Funded research projects completed / continuing:
Our Lab's research interest include Chaperone mediated folding studies of large and small homologous and heterologous substrates in Escherichia coli. We are also involved in developing suitable methods for the production of correctly folded recombinant proteins in cells using the assistance of molecular chaperones GroEL and GroES, utilizing protein Engineering approaches for the elucidation of function of different parts of the protein molecules to understand the role and to develop functionally efficient counterparts. Our lab is involved in variety of projects supported by different funding bodies of governemnt of India.
Developing next generation platform for improving recombinant Human Serum Albumin (rHSA) protein production in Escherichia coli: A combinatorial approach involving genome engineering, chaperone assisted protein folding and advanced downstream processing
Developing next-generation platform for high value recombinant protein production: Efforts for high yield preparation of recombinant human serum albumin in E. coli
Preparation and physical-chemical characterization of self-monitoring and self-assembling protein particles for biomedical application.
Development of a therapeutic cocktail for Gram-negative biofilm infections using engineered enzymatic quorum quenchers in combination with lytic phages.
Investigating the molecular mechanism of inhibition of dialysis related amyloidosis involving amyloid fibrils formation by beta-2 microglobulin using molecules of herbal origin such as curcumin, EGCG, and resveratrol.
Developing self-monitoring, self-assembled protein particle based drug delivery system for biomedical application
A mechanistic approach for understanding acid resistance by Enterohemorrhagic Escherichia coli in mammalian stomach.
Production of a crucial therapeutic protein for Trauma and Accident care in Escherichia coli system.
Satellite project-I: Development of strategies for recombinant production and functional expression of therapeutically important proteins in microbial systems.
Characterisation of refolding intermediates of multi-domain protein malate synthase G using mass spectroscopic method.
GroEL-GroES assisted folding of multiple proteins in vivo and in vitro.
