Shear-Induced Orientational Order of the Nematic Phase of Amyloid Fibrils probed by in-situ Rheo – GISANS
The fibrillization of peptides has attracted a lot of interest for many years as a result of its close association with degenerative diseases, for example, Alzheimer’s, Parkinson’s, and diabetes type II. It is widely recognized that such disorders arise from protein misfolding followed by self-assembly into cytotoxic oligomers which form fibrillar structures usually rich in β-strands, which are so-called amyloid fibrils. Understanding the mechanisms involved in amyloid formation is a significant challenge in both fundamental research and in the development of amyloid fibril-based nanomaterials. The proposed experiment aims to perform simultaneous GISANS/rheology on a class of octapeptides including (RF)4 and RFL4FR, which is a bola-amphiphile based also on the Arg-Phe pair but with a tetraleucine “central spacer”. The correlation between the structure and alignment, at the solid liquid surface probed by GISANS, with changes in the rheological response (shear and temperature) will be completed.
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NEWBY GEMMA; DA SILVA Emerson Rodrigo; GUTFREUND Philipp; HAMLEY Ian; HERMIDA MERINO DANIEL and PEDERSEN Martin Nors. (2016). Shear-Induced Orientational Order of the Nematic Phase of Amyloid Fibrils probed by in-situ Rheo – GISANS. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-02-782
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