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Structure–activity relationship of amyloid fibrils
Author(s) -
Maji Samir K.,
Wang Lei,
Greenwald Jason,
Riek Roland
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.07.003
Subject(s) - fibril , cooperativity , amyloid fibril , amyloid (mycology) , beta sheet , biophysics , chemistry , protein aggregation , amyloid disease , protein structure , amyloid β , biology , biochemistry , disease , medicine , pathology , inorganic chemistry
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.