Monitoring α-synuclein aggregation.

Estaun-Panzano J(1), Arotcarena ML(1), Bezard E(2).

Author information:
(1)Univ. Bordeaux, CNRS, IMN, UMR 5293, F-33000 Bordeaux, France.
(2)Univ. Bordeaux, CNRS, IMN, UMR 5293, F-33000 Bordeaux, France; Motac Neuroscience Ltd, Manchester, United Kingdom. Electronic address: .

Synucleinopathies, including Parkinson’s disease (PD), dementia with Lewy Bodies (DLB), and multiple system atrophy (MSA), are characterized by the misfolding and subsequent aggregation of alpha-synuclein (α-syn) that accumulates in cytoplasmic inclusions bodies in the cells of affected brain regions. Since the seminal report of likely-aggregated α-syn presence within the Lewy bodies by Spillantini et al. in 1997, the keyword « synuclein aggregation » has appeared in over 6000 papers (Source: PubMed October 2022). Studying, observing, describing, and quantifying α-syn aggregation is therefore of paramount importance, whether it happens in tubo, in vitro, in post-mortem samples, or in vivo. The past few years have witnessed tremendous progress in understanding aggregation mechanisms and identifying various polymorphs. In this context of growing complexity, it is of utmost importance to understand what tools we possess, what exact information they provide, and in what context they may be applied. Nonetheless, it is also crucial to rationalize the relevance of the information and the limitations of these methods for gauging the final result. In this review, we present the main techniques that have shaped the current views about α-syn structure and dynamics, with particular emphasis on the recent breakthroughs that may change our understanding of synucleinopathies.

Copyright © 2022 The Authors. Published by Elsevier Inc. All rights reserved.

Conflict of interest statement: Declaration of Competing Interest EB is a director and shareholder of Motac Neuroscience Ltd. The other authors declare no conflict of interest.

Auteurs Bordeaux Neurocampus