Oleuropein aglycone stabilizes the monomeric α-synuclein and favours the growth of non-toxic aggregates

In this study Palazzi and her research team studied whether oleuropein aglyconeexhibits anti-amyloidogenic power in vitro by interacting with, and stabilizing, αsynuclein monomers. α-synuclein plays a key role in the pathogenesis of Parkinson's disease (PD); its deposits are found as amyloid fibrils in Lewy bodies and Lewy neurites, the histopathological hallmarks of PD. Amyloid fibrillation is a progressive polymerization path starting from peptide/protein misfolding and proceeding through the transient growth of oligomeric intermediates widely considered as the most toxic species.


The researchers showed that oleuropein aglycone exhibits anti-amyloidogenic power in vitro by interacting with, and stabilizing, α-synuclein monomers thus hampering the growth of on-pathway oligomers and favouring the growth of stable and harmless aggregates with no tendency to evolve into other cytotoxic amyloids. They also found that OleA reduces the cytotoxicity of α-synuclein aggregates by hindering their binding to cell membrane components and preventing the resulting oxidative damage to cells.


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