Dresden 2014 – wissenschaftliches Programm
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CPP: Fachverband Chemische Physik und Polymerphysik
CPP 19: Poster Session 1 (joint session with BP)
CPP 19.16: Poster
Dienstag, 1. April 2014, 09:30–13:00, P1
Amino Acid-Sequence Dependent Interactions between Receptors and Ligands Studied with Optical Tweezers — •Tim Stangner1, Carolin Wagner1, David Singer2, Stefano Angioletti-Uberti3, Christof Gutsche1, Joachim Dzubiella3, Ralf Hoffmann2, and Friedrich Kremer1 — 1University of Leipzig, Department of Experimental Physics I, D-04103 Leipzig, Germany — 2University of Leipzig, BBZ, D-04103 Leipzig, Germany — 3Humboldt University Berlin, Department of Physics, Berlin 12489, Germany
For diagnostic procedures that rely on monoclonal antibodies (mAbs), it is imperative to know whether the antibody recognizes the epitope of its target peptide/protein specific or whether possible cross-reactions to other forms of the protein may occur. In a previous study non-specific interactions of the phosphorylation-specific mAb HPT-101 to tau-peptides with similar epitopes, differing only by a single isolated phosphorylation site, were detected. Based on this result, it is obvious that the specificity of this mAb refers not exclusively to the phosphorylation pattern but also to the amino acid sequence in the tau peptide. Here, we investigate with the help of optical tweezers assisted dynamic force spectroscopy the influence of single amino acids on the binding of mAb HPT-101 to the peptide tau[pThr231/Ser235]. For this purpose, we characterize the unbinding process by analyzing the measured rupture force distributions. Furthermore, the binding process is specified by means of the relative binding frequency. Using these parameters, it is possible to identify essential as well as secondary amino acids for the interaction of this receptor-ligand system.