Protein misfolding is the major cause for neurodegenerative disorders, which affects more than 50 million people worldwide with symptoms like dementia. The detailed mechanisms of misfolding are yet to be understoodin particular to find treatments and preventive measures but are tightly linked to the phenomenon of intrinsic disorder proteins, which can undergo disorder-to-order transitions towards misfolded species upon interactions with certain biomolecules. Alzheimer's disease (AD) is the most common form of dementia and is associated with the aggregation of misfolded amyloid-beta (Aβ) peptides in AD patient's brain. The formation, structure and properties of these aggregates, socalled amyloid plaques, have been extensively studied in vitro and in vivo, and were thought for a long time to be the main cause of AD symptoms. However, more recently it has been pointed out that it is rather early stage oligomers that have cytotoxic properties, for instance, by perturbing the integrity of the lipid membrane in neuronal tissues. Investigating these early-stage structures and their specific interactions presents a considerable challenge and, thus, requires the development of methods that are able to track the structural transformations of Aβ in situ.