Interested candidates with CSIR-JRF/UGC-JRF/Inspire fellowship are invited to join our research group. Send your CV to ganesh@clri.res.in
Supramolecular gels obtained from organic low molecular mass (LMM) compounds find potential applications in various fields including biology, medicine, chemistry, and biological materials.
We @ CLRI develop various supramolecular gels to understand the molecular mechanism of LMM self-assembly-induced gelation.
Our research interest also includes the development of supramolecular hydrogels and organogels using biomimetic LMM compounds for diverse applications, especially in drug delivery, cell proliferation, Anti-microbial activity, dye removal, etc.
Not only hydrogels and organogels, we are also interested in developing "ambidextrous gelators" using LMM compounds as they provide additional advantages in the arena of supramolecular gels.
In addition to supramolecular gels, our group is also interested in developing supramolecular hierarchical structures from amino acids and smaller peptide-based LMM compounds.
Collagens derived from animals are commonly used in biomaterial preparations for tissue engineering and other biomedical applications. However, these collagens have inherent limitations, such as causing allergic reactions. In this context, collagen mimetic peptides (CMPs) are considered a promising alternative to animal collagen for biomaterial development. Nevertheless, mimicking collagen with CMPs presents significant challenges due to the difficulty in designing CMPs that exhibit stable triple-helix structures, fibril formation, and hydrogel-forming tendencies in short sequences.
Our group at CLRI has undertaken the challenge of replicating these properties of collagen using strategically designed short CMP sequences. This effort has led to the development of novel CMPs, which hold potential for applications in tissue engineering and drug delivery systems.
Protein fibrillation is the major cause of amyloidosis which includes Alzheimer's disease, Parkinson's Disease, Prion Diseases, etc. Inhibition of such protein fibrillation is one of the best therapeutic ways for amyloid diseases.
We @ CLRI searching for natural small molecules as protein fibril inhibitors using various biophysical techniques.
Collagen is the most abundant fibrous protein in the extracellular matrix of our body. Under normal physiological conditions, homeostasis of tissue collagen is constantly maintained. But, during a number of pathological processes, collagens are over produced and accumulated. Such excess accumulation of collagens (referred to as fibrosis) is found to be the hallmark of many localized fibrotic diseases namely keloids, systemic scleroderma, atherosclerosis, and hypertrophic scars.
We @ CLRI searching for inhibitors of collagen fibrillation, a proposed to way to stop fibrosis, using biophysical techniques.
In addition, we are also interested in understanding the interaction of various small molecules with collagen which is needed for the stabilization of collagen.