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5 March 2021 Thermophoretic trapping of single amyloid fibrils
Tobias Thalheim, Benjamin Fanselow, Martin Fränzl, Juliane Adler, Daniel Huster, Juliane Posseckardt, Michael Mertig, Frank Cichos
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Proceedings Volume 11647, Imaging, Manipulation, and Analysis of Biomolecules, Cells, and Tissues XIX; 1164711 (2021) https://doi.org/10.1117/12.2578289
Event: SPIE BiOS, 2021, Online Only
Abstract
Amyloid fibrils are highly stable and organized peptide or protein structures that on the one hand can cause partially severe diseases such as Alzheimer's disease and on the other hand play fundamental roles during a plethora of biological processes. Nevertheless, there are still plenty open questions concerning their formation. We present a thermophoretic trap which is able to confine the Brownian motion of single amyloid fibrils via temperature gradients. The time-resolved tracking of the fibrils' rotational diffusion coefficients in presence of monomers permits to extract their growth rates or to directly observe secondary growth processes as fragmentation.
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Tobias Thalheim, Benjamin Fanselow, Martin Fränzl, Juliane Adler, Daniel Huster, Juliane Posseckardt, Michael Mertig, and Frank Cichos "Thermophoretic trapping of single amyloid fibrils", Proc. SPIE 11647, Imaging, Manipulation, and Analysis of Biomolecules, Cells, and Tissues XIX, 1164711 (5 March 2021); https://doi.org/10.1117/12.2578289
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KEYWORDS
Diffusion
Alzheimer's disease
Plasmonics
Proteins
Thermography
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