Dr. Bhaswati Sengupta’s Interview
Dr. Bhaswati Sengupta is currently working on Nucleosome dynamics and chromatin remodelling using smFRET as a postdoc in the Department of Chemistry at Pennsylvania State University, USA. She completed her PhD in the lab of Prof. Pratik Sen, Department of Chemistry, Indian Institute of Technology Kanpur, India. The last part of her PhD work, titled “Fluorescence correlation spectroscopy as a tool to investigate the directionality of proteolysis”, was published as first author in the International Journal of Biological Macromolecules (2020).
How would you explain your paper’s key results to the non-scientific community?
Proteins are long chains of amino acids joined by peptide bonds. In our body, proteolysis breaks down these proteins into smaller peptides – an essential part of digestion. In our research, we used human serum albumin (HSA) as a model protein and enzymes like papain, chymotrypsin, and trypsin to break it down.
Since HSA is a long chain, it can be digested from either end. We wanted to find out from which side the digestion starts. To do this, we used fluorescence correlation spectroscopy (FCS), a sensitive technique that tracks the change in size of fluorescently labelled fragments during digestion.
By labeling both ends of HSA with different dyes, we could monitor which side the digestion started from. We found that all three enzymes begin digesting HSA from domain I. This was evident as fragments tagged with dye near domain I reduced in size faster. We confirmed these results using reverse-phase high-performance liquid chromatography (RP-HPLC).
What are the possible consequences of these findings for your research area?
Existing techniques like mass spectrometry and HPLC can measure digested protein fragments, but they often require larger samples and don’t reveal the direction of digestion. Our approach using FCS is unique in that it determines directionality and requires only minimal amounts of protein—thanks to its picomolar to nanomolar sensitivity. This opens a new application for single-molecule techniques in proteolysis studies.
“I see you are now able to think of novel ideas and design the experiments; your training has been completed.”
What was the exciting moment (eureka moment) during your research?
There were three major “Eureka” moments:
- When I shared the idea with my advisor and he said, “Your training is complete.” That encouragement gave me a huge morale boost.
- When the data showed a difference between the two fluorophore-labelled sides of HSA. Without this, the study would not have been conclusive.
- When the RP-HPLC results aligned with the FCS measurements, validating everything we observed.
What do you hope to do next?
I’m not currently following up on this line of research. I had to leave for my postdoctoral work before we could expand it further. There were ideas to try this technique on other proteins, enzymes, environments, and drug treatments. I hope to revisit these someday if I get the opportunity.
Where do you seek scientific inspiration?
What excites me most about research is the unknown. From childhood, I was curious about unexplored ideas. That curiosity keeps me in science. I’ve also had great mentors who believed in me, and that support has been vital. The joy of discovering something new is unmatched, and I hope to continue exploring science for life.
How do you intend to help Indian science improve?
“Improving Indian science” is a massive goal. I’m still early in my career, currently pursuing postdoctoral research. But I dream of setting up my own lab in India. My focus would be to:
- Design cost-effective experiments using limited resources.
- Equip the lab with affordable yet efficient tools.
- Promote single-molecule research with minimal sample usage to reduce costs of expensive reagents and materials.
Reference
Sengupta B, Das N, Singh V, Thakur AK, Sen P.
Fluorescence correlation spectroscopy as a tool to investigate the directionality of proteolysis.
International Journal of Biological Macromolecules, 2020; 164: 2524–2534.
Read the paper
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