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Fluorescence Self-Quenching from Reporter Dyes Informs on the Structural Properties of Amyloid Clusters Formed in Vitro and in Cells
Abstract
The characterization of the aggregation kinetics of protein amyloids and the structural properties of the ensuing aggregates are vital in the study of the pathogenesis of many neurodegenerative diseases and the discovery of therapeutic targets. In this article, we show that the fluorescence lifetime of synthetic dyes covalently attached to amyloid proteins informs on the structural properties of amyloid clusters formed both in vitro and in cells. We demonstrate that the mechanism behind such a “lifetime sensor” of protein aggregation is based on fluorescence self-quenching and that it offers a good dynamic range to report on various stages of aggregation without significantly perturbing the process under investigation. We show that the sensor informs on the structural density of amyloid clusters in a high-throughput and quantitative manner and in these aspects the sensor outperforms super-resolution imaging techniques. We demonstrate the power and speed of the method, offering capabilities, for example, in therapeutic screenings that monitor biological self-assembly. We investigate the mechanism and advantages of the lifetime sensor in studies of the K18 protein fragment of the Alzheimer’s disease related protein tau and its amyloid aggregates formed in vitro. Finally, we demonstrate the sensor in the study of aggregates of polyglutamine protein, a model used in studies related to Huntington’s disease, by performing correlative fluorescence lifetime imaging microscopy and structured-illumination microscopy experiments in cells.
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“In addition, the dense packing of TauRD‐CFP in the accumulations may lead to self‐quenching of CFP, which would reduce the CFP lifetime independent of FRET with YFP acceptor molecules.”
From Molecular crowding and RNA synergize to promote phase separation, microtubule interaction, and seeding of Tau condensates (2022) · cites this paper as Chen et al, 2017
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Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders
Ballatore, C., Lee, V. M.-Y., & Trojanowski, J. Q. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2194 · Cited by 2,174
Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases
Selkoe, D. J. (2004) · Nature Cell Biology · doi:10.1038/ncb1104-1054 · Cited by 863
Sites of Tau Important for Aggregation Populate β-Structure and Bind to Microtubules and Polyanions
Mukrasch, M. D., Biernat, J., von Bergen, M., Griesinger, C., Mandelkow, E., & Zweckstetter, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501565200 · Cited by 324
Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins
Ciryam, P., Tartaglia, G. G., Morimoto, R. I., Dobson, C. M., & Vendruscolo, M. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.09.043 · Cited by 270
Extracellular Monomeric Tau Protein Is Sufficient to Initiate the Spread of Tau Protein Pathology
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Cited by
Hochmair, J., Exner, C., Franck, M., Dominguez‐Baquero, A., Diez, L., Brognaro, H., Kraushar, M. L., Mielke, T., Radbruch, H., Kaniyappan, S., et al. (2022) · The EMBO Journal · doi:10.15252/embj.2021108882 · Cited by 106
Metadata
- Authors
- Chen, W., Young, L. J., Lu, M., Zaccone, A., Ströhl, F., Yu, N., Kaminski Schierle, G. S., & Kaminski, C. F.
- Venue
- Nano Letters
- Publisher
- American Chemical Society (ACS)
- Published
- 2016-11-30
- Volume
- 17
- Issue
- 1
- Pages
- 143-149
- ISSN
- 1530-6984
- 1530-6992
- PMC
- PMC5338000
- Cited by
- 85
- References
- 5
- Language
- en
- Funders
- Wellcome Trust (NA)
- Medical Research Council (NA)
- Engineering and Physical Sciences Research Council (NA)
- Biotechnology and Biological Sciences Research Council (NA)
- Alzheimer’s Research UK (NA)
- Cambridge Commonwealth, European and International Trust (NA)
- China Scholarship Council (NA)
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- CoChat. (2026). Citation check: Fluorescence Self-Quenching from Reporter Dyes Informs on the Structural Properties of Amyloid Clusters Formed in Vitro and in Cells. https://app.cochat.ai/papers/10.1021/acs.nanolett.6b03686
- The paper
- Chen, W., Young, L. J., Lu, M., Zaccone, A., Ströhl, F., Yu, N., Kaminski Schierle, G. S., & Kaminski, C. F. (2017). Fluorescence Self-Quenching from Reporter Dyes Informs on the Structural Properties of Amyloid Clusters Formed in Vitro and in Cells. Nano Letters. https://doi.org/10.1021/acs.nanolett.6b03686
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