Parts | Days | Selection | Search | Updates | Downloads | Help
BP: Fachverband Biologische Physik
BP 12: Poster II
BP 12.44: Poster
Tuesday, April 2, 2019, 14:00–16:00, Poster B2
Protein-radical interaction: structure analysis using atomic force microscopy — •Sanjai Karanth1,2, Una Janke1,2, and Mihaela Delcea1,2 — 1Institute of Biochemistry, University of Greifswald, Greifswald, Germany — 2ZIK HIKE, University of Greifswald, Greifswald, Germany
Reactive nitrosative species (RNS) such as nitric oxide (NO.) released in the body attack the thiol groups of proteins altering their function (e.g. protein activation upon ligand binding)[1]. Here, we investigate in a biomimetic system the interaction of RNS with integrin alpha IIb beta 3 (αIIbβ3)- a transmembrane protein present on blood platelets and responsible for thrombotic activity. αIIbβ3 protein was reconstituted into nanodiscs which generate planar lipid bilayers which stabilize the protein. Using atomic force microscopy (AFM) imaging, we were able to distinguish the different states of protein (i.e. open/active and closed/bent state). Radical attack on the nanodiscs was performed and structural analysis was carried out using AFM imaging and single molecule force spectroscopy (SMFS). Nanodiscs prove to be a reliable membrane system to study biophysical properties of transmembrane proteins.
[1] Mor-Cohen, R. (2016). Disulfide bonds as regulators of integrin function in thrombosis and hemostasis. Antioxidants & redox signaling, 24(1), 16-31.