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The molecular lifecycle of amyloid – Mechanism of assembly, mesoscopic organisation, polymorphism, suprastructures, and biological consequences

Lutter, Liisa, Serpell, Christopher J., Tuite, Mick F., Xue, Wei-Feng (2019) The molecular lifecycle of amyloid – Mechanism of assembly, mesoscopic organisation, polymorphism, suprastructures, and biological consequences. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 1867 (11). p. 140257. ISSN 1570-9639. (doi:10.1016/j.bbapap.2019.07.010) (Access to this publication is currently restricted. You may be able to access a copy if URLs are provided)

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Abstract

The formation of a diverse range of amyloid structures from normally soluble proteins and peptides is a hallmark of devastating human disorders as well as biological functions. The current molecular understanding of the amyloid lifecycle reveals four processes central to their growth and propagation: primary nucleation, elongation, secondary nucleation and division. However, these processes result in a wide range of cross-β packing and filament arrangements, including diverse assemblies formed from identical monomeric precursors with the same amino acid sequences. Here, we review current structural and mechanistic understanding of amyloid self-assembly, and discuss how mesoscopic, i.e. micrometre to nanometre, organisation of amyloid give rise to suprastructural features that may be the key link between the polymorphic amyloid structures and the biological response they elicit. A greater understanding of the mechanisms governing suprastructure formation will guide future strategies to combat amyloid associated disorders and to use and control the amyloid quaternary structure in synthetic biology and materials applications.

Item Type: Article
DOI/Identification number: 10.1016/j.bbapap.2019.07.010
Uncontrolled keywords: amyloid; prions; polymorphism; suprastructure; self-assembly
Subjects: Q Science
Q Science > QD Chemistry > QD431 Organic Chemistry- Biochemistry- Proteins, peptides, amino acids
Divisions: Faculties > Sciences > School of Biosciences > Protein Science Group
Depositing User: Wei-Feng Xue
Date Deposited: 20 Aug 2019 12:38 UTC
Last Modified: 01 Oct 2019 10:35 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/75899 (The current URI for this page, for reference purposes)
Serpell, Christopher J.: https://orcid.org/0000-0002-2848-9077
Tuite, Mick F.: https://orcid.org/0000-0002-5214-540X
Xue, Wei-Feng: https://orcid.org/0000-0002-6504-0404
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