Ice-binding proteins (IBPs) offer protection against freezing to sustain life at subzero temperatures in ice-laden environments. How IBPs work exactly is not yet known, but it is clear that their activity is closely related to the way in which IBPs interact with ice. Recently, we adopted sub-zero nanoscopy to study for the first time the interfacial dynamics of ice-bound IBPs at the single molecule level (see preprint
for more information). These pioneering experiments offer unprecedented insight in the structure-activity relations of IBPs. In this project you will use subzero nanoscopy to study the interaction with ice of biological IBPs and (de novo) designed ice-binders at the single molecule level aiming to better understand how biological and (bio)synthetic antifreezes block ice growth, shape ice crystals, inhibit ice recrystallization and control ice nucleation. You will work in close collaboration with other group members, who design and prepare biological and (bio)synthetic IBPs and explore their application potential in cardiomyocyte preservation. Our aim is to unravel how biological and engineered ice-binders function and to customize these cryoprotectants for biomedical and other applications.