The relationship between amyloid structure and cytotoxicity.

Marshall, Karen E and Marchante, Ricardo and Xue, Wei-Feng and Serpell, Louise C (2014) The relationship between amyloid structure and cytotoxicity. Prion, 8 (2). pp. 192-196. ISSN 1933-690X. (doi:https://doi.org/10.4161/pri.28860) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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Official URL
http://dx.doi.org/10.4161/pri.28860

Abstract

Self-assembly of proteins and peptides into amyloid structures has been the subject of intense and focused research due to their association with neurodegenerative, age-related human diseases and transmissible prion diseases in humans and mammals. Of the disease associated amyloid assemblies, a diverse array of species, ranging from small oligomeric assembly intermediates to fibrillar structures, have been shown to have toxic potential. Equally, a range of species formed by the same disease associated amyloid sequences have been found to be relatively benign under comparable monomer equivalent concentrations and conditions. In recent years, an increasing number of functional amyloids have also been found. These developments show that not all amyloid structures are generically toxic to cells. Given these observations, it is important to understand why amyloid structures may encode such varied toxic potential despite sharing a common core molecular architecture. Here, we discuss possible links between different aspects of amyloidogenic structures and assembly mechanisms with their varied functional effects. We propose testable hypotheses for the relationship between amyloid structure and its toxic potential in the context of recent reports on amyloid sequence, structure, and toxicity relationships.

Item Type: Article
Subjects: Q Science > QC Physics
Q Science > QD Chemistry
Q Science > QP Physiology (Living systems) > QP517 Biochemistry
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Wei-Feng Xue
Date Deposited: 30 Jul 2014 16:10 UTC
Last Modified: 06 May 2015 09:16 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/42039 (The current URI for this page, for reference purposes)
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