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Rapid amyloid fibril formation by a winter flounder antifreeze protein requires specific interaction with ice
Author(s) -
Dubé André,
Leggiadro Cindy,
Ewart Kathryn Vanya
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12175
Subject(s) - winter flounder , antifreeze protein , antifreeze , ice formation , chemistry , amyloid (mycology) , amyloid fibril , biophysics , ice crystals , flounder , biochemistry , biology , fish <actinopterygii> , amyloid β , geology , fishery , organic chemistry , medicine , meteorology , inorganic chemistry , physics , disease , atmospheric sciences
A typically α‐helical antifreeze protein (wfl AFP ‐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 wfl AFP ‐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 wfl AFP ‐6 on demand under physiological conditions.