Georg Krainer

Nov 20, 2024 | nature.com | Dhiman Ghosh |Matthias Schneider |Dzmitry Ashkinadze |Harindranath Kadavath |Peter Güntert |Georg Krainer | +4 more

AbstractThe complex kinetics of disease-related amyloid aggregation of proteins such as α-Synuclein (α-Syn) in Parkinson’s disease and Aβ42 in Alzheimer’s disease include primary nucleation, amyloid fibril elongation and secondary nucleation. The latter can be a key accelerator of the aggregation process. It has been demonstrated that the chaperone domain BRICHOS can interfere with the secondary nucleation process of Aβ42.

Aug 17, 2024 | nature.com | Catherine Xu |Georg Meisl |Ewa Andrzejewska |Georg Krainer |Irina Edu |Michele Vendruscolo | +1 more

AbstractOligomeric species arising during the aggregation of α-synuclein are implicated as a major source of toxicity in Parkinson’s disease, and thus a major potential drug target. However, both their mechanism of formation and role in aggregation are largely unresolved. Here we show that, at physiological pH and in the absence of lipid membranes, α-synuclein aggregates form by secondary nucleation, rather than simple primary nucleation, and that this process is enhanced by agitation.