Regensburg 2019 – wissenschaftliches Programm
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BP: Fachverband Biologische Physik
BP 1: Protein structure and dynamics
BP 1.4: Vortrag
Montag, 1. April 2019, 10:30–10:45, H4
Single Amyloid Fibrils Studied in a Thermophoretic Trap — •Martin Fränzl1, Tobias Thalheim1, Juliane Adler2, Daniel Huster2, and Frank Cichos1 — 1Peter Debye Institute for Soft Matter Physics, Molecular Nanophotonics Group, Universität Leipzig, Linnéstr. 5, 04103 Leipzig, Germany — 2Institute for Medical Physics and Biophysics, Universität Leipzig, Härtelstr. 16-18, 04107 Leipzig, Germany
The aggregation of soluble proteins into highly ordered, insoluble amyloid fibrils is characteristic for a range of neurodegenerative disorders. While many different techniques have been applied to the investigation of fibril formation, almost all of them address the average properties of the ensemble. Here, we present a method that removes the ensemble average observing single fibrils freely dispersed in solution enabling to detect events commonly hidden in the ensemble average. The trapping scheme is based on the thermophoretic drift of nano-objects in temperature gradients allowing to probe the dynamics of a single fibril at various stages of its growth, e.g., the time evolution of the diffusion coefficients. It is shown that the rotational diffusion coefficient provides a unique measure to follow the growth of single fibrils with a precision below the optical resolution. Fibril growth of a few 10 nm can be identified providing a promising platform for studies of molecular interactions and in particular of protein and macromolecular aggregation processes at the single fibril level.