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Protein-protein and protein-lipid interfaces on cell surfaces are the physical domains where membrane-bound proteins interact with other proteins or the lipid bilayer to facilitate essential cellular processes. These interfaces are critical for the assembly of signaling complexes, the regulation of receptor activity, and the maintenance of cell-cell adhesion (Source: Nature Reviews Drug Discovery, 2016). In many disease states, such as cancer and viral infections, these interfaces are often dysregulated or exploited, leading to aberrant signaling or pathogen entry (Source: Annual Review of Biomedical Engineering, 2016). While historically considered 'undruggable' due to their large and relatively featureless topography, they are increasingly targeted by specialized small molecules, macrocycles, and biologics designed to disrupt or stabilize specific interactions (Source: Frontiers in Molecular Biosciences, 2019). As a target class, they represent a broad structural category rather than a single discrete molecule, encompassing a wide variety of therapeutic mechanisms across multiple disease areas.
Modulation of cellular signaling or structural integrity by competitively inhibiting or allosterically stabilizing the physical contact between two proteins or between a protein and the surrounding lipid bilayer.
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