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CPP: Fachverband Chemische Physik und Polymerphysik
CPP 24: Poster Session I
CPP 24.25: Poster
Montag, 16. März 2020, 17:30–19:30, P3
Thermophoretic Trapping of Single Amyloid Fibrils — Martin Fränzl1, •Tobias Thalheim1, Juliane Adler1, Daniel Huster1, Juliane Posseckardt2, Michael Mertig2,3, and Frank Cichos1 — 1Leipzig University, Germany — 2Kurt-Schwabe-Institut für Mess- und Sensortechnik e.V. Meinsberg, Germany — 3TU Dresden, Germany
The formation of aggregates of peptides is responsible for a number of neurodegenerative diseases. The individual steps of this aggregation from single soluble monomers or oligomers to highly ordered, insoluble amyloid fibrils, however, are commonly hidden in the ensemble average of common measurement techniques. The heterogeneity of the ensemble at all stages of the aggregation process hides the growth details such as secondary nucleation processes or fibril fragmentation. I will present on my poster a method that is able to trap single amyloid fibrils freely diffusing in solution relying on thermophoresis. This thermophoretic trap allows us to extract a lot of properties of the individual fibrils, like their Soret coefficients as well as the translational and rotational diffusion coefficients over time periods of at least several 10 minutes up to even hours. Repeating the measurement for several single fibrils permits us to measure a length dependence of the translational and rotational diffusion coefficients. Due to the high sensitivity of the rotational diffusion coefficient on length changes, we are furthermore able to study the growth of single fibrils down to a few 10 nm in the presence of monomers or monitor secondary nucleation events and fragmentation which have not been seen directly before.