Tin oxide nanoparticles trigger the formation of amyloid β oligomers/protofibrils and underlying neurotoxicity as a marker of Alzheimer's diseases

Alzheimer's disease (AD) is known as one of the most common forms of dementia, and oligomerization of amyloid β (Aβ₄₂) peptides can result in the onset of AD. Tin oxide nanoparticles (SnO₂ NPs) showed several applications in biomedical fields can trigger unwanted interaction with proteins and inducing protein aggregation. Herein, we synthesized SnO₂ NPs via the hydrothermal method and characterized by UV-visible, XRD, FTIR, TEM, and DLS techniques. Afterward, the formation of Aβ₄₂ amyloid oligomers/protofibrils treated alone and with SnO₂ NPs was explored by ThT and Nile red fluorescence and CD spectroscopic methods along with TEM imaging. The neurotoxicity of different spices of Aβ₄₂ samples against PC-12 cells was then explored by MTT and caspase-3 activity assays. The characterization of SnO₂ NPs confirmed the successful synthesis of crystalline NPs (20-30 nm). Different biophysical and cellular analyses indicated that SnO₂ NPs accelerated Aβ₄₂ fibrillogenesis and promoted amyloid oligomers/protofibrils cytotoxicity. As compared to the Aβ₄₂ samples grown alone, the ThT and ANS fluorescence intensity along with ellipticity results indicated the promotory effect of SnO₂ NPs on the formation of oligomers/protofibrils. Also, the cellular results showed that the treated Aβ₄₂ samples with SnO₂ NPs further reduced cell viability through activation of caspase-3. In conclusion, SnO₂ NPs greatly accelerate the fibrillation of Aβ₄₂ peptides and lead to the formation of more toxic species. The present data may offer further warrants into nano-based systems for biomedical applications in the central nervous system.