Protein misfolding leading to aggregation and amyloid fibril formation has been implicated in a variety of neurodegenerative disorders. Under suitably designed in vitro conditions, intermolecular contacts between polypeptide chains mediated by various non-covalent interactions result in the formation of oligomeric species that are eventually sequestered into β-sheet-rich amyloid fibrils. Owing to the inherent heterogeneity and complexity of protein aggregation processes, detec- tion and structural characterization of the early, transiently-populated cytotoxic oligomeric intermediates during the amyloid fibrillation cascade still poses a formidable challenge. Fluorescence spectroscopy is an extremely sensitive multiparametric technique that provides simultaneous information about the con- formational- and size changes for both early oligomeric species as well as for the large-sized aggregates. In this review, we emphasize recent and selected examples on the application of various fluorescence spectroscopic techniques in the study of protein aggregation. Additionally, we also summarize the recent results on protein aggregation studies using fluorescence spectroscopy from our laboratory.
Learmonth, R. P. (2012). Reviews in Fluorescence 2010, 2010, 67–93. Retrieved from http://link.springer.com/10.1007/978-1-4419-9828-6