title: Structure-activity relationship of amyloid fibrils.
abstract: 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-beta-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-beta-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.
authors: School of Bioscience and Bioengineering, IIT-Bombay, Powai, Mumbai, India. samirmaji@iitb.ac.in
authors: Samir K
authors: SK
authors: Maji
authors: Lei
authors: L
authors: Wang
authors: Jason
authors: J
authors: Greenwald
authors: Roland
authors: R
authors: Riek
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D018360:Crystallography, X-Ray; D006801:Humans; D019636:Neurodegenerative Diseases / Q000378:metabolism*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship
chemical_list: D000682:Amyloid