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

DOI	Resolve DOI: https://doi.org/10.1002/1873-3468.12175
Author	Search for: Dubé, André; Search for: Leggiadro, Cindy¹; Search for: Ewart, Kathryn Vanya
Name affiliation	National Research Council Canada. Aquatic and Crop Resource Development
Format	Text
Type	Article
Journal title	FEBS Letters
ISSN	0014-5793 1873-3468
Volume	590
Issue	9
Pages	1335–1344
Subject	amyloid; 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	2017-04-27
Publisher	Wiley
Language	English
Peer reviewed	Yes
NPARC number	23001953
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Record identifier	4228be85-72d0-448a-8ed4-0a22bfd2070e
Record created	2017-06-28
Record modified	2020-03-16