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"The response of proteins towards different environmental conditions, namely binding and non-binding entities, is not understood clearly in order to correlate with in vivo stability. We are addressing this problem in a variety of ways, such as environmental effects like ligand/dye/drug binding, effect of co-solvents (Ionic Liquids), the effect of glycosaminoglycan (GAG; one of the major components of the extracellular matrix), and different glucose molecules on protein stability and dynamics.  (Details are in “Research Page)"

"We are also interested in digging out the folding pathways (specifically, the physical and thermodynamic parameters) affected by the above-said binding and non-binding molecules directly or indirectly on the protein of interest. We are using the “bottom-up” approach, where we are mimicking the cellular components in in Vitro."

"Our research focuses on transforming protein aggregation from a pathological process into a functional biomaterial strategy. We investigate controlled aggregation pathways of proteins such as lysozyme, BMP-2, neurodegenerative and other globular proteins to develop bioactive and mechanically stable biomaterials. By studying aggregation kinetics, intermediate states, and structural transitions, we aim to understand the relationship between protein assembly and material properties. These insights are further utilized to design hydrogels, scaffolds, injectable systems, and drug-delivery platforms for applications in tissue engineering and regenerative medicine."

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