A FRET sensor for non-invasive imaging of amyloid formation in vivo.

ABSTRACT: Misfolding and aggregation of amyloidogenic polypeptides lie at the root of many neurodegenerative diseases. Whilst protein aggregation can be readily studied in vitro by established biophysical techniques, direct observation of the nature and kinetics of aggregation processes taking place in vivo is much more challenging. We describe here, however, a Förster resonance energy transfer sensor that permits the aggregation kinetics of amyloidogenic proteins to be quantified in living systems by exploiting our observation that amyloid assemblies can act as energy acceptors for variants of fluorescent proteins. The observed lifetime reduction can be attributed to fluorescence energy transfer to intrinsic energy states associated with the growing amyloid species. Indeed, for a-synuclein, a prote

SUBMITTER: Kaminski Schierle GS 

PROVIDER: S-EPMC5402868 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature