Regensburg 2013 – scientific programme
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BP: Fachverband Biologische Physik
BP 8: Posters: Proteins
BP 8.6: Poster
Monday, March 11, 2013, 17:30–19:30, Poster B2
Dynamic force spectroscopy on the binding of monoclonal antibodies to tau peptides — •Carolin Wagner1, David Singer2, Tim Stangner1, Christof Gutsche1, Ralf Hoffmann2, and Friedrich Kremer1 — 1Leipzig University, Department of Molecular Physics, Leipzig, Germany — 2Leipzig University, Institute for Bioanalytical Chemistry, Leipzig, Germany
Optical tweezers-assisted dynamic force spectroscopy (DFS) is employed to investigate specific receptor/ligand bindings on the level of single binding events [1]. Here, the binding of the phosphorylation-specific antibody HPT-101, to synthetic tau-peptides with two potential phosphorylation sites (Thr231 and Ser235) is analyzed. According to ELISA-measurements, the antibody binds only specificly to the double-phosphorylated tau-peptide. It is shown by DFS that HPT-101 binds also to each sort of the mono-phosphorylated peptides. By analyzing the measured rupture-force distributions characteristic parameters like the lifetime of the bond without force, the characteristic length and the free energy of activation are determined for all interactions. The longest lifetime is obtained for the specific binding to the double-phosphorylated peptide. Furthermore we introduce a method to estimate the relative affinity of the bonds from dynamic single-molecule experiments. The result is in accordance with the ELISA measurements.
[1] C. Wagner et al., Soft Matter, 2011, 7 (9), 4370 - 4378