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BP: Fachverband Biologische Physik
BP 21: Poster IIIb
BP 21.27: Poster
Wednesday, March 20, 2024, 11:00–14:30, Poster C
Binding Study of Beta-2-Glycoprotein I and Integrin-Containing Artificial Lipid Membranes — •Emma Weilbeer1, Una Janke1, Thomas McDonnell2, and Mihaela Delcea1 — 1Biophysical Chemistry Department, Institute of Biochemistry, University of Greifswald — 2Division of Medicine/ Biochemical Engineering, University College London, UK
Beta-2-glycoprotein I (β2GPI) is a highly glycosylated plasma protein and the most important antigenic target for autoantibodies in antiphospholipid syndrome. β2GPI circulates as a closed form but opens up under specific conditions. Although β2GPI has been found in blood clots, its physiological role is not yet fully understood. Therefore, it is of great importance to investigate the function and the dynamics of β2GPI in the coagulation cascade using for example, biophysical methods. Imaging of fluorescently labeled protein suggests that β2GPI binds to human embryonic kidney cells expressing αIIbβ3 integrin (i.e. the main platelet receptor essential for platelet aggregation and undergoing conformational dynamics). We have investigated the interaction of open and closed β2GPI with activated and non-activated integrin αIIbβ3-containing lipid bilayers mimicking the outer leaflet of platelet membranes. A combination of various biophysical methods (e.g. dynamic light scattering, circular dichroism spectroscopy, atomic force microscopy, surface plasmon resonance) have been used for protein characterization and protein-protein interactions. Our biomimetic model enables the specific analysis of disease relevant protein-protein interactions involving protein conformational dynamics.
Keywords: Beta-2-glycoprotein I; αIIbβ3 integrin; human embryonic kidney cells; artificial lipid membrane; conformational dynamics