title: Formation of amyloid fibrils from β-amylase.
abstract: Fibril formation has been considered a significant feature of amyloid proteins. However, it has been proposed that fibril formation is a common property of many proteins under appropriate conditions. We studied the fibril formation of β-amylase, a non-amyloid protein rich in α-helical structure, because the secondary structure of β-amylase is similar to that of prions. With the conditions for the fibril formation of prions, β-amylase proteins were converted into amyloid fibrils. The features of β-amylase proteins and fibrils are compared to prion proteins and fibrils. Furthermore, the cause of neurotoxicity in amyloid diseases is discussed.
authors.affiliation: Department of Life Science, National Chung Cheng University, Ming-Hsiung, Chia-Yi, Taiwan.
authors.forename: Jian-Chau
authors.initials: JC
authors.lastname: Luo
authors.forename: Shing-Chuen
authors.initials: SC
authors.lastname: Wang
authors.forename: Wei-Bang
authors.initials: WB
authors.lastname: Jian
authors.forename: Chien-Hsing
authors.initials: CH
authors.lastname: Chen
authors.forename: Jaw-Luen
authors.initials: JL
authors.lastname: Tang
authors.forename: Cheng-I
authors.initials: CI
authors.lastname: Lee
mesh_terms: D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure; D000818:Animals; D002942:Circular Dichroism; D004795:Enzyme Stability; D006801:Humans; D017096:Prion Diseases / Q000473:pathology; D011328:Prions / Q000737:chemistry / Q000378:metabolism; D017433:Protein Structure, Secondary; D001614:beta-Amylase / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D000682:Amyloid; D011328:Prions; D001614:beta-Amylase