Dr. Durba Roy is an Assistant Professor at the Department of Chemistry, Birla Institute of Technology and Science-Pilani, Hyderabad Campus (2013-). Before joining BITS-Pilani, Hyderabad, she completed four years of postdoctoral research in USA. Briefly, she completed her PhD under the supervision of Professor Kankan Bhattacharyya at Indian Association for the Cultivation of Science (IACS), Kolkata in 2008, on ultrafast chemical dynamics involving Laser induced fluorescence spectroscopy. After completing her doctoral work, she joined Pennsylvania State University, USA, as a postdoctoral researcher to work under the supervision of Professor Mark Maroncelli, Department of Chemistry (2009-2011), where she learned how to create realistic simulation models of complex liquids and organized assemblies. She worked for a year (2011-2012) with Professor Tamar Schlick at New York University to learn Chromatin Folding simulations using Monte Carlo technique. Currently, one of her interests is in exploring the structure, function and dynamics of cystin rich venom peptides in several biocompatible and toxic ionic liquids and comparing the results with those from other simulations and experiments. The results would predict and help design tailor made biocompatible and non-toxic ionic liquids for maximum efficiency in the folding of the disulfide containing peptide toxins.
Abstract OpenTox Asia 2019
Dynamical simulations of Peptide Toxins reveal the link among peptide sequence, structure and disulfide bond isoforms:
Conopeptides, the toxins found in marine cone snail venoms target ion channels and neuroreceptors and have huge therapeutic potential to be developed as non-addictive pain relievers. When synthesized from linear precursors, these peptides yield several disulfide bond isoforms whose structural elucidation and separation are challenging. Recent experiments indicate that oxidative folding of such peptides in certain ionic liquids produce high yield of correctly folded native isoform. Using molecular dynamics simulations, we aim to understand the reason behind such recognition. Apart from shedding light on the general aspects of ionic solvation, our simulations reveal strong control of peptide sequence along with solvent and temperature in biasing the disulfide scrambling equilibrium towards a given isoform.