Dysregulated protein-protein interactions on the cell-surface initiate pathogenesis in diseases including cancer. Although antibodies and fusion proteins are the preferred approach to modulate such dysregulation, they suffer from a) need for parenteral dosing b) lack of flexibility in adjusting the exposure posing challenges for use in combination with other agents and to manage any emergent adverse events, c) suboptimal response due to poor tissue penetration and d) unaffordable cost. While lack of specific binding pockets is a deterrent for conventional small molecule approach, our peptide-derived approach exploits allosteric modulation and/or partial binding without disruption leading to functional antagonism and therapeutic benefit. We have established the technology to target cell surface protein interactions by arriving at a minimal pharmacophore based on the sequences from the receptor-ligand interface and then incorporating the pharmacophore on a non-peptidic template for optimal pharmacological activity. Our approach has resulted in drug candidates including the first immune checkpoint inhibitor with encouraging clinical activity.

Health and social work

Source: Ministry of Corporate Affairs company master (open data). Capital figures are as-of the 2021 registry snapshot, not live.