Thesis Defense: Sanjukta Ghosh, Master’s Student, Chemistry Department
University of Massachusetts Boston
Department of Chemistry
Investigation of Amyloidogenic Systems by the Application of Small Molecular Probes
Presented by Sanjukta Ghosh
for the MS in Chemistry
Advisor: Professor Marianna Torok
Wednesday, May 21, 2014 | 10 AM - 11 AM
Chemistry Conference Room | Science S01-0089
Amyloidoses is a group of human diseases characterized by harmful accumulation of misfolded protein aggregates, rich in β-sheet structures referred as amyloids. Alzheimer’s disease (AD), the most common neurodegenerative disease, associated with the misfolding of a small peptide called amyloid-beta (Aβ) is often considered to be the archetype of amyloidosis. Several small molecule inhibitors of Aβ self-assembly have been suggested that reduce the production of the amyloidogenic form of proteins or increase their clearance rate as an attempt to treat amyloidoses. In the present work we investigated the impact of small organic molecules on self-assembly of Aβ by biochemical, biophysical and imaging techniques. Chalcones and coumarins, diarylhydrazones, phenylhydrazine and carbonyl compounds were selected based on the analysis of literature information on inhibitors of amyloid formation. We further extended our study to investigate the impact of these small molecules on the fibril formation of hen egg white lysozyme (HEWL) to observe if the effect of these compounds displays any similar trends in two distinct amyloidogenic systems. Our results indicated that these small molecules have profound impact on the self-assembly of Aβ. We have identified new compounds that have resulted in significant decrease in the fibril formation of Aβ. Our preliminary investigations in HEWL suggest that the molecular probes showed similar inhibitory effect in the fibrillogenesis of lysozyme.
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