Department: Integrative Biology

Education: Honours BSc. Wildlife Biology, Fourth Year

Research: Investigating the role of keratin matrix proteins in modulating the hydration state and mechanics of intermediate filaments in hard alpha-keratin structures.

Intermediate filaments were thought to be inherently hydrophobic, however past work has shown that hagfish threads (pure intermediate filament threads) are very soft and extensible in water. If you dry a hagfish thread, the story changes: it becomes very stiff and similar to keratin structures like wool. Hard alpha-keratins are also composed of intermediate filaments, albeit they are embedded in a matrix of globular proteins. These structures retain much of their mechanical properties in water. Thus, the question arises of why do hagfish threads become soft while keratins do not?

Hard alpha-keratin structures take on a diverse variety of forms and functions, yet all alpha-keratins are composed of the same constituent proteins. Thus, what I hope to better understand is how the proportion of specific proteins in a given keratin structure alters its mechanics and thus function. As well, the role of other factors such as calcification (as has been shown in whale baleen) and covalent cross-linking of intermediate filaments could be substantial. Elucidating how all these factors come into play could advance the biomimetic model for hagfish threads.

Contact: greenbed@uoguelph.ca