Department of
Biology

Sarita obtained her PhD from the Indian Institute of Technology, Delhi (IITD), India on investigating the folding pathways of multidomain proteins. For her postdoctoral training, she moved to the Institute of Biological Chemistry, Academia Sinica, Taiwan where she worked on knotted protein folding pathways and investigated the impact of post-translational modifications on the structure-function relationship of deubiquitinase enzymes. For her second postdoctoral stint, she moved to the Department of Bioscience, University of Milan, Italy where she was exposed to research on systemic amyloid diseases specifically AL amyloidosis. She joined IISER Pune as a DST Inspire faculty fellow in 2024.

Research

Protein misfolding and aggregation are responsible for more than 40 known diseases including neurodegenerative and systemic amyloid diseases contributed by genetic, environmental, and stress factors. It is a complex phenomenon where natively folded proteins turn to misfolded/unfolded conformations eventually shifting the equilibrium towards aggregation and amyloid deposition. Some well-studied proteins to understand aggregation pathways are from neurodegenerative diseases including α-synuclein, tau, prions, Aβ, etc. 

Systemic amyloid diseases offer more complex scenarios, in which amyloid fibrils of proteins deposit in multiple organs. Out of many systemic diseases, light chain (AL) amyloidosis is the most common type of systemic amyloid disease where fibrils of antibody light chains deposit in multiple organs including the heart, kidneys, skin, peripheral nerves, etc. The life expectancy of patients is less than six months in case of heart deposits. However, the pathways of their aggregation and factors governing their transition from native to misfolded conformations are not known. To understand the unfolding, misfolding, and aggregation behavior of amyloidogenic light chains associated with AL amyloidosis, Dr. Sarita’s group employs biophysical, biochemical, and structural biology methods on patient-derived amyloidogenic light chains.