In neuronal cells, tau proteins regulate the access of other protein to microtubules. Pathological self-assembly of tau is a hallmark of a several neurodegenerative diseases, including Alzheimer’s. While super-resolution microscopy has become the essential tool in understanding the structure and function of living systems, its fluorescence principle hinders imaging highly dynamical or complex systems. This blind spot in the observation of assembling protein structures hinders our understanding of some of the key processes including the earliest stages of the tau aggregate formation. To capture the mechanisms of tau aggregates formation at single-protein details we will introduce a new label-free method based on direct detection of single-protein fluctuation using interferometric scattering microscopy (iSCAT). We will advance the interferometric scattering microscopy to resolve fluctuations of single proteins addressing details of the assembly of tau proteins into protein envelopes on microtubules.
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