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Single-molecule studies of amyloid proteins: from biophysical properties to diagnostic perspectives

Published online by Cambridge University Press:  05 November 2020

Jinming Wu ,
Chan Cao ,
Rolf Antonie Loch ,
Ann Tiiman  and
Jinghui Luo Open the ORCID record for Jinghui Luo [Opens in a new window]
Jinming Wu
Affiliation:
Department of Biology and Chemistry, Paul Scherrer Institute, 5232, Villigen, Switzerland
Chan Cao
Affiliation:
Institute of Bioengineering, School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL), 1015, Lausanne, Switzerland Swiss Institute of Bioinformatics (SIB), 1015, Lausanne, Switzerland
Rolf Antonie Loch
Affiliation:
Department of Biology and Chemistry, Paul Scherrer Institute, 5232, Villigen, Switzerland
Ann Tiiman
Affiliation:
Department of Clinical Neuroscience (CNS), Center for Molecular Medicine CMM L8:01, Karolinska Institutet, 17176, Stockholm, Sweden
Jinghui Luo*
Affiliation:
Department of Biology and Chemistry, Paul Scherrer Institute, 5232, Villigen, Switzerland
*
Author for correspondence: Jinghui Luo, E-mail: [email protected]
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Abstract

In neurodegenerative diseases, a wide range of amyloid proteins or peptides such as amyloid-beta and α-synuclein fail to keep native functional conformations, followed by misfolding and self-assembling into a diverse array of aggregates. The aggregates further exert toxicity leading to the dysfunction, degeneration and loss of cells in the affected organs. Due to the disordered structure of the amyloid proteins, endogenous molecules, such as lipids, are prone to interact with amyloid proteins at a low concentration and influence amyloid cytotoxicity. The heterogeneity of amyloid proteinscomplicates the understanding of the amyloid cytotoxicity when relying only on conventional bulk and ensemble techniques. As complementary tools, single-molecule techniques (SMTs) provide novel insights into the different subpopulations of a heterogeneous amyloid mixture as well as the cytotoxicity, in particular as involved in lipid membranes. This review focuses on the recent advances of a series of SMTs, including single-molecule fluorescence imaging, single-molecule force spectroscopy and single-nanopore electrical recording, for the understanding of the amyloid molecular mechanism. The working principles, benefits and limitations of each technique are discussed and compared in amyloid protein related studies.. We also discuss why SMTs show great potential and are worthy of further investigation with feasibility studies as diagnostic tools of neurodegenerative diseases and which limitations are to be addressed.

Keywords

Amyloid proteinsingle-molecule techniquessingle-molecule fluorescence imagingsingle-molecule force spectroscopysingle-nanopore electrical recordingneurodegenerative diseases
Type
Review
Information
Quarterly Reviews of Biophysics , Volume 53 , 2020 , e12
Copyright
Copyright © The Author(s) 2020. Published by Cambridge University Press

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