Abstract
Recently, there have been reports of an intrinsic protein fluorescence that is specific to structures containing a high proportion of β-sheets. It has been observed from a range of protein aggregates and crystals, and most notably also from protein amyloids that have been associated with protein misfolding diseases, including Alzheimer's disease, Parkinson's disease and various types of amyloidosis. Fluorescence emission of this kind occurs in the visible range, and appears to be independent of the presence of aromatic residues within the polypeptide structure. In this chapter, we review current evidence for this recently discovered amyloid-specific intrinsic fluorescence, and explore possible directions for future research. We outline studies of protein aggregation kinetics using intrinsic protein fluorescence, which open up exciting new opportunities for the study of protein misfolding diseases with optical methods.
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