New strategies for fluorescently labeling proteins in the study of amyloids

Abstract

Amyloid proteins are widely studied, both for their unusual biophysical properties and their association with disorders such as Alzheimer's and Parkinson's disease. Fluorescence-based methods using site-specifically labeled proteins can provide information on the details of their structural dynamics and their roles in specific biological processes. Here, we describe the application of different labeling methods and novel fluorescent probe strategies to the study of amyloid proteins, both for in vitro biophysical experiments and for in vivo imaging. These labeling tools can be elegantly used to answer important questions on the function and pathology of amyloid proteins.

Keywords: Amyloid; Aβ; Click chemistry; ESIPT; FRET; Fluorescent; Huntingtin; Native chemical ligation; SNAP tag; Tau; Unnatural amino acid; α-synuclein.