Sub‐Diffraction Imaging of Huntingtin Protein Aggregates by Fluorescence Blink‐Microscopy and Atomic Force Microscopy

Neurodegenerative disorders such as Alzheimer’s, Parkinson’s, and Huntington’s diseases are all associated with protein misfolding, aggregation, and the accumulation of insoluble amyloid aggregates in neurons.[1] Huntington’s disease is caused by expansion of a polyglutamine (polyQ) tract within exon 1 of the huntingtin (Htt) protein beyond a threshold of approximately 40 glutamine residues. An expanded polyQ tract enhances Htt propensity for aggregation and leads to the neuronal dysfunction and loss associated with Huntington’s disease.[2] Characterization of Htt aggregate species is critical for understanding the mechanism of Huntington’s disease and identifying potential therapies.