Related Experiment Video
Updated: May 18, 2026
Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease
Published on: May 13, 2010
Crystallization and preliminary X-ray diffraction analysis of two peptides from Alzheimer PHF in complex with the
Rostislav Skrabana1, Ondrej Cehlar, Zuzana Flachbartova
1Institute of Neuroimmunology, Slovak Academy of Sciences, Dubravska cesta 9, 84 510 Bratislava, Slovakia.
Abstract:
The major constituent of the Alzheimer's disease paired helical filaments (PHF) core is the intrinsically disordered protein (IDP) tau. Globular binding partners, e.g. monoclonal antibodies, can stabilize the fold of disordered tau in complexes. A previously published structure of a proteolytically generated tau fragment in a complex with the PHF-specific monoclonal antibody MN423 revealed a turn-like structure of the PHF core C-terminus [Sevcik et al. (2007). FEBS Lett. 581, 5872-5878]. To examine the structures of longer better-defined PHF segments, crystals of the MN423 Fab fragment were grown in the presence of two synthetic peptides derived from the PHF core C-terminus. For each, X-ray diffraction data were collected at 100 K at a synchrotron source and initial phases were obtained by molecular replacement.
