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BP: Fachverband Biologische Physik
BP 7: Bioimaging and biospectroscopy II
BP 7.2: Talk
Tuesday, April 2, 2019, 09:45–10:00, H4
Imaging nanoscale aggregation of proteins ex vivo using the contrast in Förster resonance energy transfer obtained from 2D polarization fluorescence imaging (2D POLIM) — •Daniela Täuber1, Adrian T. Press2, Petra Martinac2, Kay-Jovanna Benecke2, Michael Bauer2, Juanzi Shi3, and Ivan G. Scheblykin3 — 1Biopolarisation, Leibniz-IPHT & Friedrich-Schiller-University Jena, Germany — 2Anesthesiology and Intensive Care Medicine & Center for Sepsis Control and Care, Jena University Hospital — 3Single Molecule Spectroscopy, Lund University, Sweden
Förster resonance energy transfer (FRET) is a well-established nanoruler suited to discriminate small aggregates of fluorescent molecules from just high concentration. Contrary to spectrally resolved two-color-FRET, polarization resolved fluorescence microscopy allows to determine homo-FRET between similar fluorophores. Conventional fluorescence anisotropy is restricted to isotropic samples, otherwise, the results depend on the choice of the lab frame. 2D POLIM was recently applied to study early protein aggregation of GFP-labeled human α-synuclein in models of Parkinson's disease ex vivo.[1] We used 2D POLIM to study f-actin aggregation in healthy and pathologic liver tissue, which is related to liver damage in systemic infection. A qualitative analysis showed variations of the FRET parameter, which can be compared to the pathologic condition of the sample. -- [1] Camacho et al. 2D Polarization Imaging as a Low-Cost Fluorescence Method to Detect α-Synuclein Aggregation Ex Vivo in Models of Parkinson's Disease. Commun. Biol. 2018, 1, 157.