Hannover 2013 – scientific programme
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MO: Fachverband Molekülphysik
MO 19: Poster 2: Biomolecules, Cold Molecules, Experimental Techniques, Various Topics
MO 19.21: Poster
Wednesday, March 20, 2013, 16:00–18:30, Empore Lichthof
Fluorescence spectroscopy on a potential new drug: Interaction of anle138b with α-synuclein aggregates — •Anne Reiner1, Andreas Deeg1, Felix Schmidt2, Florian Schüder1, Andrei Leonov3, Sergey Ryazanov3, Wolfgang Zinth1, Christian Griesinger3, and Armin Giese2 — 1Lehrstuhl für BioMolekulare Optik, LMU München, Oettingenstr. 67, 80538 München — 2Zentrum für Neuropathologie und Prionenforschung, LMU München, Feodor-Lynen-Str.23, 81377 München — 3MPI for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen
In neurodegenerative diseases such as Alzheimer’s, Parkinson’s and prion diseases, deposits of aggregated disease-specific proteins are found. Since protein aggregation is supposed to be a key event in the pathogenesis, compounds that bind to pathological aggregates and interfere with aggregation may provide a chance of disease-modifying therapy. In this contribution we investigate the aggregation inhibitor anle138b. The intrinsic fluorescence properties of anle138b are measured, to identify its binding to α-synuclein protein, which forms pathological cytoplasmic inclusion bodies in Parkinson’s disease. Measurements on anle138b incubated with monomeric α-synuclein did not show any changes in fluorescence properties. However one could find a strong change in the fluorescence and anisotropy in combination with fibrillar α-synuclein aggregates. These findings indicate that anle138b interacts selectively with specific structural epitopes present in aggregated α-synuclein. This observation may open a way to the understanding of the molecular mode of action of anti-aggregation drugs.