ArticleJournal of materials chemistry. B2026
Single-molecule force spectroscopy of ligand-receptor mechanics at extracellular vesicle biointerfaces.
Article in Journal of materials chemistry. B, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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9 authors.
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Abstract
Extracellular vesicles (EVs) are nanoscale membrane-bound particles that present surface receptors for affinity capture, sensing, and targeted biointerface design. Although EV surface-marker expression is widely used to guide ligand selection, the molecular-scale rupture mechanics and force-dependent dissociation behavior of EV receptor-ligand interactions remain poorly understood. Here, atomic force microscopy-based single-molecule force spectroscopy and dynamic force spectroscopy are used to quantify ligand-accessible recognition, rupture-force distributions, and apparent Bell-Evans parameters for three pancreatic cancer-associated EV surface targets: integrins (ITG), epithelial cell adhesion molecule (EpCAM), and glypican-1 (GPC1). EVs derived from PANC-1 and hTERT-HPNE cells were compared as a model system. PANC-1 EVs exhibited higher particle concentrations and stronger ITG and GPC1 expression than HPNE EVs. AFM recognition maps showed markedly higher apparent ITG recognition and moderately higher GPC1 recognition on PANC-1 EVs, whereas EpCAM recognition was similar between the two EV preparations. Fixed-speed rupture-force distributions and loading-rate-dependent analysis revealed interaction-dependent differences in apparent rupture behavior. Across both EV preparations, EpCAM-antibody interactions tended to show higher apparent force-free off-rates than ITG-cRGD and GPC1-antibody interactions, while ITG and GPC1 were less clearly separated. Together with recognition mapping, these results demonstrate that ligand-accessible recognition and force-dependent rupture behavior provide complementary information about EV surface interactions.
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