The faculty of the School actively pursue research in their areas of expertise. The research areas range from chaperone assisted protein folding, protein engineering, amyloids, to virus-host interactions, cell penetrating peptides, diabetes, kinetcs of self assembly and protein folding. More details about the research of individual faculty members is given below..
The School has labs located in two contiguous buildings connected by a corridor - the Basement labs and the Main Building labs. The faculty have designated lab areas and an open policy is followed by the School where all equipment and facilities are shared.
The lab infrastructure was created by IIT Delhi and the equipment was obtained purchased using the core Kusuma Trust grant and grants obtained by the faculty from various sponsoring agencies.
The labs as designated under faculty members is as given below.
Application of engineering principles towards mechanistic insights into biological systems and engineering robust solutions inspired by bio-design (self assembly and coordinated events).Learn More →
Our lab intends to explore versatility of cell penetrating peptides (CPPs). They can be used as therapeutic peptides as well as Nano carriers. Additionally, we are working on plant phenomics and IPR and regulatory issues in novel life science technologies such as nanomedicine, synthetic biology.Learn More →
Ashok’s early training at BSc. and MSc. Level was in Physics at BHU, Varanasi, India. He joined the Molecular Biology Unit, Institute of Medical Sciences, BHU, Varanasi for Ph.D. with Prof. J.V. Medicherla where he carried out structural and biophysical studies of proteins from natural source.Learn More →
"Genome to Drug" vision of SCFBio envisages delivering a drug molecule to society from genomic / proteomic information. It assimilates the language of genomic DNA and identifying a druggable protein coding gene (via Chemgenome) for a disease / disorder, determination of the three dimensional structure of the protein targets (via BhageerathH+) and ultimately creating a small molecule (drug) that can bind with high affinity and specificity to the Protein/DNA target but with least toxicity to humans (via Sanjeevini).Learn More →
Our group studies L-asparaginases from thermophilic and pathogenic bacterium and works on identifying their physiological function, engineering them to work under optimal physiological conditions and designing small molecules that could effectively block their activity.Learn More →
During last two decades our research interests have been understanding the molecular mechanism of insulin resistant diabetes. In one hand my laboratory has contributed in deciphering the complex signal transduction cascade to elucidate the mechanism of regulation of insulin resistance in skeletal muscle and neuronal cells.Learn More →
Our group works in the area of neurodegenerative diseases with focus on amyotrophic lateral sclerosis (ALS) and Alzheimer's disease(AD). We use methods of network analyses and systems theory to examine how these diseases onset and progress. Currently, were are studying the role of the angiogenin protein in ALS. In collaboration with AIIMS we study the clinical aspects, and in the lab we use computational method to design experiments to test hypothesis and perform cell culture experiments for validation. We also collaborate with the Chem Eng Dept IITD to design advanced controllers and develop control strategies for bioprocesses.Learn More →
Understanding how viruses interact with the host cells, how they disassemble to release their genome and assemble into progeny virions, and how they subvert the host cellular innate immunity system will not only help develop effective anti-virals, but also affords us analyses of many basic biological questions.
It is conventionally known from the time of C. B. Anfinsen that the information needed for the correct folding of a nascent polypeptide is inscribed within its amino acid sequence. However, over the years, it has been understood that a substantial fraction of the information needed for the folding process comes from the specific environment in which the protein is located. Often, neither of these information inputs are optimum for the efficient folding of a protein. As a result, a great number of proteins are susceptible to misfolding and aggregation inside the cell. Molecular chaperones appear to have evolved to facilitate protein folding by somehow preventing these adverse side reactions.Learn More →