title: Freezing of a fish antifreeze protein results in amyloid fibril formation.
abstract: Amyloid is associated with a number of diseases including Alzheimer's, Huntington's, Parkinson's, and the spongiform encephalopathies. Amyloid fibrils have been formed in vitro from both disease and nondisease related proteins, but the latter requires extremes of pH, heat, or the presence of a chaotropic agent. We show, using fluorescence spectroscopy, electron microscopy, and solid-state NMR spectroscopy, that the alpha-helical type I antifreeze protein from the winter flounder forms amyloid fibrils at pH 4 and 7 upon freezing and thawing. Our results demonstrate that the freezing of some proteins may accelerate the formation of amyloid fibrils.
authors.affiliation: Canadian Institute of Health Research Group in Protein Structure and Function, Department of Biochemistry and Protein Engineering Network of Centres of Excellence, University of Alberta, Edmonton, T6G 2H7 Canada.
authors.forename: Steffen P
authors.initials: SP
authors.lastname: Graether
authors.forename: Carolyn M
authors.initials: CM
authors.lastname: Slupsky
authors.forename: Brian D
authors.initials: BD
authors.lastname: Sykes
mesh_terms: D016229:Amyloid beta-Peptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure*; D000818:Animals; D021301:Antifreeze Proteins / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D021322:Antifreeze Proteins, Type I / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure*; D005432:Flounder / Q000378:metabolism; D005615:Freezing; D006863:Hydrogen-Ion Concentration; D008854:Microscopy, Electron; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D013050:Spectrometry, Fluorescence; D013696:Temperature
chemical_list: D016229:Amyloid beta-Peptides; D021301:Antifreeze Proteins; D021322:Antifreeze Proteins, Type I