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Putting Proteins to Work

Antifreeze proteins (AFPs) have the remarkable ability to bind to ice to control, and even stop, its growth. They are used by freeze-resistant organisms like fish and insects to lower their freezing point, and by freeze-tolerant organisms, such as plants and bacteria, to lessen freezing damage by inhibiting ice recrystallization. They also have a potential use in preserving frozen tissues, and preventing the freezing of other biological materials like organs, cells, and crops.

Dr. Peter L. Davies, Canada Research Chair in Protein Engineering, is studying the relationship between antifreeze, ice nucleation, and ice adhesion proteins that appear to use the same mechanism to achieve different goals. He hopes to design and make inexpensive biological antifreezes that could be superior to natural proteins for various biotechnological applications.

Davies and his research team are studying the structure, function, and mechanism of calpains, which are intracellular Ca2+ dependent cysteine proteases that mediate Ca2+ signaling. Their job is to cut specific proteins where there is a local burst of Ca2+ released into the cell. When Ca2+ levels go out of control after a stroke, heart attack, or during neurodegeneration, calpain hyperactivity causes widespread tissue damage. For this reason, gaining a better understanding of calpains is important for drug design.

Davies' vision is that we will become so good at understanding the relationship between the structure and function of proteins that we will be able to design proteins for specific purposes in the future, and realize the full potential of protein engineering.