Investigation of Antifreeze Protein Activity in Blue Mussels and Amyloid-Like Transition in a Predominant Winter Flounder Serum Antifreeze Protein
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The study of marine antifreeze proteins has provided new findings. The blue mussel (Mytilus edulis) was known to have antifreeze activity; however, the antifreeze protein or other molecule responsible has never been characterized. Activity was evident in mussels from each of the Maritime provinces, Canada. The antifreeze molecule was shown to alter ice crystal morphology. It functioned over a wide range of pH values and it showed protease resistance. Nonetheless, its purification was not achieved. A winter flounder (Pseudopleuronectes americanus) ?-helical antifreeze protein, wflAFP6, has been shown to form amyloid-like fibrils during freezing. Separation of different aspects of the freezing process demonstrated that equilibrium freezing with an ice template is necessary for conversion of the wflAFP6 to the amyloid-like conformation. Amyloid-like conformation was determined by dye binding and electron microscopy. The effects of wflAFP6 concentration and solution properties were determined in order to better understand the process of conversion.