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

ABSTRACT: 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. Consequently, a promising approach of intervention against PD might be preventing α-synuclein build-up, misfolding and aggregation. A possible strategy involves the use of small molecules able to slow down the aggregation process or to alter oligomer conformation favouring the growth of non-pathogenic species. Here, we show that oleuropein aglycone (OleA), the main olive oil polyphenol, e

SUBMITTER: Palazzi L 

PROVIDER: S-EPMC5974307 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature