Prion proteins are capable of converting from their soluble, biologically-functional forms into highly ordered, fibrous cross-� aggregates, known as amyloids. This conversion is associated with certain neurodegenerative conditions, such as Alzheimer's disease. Protein misfolding is strongly influenced by specific ionic effect, known as Hofmeister effects. Using a yeast prion protein, Sup35NM, we tested the influence of a host of sodium salts on aggregation kinetics; namely the salts' effect on elongation rate and lag time. Salts known to destabilize protein, chaotropes, exhibited long lag times and slower elongation rate; whereas salts known to stabilize proteins, kosmotropes, showed short lag times and fast elongation rates. Thermostability of the resulting aggregates was then studied using DLS and gel electrophoresis. Chaotropes were significantly more thermostable than kosmotropes. The amyloids formed in different salts were also transfected in yeast and tested for their �strength.� With stability, kinetic and strength data, a. aggregation mechanism is postulated.

Hofmeister effects on Sup35NM aggregation kinetics, amyloid thermostability and strength

243rd National Meeting (2012)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.