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Fibril fragmentation in amyloid assembly and cytotoxicity: When size matters

Xue, Wei-Feng, Hellewell, Andrew L., Hewitt, Eric W., Radford, Sheena E. (2010) Fibril fragmentation in amyloid assembly and cytotoxicity: When size matters. Prion, 4 (1). pp. 20-25. ISSN 1933-6896. (doi:10.4161/pri.4.1.11378) (KAR id:31455)


Amyloid assemblies are associated with several debilitating human disorders. Understanding the intra- and extracellular assembly of normally soluble proteins and peptides into amyloid aggregates and how they disrupt normal cellular functions is therefore of paramount importance. In a recent report, we demonstrated a striking relationship between reduced fibril length caused by fibril fragmentation and enhanced ability of fibril samples to disrupt membranes and to reduce cell viability. These findings have important implications for our understanding of amyloid disease in that changes in the physical dimensions of fibrils, without parallel changes in their composition or molecular architecture, could be sufficient to alter the biological responses to their presence. These conclusions provide a new hypothesis that the physical dimensions and surface interactions of fibrils play key roles in amyloid disease. Controlling fibril length and stability toward fracturing, and thereby the biological availability of fibril material, may provide a new target for future therapeutic strategies towards combating amyloid disease

Item Type: Article
DOI/Identification number: 10.4161/pri.4.1.11378
Subjects: Q Science
Q Science > QD Chemistry
Q Science > QP Physiology (Living systems) > QP517 Biochemistry
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Wei-Feng Xue
Date Deposited: 09 Oct 2012 14:51 UTC
Last Modified: 16 Nov 2021 10:09 UTC
Resource URI: (The current URI for this page, for reference purposes)

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