Berlin 2018 – scientific programme
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BP: Fachverband Biologische Physik
BP 15: Postersession III
BP 15.14: Poster
Tuesday, March 13, 2018, 14:00–16:00, Poster B
Influence of phospholipid membranes on Beta2GPI conformation — •Peter Nestler1,2, Ina Buchholz1,2, and Mihaela Delcea1,2 — 1University of Greifswald, Institute for Biochemistry, Felix-Hausdorff-Str. 4, 17487, D-Greifswald, Germany — 2ZIK HIKE, Fleischmannstr. 42, 17489, D-Greifswald, Germany
Beta 2 glycoprotein I (Beta2GPI) is abundant in human plasma and known to be the main antigen involved in autoimmune antiphospholipid syndrome (APS). Beta2GPI exists in two main structural conformations: The open/active form which potentially leads to the formation of immunogenic antibody-protein complexes and the closed/passive form in which Beta2GPI has undergone folding and binding to itself. However, the exact physiological function of Beta2GPI has not been fully understood. Here we study the interaction of Beta2GPI with phospholipid model membranes. Supported lipid bilayers (SLB) of tetramyristoyl cardiolipin (TMCL) as well as mixtures of dimyristoyl phosphoglycerol (DMPG) and dimyristoyl phosphocholine (DMPC) are prepared using Langmuir-Blodgett transfer. A novel approach using atomic force microscopy (AFM) imaging data allows to quantitatively determine the conformation of flatly adsorbed Beta2GPI in presence and absence of SLB, respectively. First findings promise to elucidate the role of phospholipids in Beta2GPI activation.