Olive polyphenols act on protein misfolding pathways to limit amyloid aggregation in Alzheimer’s and Parkinson’s diseases, revealing nutritional approaches to neuroprotection.
Protein misfolding and amyloid aggregation, linked to neurodegenerative diseases, can result from liquid–liquid phase separation (LLPS) and a subsequent liquid-to-solid transition. This represents LLPS as a generic mechanism in amyloid nucleation.
Two distinct routes may lead to amyloid deposition in Parkinson's disease, nucleation mediated aggregation and condensate mediated aggregation, which are relevant to the pathogenesis and progression of the disease.
This review describes the effects of metal ions on the aggregation and toxicity profiles of Aβ.
Given the significance of protein aggregation in proteinopathies and the development of therapeutic protein pharmaceuticals, revamped interest in assessing and modelling the aggregation kinetics has been observed.