Rapid amyloid fibril formation by a winter flounder antifreeze protein requires specific interaction with ice

From National Research Council Canada

DOIResolve DOI: https://doi.org/10.1002/1873-3468.12175
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Name affiliation
  1. National Research Council Canada. Aquatic and Crop Resource Development
FormatText
TypeArticle
Journal titleFEBS Letters
ISSN0014-5793
1873-3468
Volume590
Issue9
Pages1335–1344
Subjectamyloid; antifreeze protein; ice; Pseudopleuronectes americanus; winter flounder
Abstract
A typically α-helical antifreeze protein (wflAFP-6) from winter flounder, Pseudopleuronectes americanus, forms amyloid fibrils during freezing. In this study, the effects of distinct components of the freezing process were examined. Freezing of wflAFP-6 in the presence of template ice was shown to be necessary for rapid conversion to an amyloid conformation. Neither subfreezing temperature nor phase change was sufficient. Thus, specific interaction with the ice surface was essential. The ice-induced formation of amyloid appeared to be unique to this helical antifreeze, it required high concentrations of protein and it occurred over a range of pH values. These results define a method for rapid formation of amyloid by wflAFP-6 on demand under physiological conditions.
Publication date
PublisherWiley
Terms of use
LanguageEnglish
Peer reviewedYes
NPARC number23001953
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Record identifier4228be85-72d0-448a-8ed4-0a22bfd2070e
Record created2017-06-28
Record modified2017-06-28
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