Dresden 2014 – scientific programme
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CPP: Fachverband Chemische Physik und Polymerphysik
CPP 19: Poster Session 1 (joint session with BP)
CPP 19.15: Poster
Tuesday, April 1, 2014, 09:30–13:00, P1
Multivalency in the binding of the viral transmembrane protein hemagglutinin with the cellular receptor sialic acid studied by single molecule force spectroscopy — •Valentin Reiter1, Sumati Bhatia2, Manuel Gensler1, Christian Sieben1, Daniel Lauster1, Susanne Liese2, Andreas Herrmann1, Rainer Haag2, Roland Netz2, and Jürgen P. Rabe1 — 1Humboldt-Universität zu Berlin — 2Freie Universität Berlin
We use force spectroscopy techniques based on the scanning force microscope (SFM) to gain insight into the multivalent interactions between the viral transmembrane protein hemagglutinin (HA)and sialic acid (SA), a part of the cellular glyco-proteins. The binding of a virion to its host in order to induce the endocytosis is the first step in the reproduction of the virus and therefore the inhibition of this attachment is a good approach to prevent infection of cells. Custom designed nano particles outfitted with SA can be used as decoy particles to prevent the virion from attaching itself to a cell membrane [1],[2]. In order to increase the probability and efficiency of the binding of the nano particle to the virus the process of binding and unbinding of the HA to the SA has to be well understood, so that scaffolds suitable to fit the HA binding pockets can be designed. In order to obtain insight into the binding affinities, single molecule force spectroscopy (SMFS) can be used by functionalizing the SFM cantilever with receptor molecules and creating structured arrays of the ligand HA using poly histidine tags. [1] I. Papp et al., small 2010, 6,No. 24, 2900-2906; [2] I. Papp et al., ChemBioChem 2011,12, 887-895;