Thermophoretic trapping of single amyloid fibrils

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.