title: Are amyloid fibrils molecular spandrels?
abstract: Amyloid-β, the protein implicated in Alzheimer's disease, along with a number of other proteins, has been shown to form amyloid fibrils. Fibril forming proteins share no common primary structure and have little known function. Furthermore, all proteins have the ability to form amyloid fibrils under certain conditions as the fibrillar structure lies at the global free energy minimum of proteins. This raises the question of the mechanism of the evolution of the amyloid fibril structure. Experimental evidence supports the hypothesis that the fibril structure is a by-product of the forces of protein folding and lies outside the bounds of evolutionary pressures.
authors.affiliation: Department of Biology, University of Waterloo, Waterloo, ON, Canada. Electronic address: fthane@uwaterloo.ca.
authors.forename: Francis
authors.initials: F
authors.lastname: Hane
mesh_terms: D000682:Amyloid / Q000737:chemistry / Q000235:genetics*; D019143:Evolution, Molecular; D006801:Humans; D017510:Protein Folding; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary
chemical_list: D000682:Amyloid
keywords: Amyloid; Protein evolution