Super-Resolution Imaging of Amyloid Structures over Extended Times Using Transient Binding of Single Thioflavin T Molecules
2018
Oligomeric amyloid structures are crucial therapeutic
targets in Alzheimer’s and other amyloid diseases. However, these
oligomers are too small to be resolved by standard light microscopy.
We have developed a simple and versatile tool to image amyloid
structures using Thioflavin T without the need for covalent labeling or
immunostaining. Dynamic binding of single dye molecules generates
photon bursts that are used for fluorophore localization on a
nanometer scale. Thus, photobleaching cannot degrade image
quality, allowing for extended observation times. Super-resolution
Transient Amyloid Binding (TAB) microscopy promises to directly
image native amyloid using standard probes and record amyloid
dynamics over minutes to days. We imaged amyloid fibrils from
multiple polypeptides, oligomeric, and fibrillar structures formed
during different stages of amyloid-β aggregation, as well as the
structural remodeling of amyloid-β fibrils by the compound epigallocatechin
gallate (EGCG).
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