期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 61, 期 10, 页码 -出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202112832
关键词
Amyloid; Fluorescence; Oligomers; Sensor; Super-resolution
资金
- Australian Research Council [DE210101176]
- University of Sydney Fellowship [CE200100012, DP180101353, DP200102463]
- Research Training Program Scholarship from the Australian Government (Department of Education, Skills and Employment)
- Australian Research Council [DE210101176] Funding Source: Australian Research Council
In this study, the researchers developed a fluorescent amyloid sensor called AmyBlink-1 and used it for super-resolution imaging of amyloid structures. They were able to achieve nanoscale imaging of different types of amyloid fibrils and quantify their morphological features.
Many soluble proteins can self-assemble into macromolecular structures called amyloids, a subset of which are implicated in a range of neurodegenerative disorders. The nanoscale size and structural heterogeneity of prefibrillar and early aggregates, as well as mature amyloid fibrils, pose significant challenges for the quantification of amyloid morphologies. We report a fluorescent amyloid sensor AmyBlink-1 and its application in super-resolution imaging of amyloid structures. AmyBlink-1 exhibits a 5-fold increase in ratio of the green (thioflavin T) to red (Alexa Fluor 647) emission intensities upon interaction with amyloid fibrils. Using AmyBlink-1, we performed nanoscale imaging of four different types of amyloid fibrils, achieving a resolution of approximate to 30 nm. AmyBlink-1 enables nanoscale visualization and subsequent quantification of morphological features, such as the length and skew of individual amyloid aggregates formed at different times along the amyloid assembly pathway.
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