Elucidating the Pathways for Protein Misfolding and Aggregation: Unity in Diversity.

Dr. Ashutosh Tiwari, Assistant Professor of Chemistry

Department of Chemistry,  Michigan Technological University     

 

November 7, 2014  ~  3:00pm  ~  Chemical Science Building, Room 101

Abstract:

Due to the aging of baby boomers in the USA, the proportion of the population in higher age groups has increased. This demographic shift coupled with a concomitant increase in longevity has brought new challenges and threats in the form of diseases and disorders that not only affect an individual but impact the whole society at large. Increased oxidative damage of proteins associated with aging causes them to misfold and aggregate and thus, disorders related to protein misfolding and aggregation are on the rise. Since many aggregated proteins share a common fibrillar structure at the molecular level, understanding the principles and contributing factors that regulate protein misfolding, surface hydrophobic exposure, aberrant interactions, or aggregation is key to understanding their relationship to cellular toxicity. I will discuss recent results from my laboratory wherein we studied several proteins for their surface-hydrophobic exposure and aggregation propensity at physiological pH and temperature. Identifying shared protein aggregation pathways for a large set of structurally diverse proteins will lead to a better understanding of the disease process and as a consequence provide common effective targets for therapy.