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Long-term, super-resolution imaging of amyloid structures using transient amyloid binding microscopy

Ding, T; Spehar, K; Bieschke, J; Lew, MD; (2019) Long-term, super-resolution imaging of amyloid structures using transient amyloid binding microscopy. In: Progress in Biomedical Optics and Imaging - Proceedings of SPIE. SPIE: San Francisco, California, United States. Green open access

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Abstract

Amyloid fibrils and tangles are signatures of Alzheimer disease, but nanometer-sized aggregation intermediates are hypothesized to be the structures most toxic to neurons. The structures of these oligomers are too small to be resolved by conventional light microscopy. We have developed a simple and versatile method, called transient amyloid binding (TAB), to image amyloid structures with nanoscale resolution using amyloidophilic dyes, such as Thioflavin T, without the need for covalent labeling or immunostaining of the amyloid protein. Transient binding of ThT molecules to amyloid structures over time generates photon bursts that are used to localize single fluorophores with nanometer precision. Continuous replenishment of fluorophores from the surrounding solution minimizes photobleaching, allowing us to visualize a single amyloid structure for hours to days. We show that TAB microscopy can image both the oligomeric and fibrillar stages of amyloid-β aggregation. We also demonstrate that TAB microscopy can image the structural remodeling of amyloid fibrils by epi-gallocatechin gallate. Finally, we utilize TAB imaging to observe the non-linear growth of amyloid fibrils

Type: Proceedings paper
Title: Long-term, super-resolution imaging of amyloid structures using transient amyloid binding microscopy
Event: SPIE BiOS, 2019
Location: San Francisco, California, United States
Dates: 2-7 Feb 2019
ISBN-13: 9781510624108
Open access status: An open access version is available from UCL Discovery
DOI: 10.1117/12.2507656
Publisher version: https://doi.org/10.1117/12.2507656
Language: English
Additional information: This version is the version of record. For information on re-use, please refer to the publisher’s terms and conditions.
UCL classification: UCL
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences > UCL Institute of Prion Diseases
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences > UCL Institute of Prion Diseases > MRC Prion Unit at UCL
URI: https://discovery.ucl.ac.uk/id/eprint/10076805
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