S. Njemoga, L. P. Jenner, V. Volko, A. Polak, L. Fialova, T. Augustin, J. Hanes, A. Kozelekova, R. Crha, L. Ilkovicova, R. Skrabana, P. Kaderavek, P. Kolenko, T. Smolek, E. Kontsekova, B. Kovacech, J. Hritz, O. Cehlar
Conformational antibody DC11 was previously shown to discriminate between physiological full length tau proteins and misfolded truncated tau proteins. It was also shown to catalyze in vitro tau aggregation, suggesting a connection with the pre-aggregation conformation of tau proteins. We have crystallized the Fab fragment of the DC11 antibody and characterized its binding with truncated tau proteins using ELISA, NMR and crosslinking mass spectrometry. The presumed model of the complex of DC11 antibody and truncated tau protein was obtained by docking tau321-391 conformations from coarse grained MD simulation into the antibody paratope.