%0 journal article
%@ 2570-4206
%A Rumancev, C.,Vöpel, T.,Stuhr, S.,von Gundlach, A.,Senkbeil, T.,Osterhoff, M.,Sprung, M.,Garamus, V.,Ebbinghaus, S.,Rosenhahn, A.

%D 2021
%J ChemSystemsChem
%N 3
%P e2000050 
%R doi:10.1002/syst.202000050
%T In Cellulo Analysis of Huntingtin Inclusion Bodies by Cryogenic Nanoprobe SAXS
%U https://doi.org/10.1002/syst.202000050
3 
%X Huntington's disease (HD) is one of nine neurodegenerative disorders associated with an extension of polyglutamine (polyQ) in proteins. In HD, the polyQ tract in the huntingtin protein is extended beyond a threshold of 38 amino acids leading to the formation of amyloidal structures in the cytoplasm and nucleus. We investigated here the structure of Htt (Huntingtin) amyloid fibrils in cellulo with nanoprobe small angle X‐ray scattering. As these measurements were performed under cryogenic conditions, the information is obtained on the aggregates in their natural, hydrated environment without the need of staining and chemical fixation. We also could show the presence of oligomer structures not visible in fluorescence microscopy. Structural information on repetitive units inside of Htt inclusion bodies was determined from the SAXS data and compared to electron microscopy images. The results suggest that nanoprobe cryo‐SAXS can serve as powerful tool to investigate the kinetics of amyloid aggregate formation inside cells and to understand how fibril formation can be influenced by drugs and other external stimuli.