Structural characterization of amyloidotic antifreeze protein fibrils and intermediates

Abstract

The propagation and detrimental effects of prion disease are thought to be associated with the amyloid-like prion fibrils or with other misfolded structures known as beta-oligomers. The freezing and thawing of high concentrations of an antifreeze protein result in fibrils that have morphological and structural properties similar to those of amyloid. The method to produce these amyloid-like fibrils is expanded upon in this study. Data showed that the C-terminal end of the protein retains its alpha-helical character even in the amyloid state, and that changing the pH of the protein solution from 4 to 8 resulted in gels that resemble the beta-oligomeric form. These interim results provide the conditions for further elucidating the structure of these fibrils and their intermediate states.