Amyloid fibrils are implicated in a number of diseases, known as amyloidosis, including Alzheimer's disease. The diseases are associated with misfolding of a particular protein into fibrils that accumulate in the body's organs as plaques. Anilinonaphthalene sulphonic acid (ANS) binds hydrophobic patches on the surface of amyloid fibrils and its fluorescence was used to report on fibril formation.
The BMG LABTECH multi-mode plate reader followed protein aggregation kinetics using fluorescence measurements. The amyloid formation was detected by an increase in ANS-fluorescence intensity. Furthermore, we have shown that using the script mode it is possible to make timed ex situ measurements fairly simply, creating an output into a single CSV file.