title: Chimera-induced folding: implications for amyloidosis.
abstract: The discoveries that non-native proteins have a role in amyloidosis and that multiple protein misfolding diseases can occur concurrently suggest that cross-seeding of amyloidogenic proteins may be central to misfolding. To study this process, a synthetic chimeric amyloidogenic protein (YEHK21-YE8) composed of two components, one that readily folds to form fibrils (YEHK21) and one that does not (YE8), was designed. Secondary structural conformational changes during YEHK21-YE8 aggregation demonstrate that, under the appropriate conditions, YEHK21 is able to induce fibril formation of YE8. The unambiguous demonstration of the induction of folding and fibrillation within a single molecule illuminates the factors controlling this process and hence suggests the importance of those factors in amyloidogenic diseases.
authors.affiliation: Department of Chemistry and §Department of Biological Sciences, University at Albany, State University of New York , Albany, New York 12222, United States.
authors.forename: Gaius A
authors.initials: GA
authors.lastname: Takor
authors.forename: Seiichiro
authors.initials: S
authors.lastname: Higashiya
authors.forename: Mirco
authors.initials: M
authors.lastname: Sorci
authors.forename: Natalya I
authors.initials: NI
authors.lastname: Topilina
authors.forename: Georges
authors.initials: G
authors.lastname: Belfort
authors.forename: John T
authors.initials: JT
authors.lastname: Welch
mesh_terms: D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism; D000686:Amyloidosis; D006801:Humans; D017510:Protein Folding; D011993:Recombinant Fusion Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D000682:Amyloid; D011993:Recombinant Fusion Proteins