhydrazyl (DPPH) assay, through which it was shown that alizarin incorporation onto the inorganic core leads to the reduction of IC50 values from 221 μg/mL to 167 μg/mL. The enhanced free radical scavenging effects of ZnO@Alzn compared to the naked-ZnO NPs, features their prospect to serve additional functions.