Abstract
Abstract More than 50 diseases are associated with a conversion of proteins or peptides from their soluble functional states to highly organized fibrillar aggregates called amyloid fibrils. Due to the specific physico-chemical properties, specifically designed iron oxide nanoparticles may be an effective strategy for inhibiting the amyloid fibrillization of proteins. The inhibitory effect of three types of iron oxide nanoparticles coated with differently modified dextran on lysozyme fibrils formation was studied by Thioflavin T assay and atomic force microscopy. The size and zeta potential of studied nanoparticles were determined by dynamic light scattering. It had been found that nanoparticles are able to inhibit formation of lysozyme amyloid aggregates in concentration-dependent manner. Our results suggest that size of nanoparticles influenced the extent of their inhibitory properties. Moreover, the most effective nanoparticles were not toxic after 48 h incubation with neuroblastoma SH-SY5Y cell line at concentration close to IC50 values.
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