Investigadora: Ruth Pietri

Protein fibrils are large aggregates of misfolded proteins that are associated with several neurodegenerative diseases such as familial amyotrophic lateral sclerosis (ALS). Superoxide dismutase (SOD) is a protein that forms fibrils, which has been implicated with ALS. Hydrogen sulfide (H2S) can inhibit protein fibrils by reacting with disulfide bonds in proteins, which in turn stimulates structural changes that prevents fibrils formation. We have recently found that SOD reacts with H2S and induces similar structures changes. We therefore hypothesize that H2S interact with the disulfide bonds of SOD, causing structural changes that can prevent fibrils formation. To prove this, we will study the mechanism of SOD fibrillation in the presence of H2S. The results of this study will convey an overall picture of the role H2S in SOD fibrils formation. This interdisciplinary research integrates techniques of and theories from Physical Chemistry to study biological systems. Consequently, these findings will impact the biomedical research on H2S and protein fibrillation by addressing the fundamental question of how persulfidation regulates fibrils formation in proteins that are involved neurodegenerative diseases.