1. We have developed novel protocol for solubilisation of proteins from inclusion bodies without the use of high urea concentration that helps in purification of recombinant proteins at industrial scale with activity retention. ( cited in 15 US patents and high impact journals)

2. Our group has successfully purified and characterised 3 novel lectins from various leguminous and non- leguminous plants and studied the folding mechanism of lectins under various conditions like in presence of urea, cosolvents and surfactants etc.

3. We have established the mechanistic insight into interaction of some drugs with serum albumins in clinically impaired condtions that may help in understanding pharmacokinaetics and pharmacodynamics of drugs.

4. Currently our studies are centred on protein misfolding and aggregation. We have designed a protocol for inducing aggregation (particularly amyloids) in all kinds of protein using SDS that aids in understanding the intricacies of the mechanism of protein aggregation. We have also designed surfactant-based rosin for inducing amorphous aggregation in protein.

Protein misfolding is major cause of neurodegenerative diseases in humans like Alzheimer’s, Parkinson’s diseases. No cure is established till date only medications to alleviate the symptoms are established, so our group is actively engaged in development of drugs for therapeutic intervention. We found antiamyloidogenic potential of naphthalene derivatives and nordihydroguaearitic acid (NDGA) that may aid in the design of more effective therapeutic strategies against amyloid associated neurodegenerative disorders. More remarkably, we recently demonstrated the anti-amyloidogenic nature of some anti-tuberculosis drugs ,vitamin A,B,C,K against amyloid beta aggregation in-vitro and study is in progress on the in-vivo system (Alzheimer’s mice model) and results obtained are highly promising. This work may have possible implication in the treatment of Alzheimer’s and other neurodegenerative diseases in humans.