The inhibition of fibril formation of lysozyme by sucrose and trehalose.

The two disaccharides, trehalose and sucrose, have been compared in many studies due to their structural similarity. Both possess the ability to stabilise and reduce aggregation of proteins. Trehalose has also been shown to inhibit the formation of highly structured protein aggregates called amyloid fibrils.

Monovalent cations have different effects on the assembly kinetics and morphology of α-synuclein amyloid fibrils.

Formation of α-synuclein amyloid fibrils is a pathological hallmark of Parkinson's disease and a phenomenon that is strongly modulated by environmental factors. Here, we compared effects of different monovalent cations (Li, Na, K) on the formation and properties of α-synuclein amyloid fibrils. Na > Li were found to have concentration-dependent catalytic effects on primary nucleation whereas K ions acted inhibitory.