A prion-derived peptide can reduce Aβ۴۲ oligomer cytotoxicity on SH-SY۵Y neuroblastoma cells without changing the structure or oligomerization state of oligomer

Background and Aim : Alzheimer's disease is an aging-related and devastating neurodegenerative disease that is caused by cerebral accumulation of amyloid beta (Aβ) peptide. Cellular prion protein is a toxic receptor with high binding affinity for Aβ۴۲ oligomers. The level of viability of neuroblastoma cells after treatment with Aβ۴۲ oligomers (ADDLs) in presence and absence of a prion- derived peptide was assessed. Aggregation state of ADDLs in present of peptide was also investigated. Methods : The viability of SH-SY۵Y neuroblastoma cells after treatment with Aβ۴۲ oligomers (ADDLs) in present and absence of a short peptide (PrP۱۰۷-۱۲۰) was analyzed using the MTT assay. To determine the effect of the peptide on ADDLs aggregation state, the ADDLs structure in presence of PrP۱۰۷-۱۲۰ prion-derived peptide was investigated using ANS fluorescence, dot blot assay, Thioflavin T fluorescence and circular dichroism spectroscopy. Results : We found that addition of the synthetic peptide PrP۱۰۷-۱۲۰ to Aβ۴۲ oligomer significantly increased cell viability compared with the cells treatment with ADDLs alone. Moreover, other results indicated that prion-derived peptide was not able to change the Aβ۴۲ ADDLs structure. Conclusion : The present study suggests that PrP۱۰۷-۱۲۰ can significantly protect neuroblastoma cells against the toxicity induced by Aβ۴۲ oligomers, although it cannot change the oligomerization state of ADDLs.

کلیدواژه ها:

Alzheimer ، Aβ۴۲ oligomer ، prion peptide ، ADDLs