Structure and epitope mapping of the conformational anti tau antibody DC11

Abstract

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.

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BibTeX RIS

BibTeX

@misc{njemoga2026structure,
  title = {{Structure and epitope mapping of the conformational anti tau antibody DC11}},
  author = {S. Njemoga and L. P. Jenner and V. Volko and A. Polak and L. Fialova and T. Augustin and J. Hanes and A. Kozelekova and R. Crha and L. Ilkovicova and R. Skrabana and P. Kaderavek and P. Kolenko and T. Smolek and E. Kontsekova and B. Kovacech and J. Hritz and O. Cehlar},
  howpublished = {bioRxiv},
  year = {2026},
  month = sep,
  doi = {10.64898/2026.09.01.748351},
  url = {https://www.biorxiv.org/content/10.64898/2026.09.01.748351v1},
  note = {CC BY-NC},
}

RIS

TY  - UNPB
TI  - Structure and epitope mapping of the conformational anti tau antibody DC11
AU  - S. Njemoga
AU  - L. P. Jenner
AU  - V. Volko
AU  - A. Polak
AU  - L. Fialova
AU  - T. Augustin
AU  - J. Hanes
AU  - A. Kozelekova
AU  - R. Crha
AU  - L. Ilkovicova
AU  - R. Skrabana
AU  - P. Kaderavek
AU  - P. Kolenko
AU  - T. Smolek
AU  - E. Kontsekova
AU  - B. Kovacech
AU  - J. Hritz
AU  - O. Cehlar
PY  - 2026
DA  - 2026/09/01
PB  - bioRxiv
DO  - 10.64898/2026.09.01.748351
UR  - https://www.biorxiv.org/content/10.64898/2026.09.01.748351v1
AB  - 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.
ER  -

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