Research Projects

Corneal blindness remains a significant global health concern, affecting millions of individuals and ranking as one of the leading causes of visual impairment. The cornea, being the transparent and avascular front layer of the eye, plays a critical role in focusing incoming light onto the retina. Any structural damage or disease affecting the cornea can result in severe vision loss. Currently, corneal transplantation either through penetrating keratoplasty or lamellar grafts represents the primary therapeutic intervention. However, its widespread application is hindered by several limitations: a persistent shortage of donor tissue, risk of immune-mediated graft rejection, post-operative complications, and the requirement for prolonged immunosuppressive therapy, all of which compromise treatment accessibility and long-term success, particularly in developing regions. In response to these limitations, corneal tissue engineering has emerged as a promising strategy aimed at reconstructing the damaged cornea using biomimetic scaffolds that promote cellular attachment, proliferation, and differentiation in three dimensions, closely mimicking in vivo conditions. Among the emerging scaffold materials, self-assembling peptide-based hydrogels have emerged as next-generation biomaterials due to their inherent biocompatibility, biodegradability, and tunable physicochemical properties. Ultrashort peptides (di-, tri-, and tetrapeptides) are especially attractive owing to their low cost, synthetic accessibility, and reduced immunogenicity. They can self-assemble into nanofibrillar networks that closely mimic the cornea's natural extracellular matrix (ECM), and their high-water content, mechanical flexibility, and ability to encapsulate and deliver bioactive molecules make them ideal for ocular applications. Their synthetic simplicity, structural tunability, and low immunogenic profile make them cost-effective and scalable alternatives to longer peptides or protein-based materials. In our earlier studies, we identified ultrashort peptide sequences (3–4 amino acids) derived from TAR DNA-binding protein 43 (TDP-43), a nuclear protein implicated in RNA metabolism and known for its pathological aggregation in neurodegenerative diseases. These short sequences were found to self-assemble into dense fibrillar structures under physiological conditions, forming hydrogel-like networks that are believed to drive the aggregation behavior of the full-length TDP-43 protein. In the present study, we propose to utilize these self-assembling peptides for their biomedical application in tissue engineering, as the resulting hydrogel scaffolds can provide a three-dimensional environment that closely mimics in vivo conditions favorable for supporting cell adhesion, proliferation, and functional tissue regeneration. This project utilizes the self-assembling properties of ultrashort peptides to develop next-generation corneal scaffolds with tunable mechanical strength that closely mimic native tissue. This peptide-based platform addresses key limitations of current grafts and holds strong potential for translation into clinically viable therapies for corneal blindness.