Results from various cell and animal models already suggest that a reduction of amyloid aggregation is beneficial. Now, researchers from IEP SAS in Kosice, Slovakia, and ISMN-CNR in Bologna, Italy, have investigated the effect of electrostatically stabilized magnetic nanoparticles (NPs) of Fe3O4 on the amyloid aggregation of lysozyme in vitro, as a prototypical amyloidogenic protein.

The work, published in the journal Nanotechnology, indicates that nanoparticles are able to inhibit the formation of amyloid aggregates and decrease the amount of amyloid fibrils. AFM images show amyloid fibrils of lysozyme (figure a) and their destruction after incubation with an increasing concentration of NPs (figures b and c). A spectroscopic technique was used to obtain IC50 and DC50 values, which indicate that NPs are able to decrease the amount of lysozyme aggregation already at stoichiometric concentrations. These features make NPs of potential interest as therapeutic agents against amyloid-related diseases.

The experimental data also provide other very interesting evidence; in vitro interaction of NPs with lysozyme does not promote amyloid aggregation. It is an important observation due to the fact that interaction of proteins with nanoparticles possessing a strong ability to promote protein amyloid aggregation can induce the onset or accelerate the development of amyloid disease.

This study proposes the potential therapeutic use of NPs in the prevention and treatment of amyloid-related diseases as well as their non-risk exploitation in nanomedicine and nanodiagnostics.

These findings will be employed for future investigation of the effect of various types of NPs on amyloid aggregates as the nanoparticle size, structure, surface composition and charge markedly influence their affect on amyloid aggregation.