Visualizing and trapping transient oligomers in amyloid assembly pathways.

Biophysical Chemistry
Emma E CawoodSheena E Radford

Abstract

Oligomers which form during amyloid fibril assembly are considered to be key contributors towards amyloid disease. However, understanding how such intermediates form, their structure, and mechanisms of toxicity presents significant challenges due to their transient and heterogeneous nature. Here, we discuss two different strategies for addressing these challenges: use of (1) methods capable of detecting lowly-populated species within complex mixtures, such as NMR, single particle methods (including fluorescence and force spectroscopy), and mass spectrometry; and (2) chemical and biological tools to bias the amyloid energy landscape towards specific oligomeric states. While the former methods are well suited to following the kinetics of amyloid assembly and obtaining low-resolution structural information, the latter are capable of producing oligomer samples for high-resolution structural studies and inferring structure-toxicity relationships. Together, these different approaches should enable a clearer picture to be gained of the nature and role of oligomeric intermediates in amyloid formation and disease.

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Citations

Jan 20, 2021·The Journal of Physical Chemistry. B·Gregory-Neal Gomes, Zachary A Levine
Feb 19, 2021·Chemistry and Physics of Lipids·Michael OverduinDavid Westaway
May 22, 2021·The Journal of Biological Chemistry·Camilla B AndersenFrans A A Mulder
Jun 22, 2021·Current Opinion in Structural Biology·Sara Linse
Jun 8, 2021·Physical Biology·Jules MorandPatrícia F N Faísca
Aug 11, 2021·Chemistry and Physics of Lipids·Ayyalusamy Ramamoorthy
Aug 28, 2021·Chemical Reviews·Jack L BennettWilliam A Donald
Aug 31, 2021·Materials Advances·Kyabeth M TorresRolando Oyola

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