Our research interest lies in the area of ‘protein aggregation diseases’ . The long-term goal of our laboratory is to understand the relationship between protein misfolding and aggregation, and their role in health and disease. Although, protein misfolding and aggregation have been directly linked to cellular toxicity for several protein deposition diseases, the underlying mechanism(s) by which these aggregated proteins impair cellular function(s) and cause toxicity is not clear and is a subject of intense debate. The focus of our lab is to analyze the biochemical and biophysical properties including stability, post-translational modifications of these proteins in vitro and to identify their unique interacting partners in vivo.

In summary, we are interested in studying consequences of protein misfolding in vitro and how it relates to misfolding in vivo, and the role molecular crowding plays in the process. Understanding the principles and the contributing factors that may regulate protein misfolding, surface hydrophobic exposure, aberrant interactions or aggregation and its relationship to cellular toxicity should help us identify novel protein targets and formulate effective therapies.