Inhibition of amyloid beta fibrillation and formation of soluble amyloid oligomers by molecular chaperone

Amyloid beta (Aβ) is known as a factor that causes Alzheimer's disease. It is important to inhibit formation of Aβ aggregation since Aβ aggregates are neurotoxic. In this study, we have studied the effect of molecular chaperone prefoldin (PFD) on the aggregation of the Aβ peptide (1-42). It was indicated that the soluble oligomeric Aβ particles were produced when Aβ was incubated with PFD, while fibrillar aggregates were produced when incubated without PFD. And, we found that the Aβ soluble oligomer with PFD exhibited higher toxicity than Aβ aggregates without PFD. Our data suggest that PFD recognizes these toxic soluble oligomers and prevent further fibrillation.