Neurodegenerative diseases are linked to aggregation of particular proteins. The investigation of pathologic pathways and the development of suitable medication demand for methods to visualize protein aggregation ex vivo. Sophisticated microscopy often requires two color labelling, while conventional fluorescence microscopy can reveal the expression of such proteins in brain tissue, but not their aggregation. Here we apply 2-dimensional polarization imaging [1] to visualize aggregation of human α-synuclein expressed in brain tissue from transgenic mice. We employ Förster Resonance Energy Transfer (FRET) between identical (single color) green fluorescent protein (GFP) tags linked to α-synuclein. We obtain information on aggregation, which cannot be seen from fluorescence intensity [3]. Our finding of α-synuclein aggregation in olfactory bulbs of old mice correlates with results from a behavioral study on that mice [2]. The aggregation pattern was not found in young mice.

[1] Camacho, R. et al., Chem. Phys. 406, 30, 2012.

[2] Hansen, C. et al., Neurobiol. Dis. 56, 145, 2013.

[3] Camacho, R. et al., submitted.