The relationship between amyloid structure and cytotoxicity

Marshall, Karen E, Marchante, Ricardo, Xue, Wei-Feng and Serpell, Louise C (2014) The relationship between amyloid structure and cytotoxicity. Prion, 8 (2). pp. 5-4. ISSN 1933-6896

[img]
Preview
PDF (This is a Gold OA article. Please ignore Landes Bioscience watermark which is incorrect) - Published Version
Available under License Creative Commons Attribution.

Download (1MB) | Preview

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 amyloid systems 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
Schools and Departments: School of Life Sciences > Biochemistry
Subjects: Q Science > QD Chemistry > QD0241 Organic chemistry > QD0415 Biochemistry
Depositing User: Catrina Hey
Date Deposited: 11 Sep 2014 13:24
Last Modified: 18 Mar 2017 17:35
URI: http://sro.sussex.ac.uk/id/eprint/49897

View download statistics for this item

📧 Request an update