Marshall2014PRION0007R.pdf (1.31 MB)
The relationship between amyloid structure and cytotoxicity
journal contribution
posted on 2023-06-08, 18:16 authored by Karen MarshallKaren Marshall, Ricardo Marchante, Wei-Feng Xue, Louise SerpellLouise SerpellSelf-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.
History
Publication status
- Published
File Version
- Published version
Journal
PrionISSN
1933-6896Publisher
Landes BioscienceExternal DOI
Issue
2Volume
8Page range
5-4Department affiliated with
- Biochemistry Publications
Full text available
- Yes
Peer reviewed?
- Yes
Legacy Posted Date
2014-09-11First Open Access (FOA) Date
2014-09-11First Compliant Deposit (FCD) Date
2014-09-11Usage metrics
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