Recognizing cell surface proteins through protein–protein interactions or broader receptor-ligand interactions is a central strategy for regulating intracellular signal transduction,as well as for the diagnosis and treatment of diseases,particularly autoimmune disorders[1].The most widely used approach involves functionalizing nanoparticles through post-grafting methods such as chemical bonding,physical adsorption,and electrostatic interactions to modulate signal transduction mediated by membrane receptor proteins.These synthetic particles—comprising polymers,dendrimers,inorganic particles,nanofibers,and others—possess nanoscale features that translate the subtle differences in ligand nanostructures into diverse cellular responses through ligand-receptor interactions[2].Notably,protein receptors on the cell surface typically exhibit a heterogeneous or discontinuous dynamic distribution,complicating the precise recognition and targeted isolation of these membrane receptors.Furthermore,certain membrane protein receptors tend to aggregate into specific structural domains,or even form higher-order clusters,coexisting with adjacent proteins to regulate their functions[3].Traditional particle surface technologies have typically relied on simple anchored ligand approaches.These methods often fail to effectively control the density,spacing,and spatial arrangement of ligands,posing challenges in precisely regulating cellular signal transduction.By contrast,DNA origami technology capitalizes on the self-assembly capabilities of DNA molecules to create precise nanoscale structures.It is notable for its programmability,high precision,and excellent biocompatibility.By designing specific DNA strands,various shapes and patterns can be folded,achieving the meticulous spatial design of molecular arrangements.DNA origami enables the construction of arbitrary 2D nanostructures and provides templates for arranging nanomaterials and 3D structures,making a significant advancement in DNA nanotechnology[4].In summary,DNA origami t
