Structure–activity relationship of amyloid fibrils

Protein aggregation is a process in which proteins self-associate into imperfectly ordered macroscopic entities. Such aggregates are generally classified as either amorphous or highly ordered, the most common form of the latter being amyloid fibrils. Amyloid fibrils composed of cross-β-sheet structu...

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Bibliographic Details
Published in:FEBS letters 2009-08, Vol.583 (16), p.2610-2617
Main Authors: Maji, Samir K., Wang, Lei, Greenwald, Jason, Riek, Roland
Format: Article
Language:English
Subjects:
Aggregation
Alzheimer's disease
Amyloid
Amyloid - chemistry
circular dichroism
Crystallography, X-Ray
electron microscope
electron paramagnetic resonance
EPR
Fibril
Humans
IAPP
islet amyloid polypeptide
Neurodegenerative Diseases - metabolism
NMR
Nuclear magnetic resonance
Nuclear Magnetic Resonance, Biomolecular - methods
Protein
Protein Structure, Secondary
Structure-Activity Relationship
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Summary:Protein aggregation is a process in which proteins self-associate into imperfectly ordered macroscopic entities. Such aggregates are generally classified as either amorphous or highly ordered, the most common form of the latter being amyloid fibrils. Amyloid fibrils composed of cross-β-sheet structure are the pathological hallmarks of several diseases including Alzheimer’s disease, but are also associated with functional states such as the fungal HET-s prion. This review aims to summarize the recent high-resolution structural studies of amyloid fibrils in light of their (potential) activities. We propose that the repetitive nature of the cross-β-sheet structure of amyloids is key for their multiple properties: the repeating motifs can translate a rather non-specific interaction into a specific one through cooperativity.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2009.07.003