Ice-Binding Proteins: Nature’s Nanotools for Ice Control

Ido Braslavsky

Living organisms across diverse environments have evolved ice-binding proteins (IBPs) to manage the challenges of freezing temperatures. These proteins regulate ice formation through two distinct mechanisms: antifreeze proteins (AFPs) inhibit ice growth, preventing freezing in supercooled organisms, while ice nucleation proteins (INPs) promote ice formation, aiding bacterial colonization and potentially influencing weather patterns.

The molecular basis of the IBP function involves precise interactions with ice through the manipulation of hydration layers, forming an ice-like network that binds to the crystal surface. The key difference between AFPs and INPs lies in their size—AFPs are nanometric and disrupt ice growth, whereas INPs must be large and aggregated to nucleate ice efficiently. Our findings demonstrate that AFPs can paradoxically enhance nucleation at small scales, while INPs require cooperative assembly for maximal efficiency. Furthermore, we explore whether small peptides can self-assemble into functional IBPs, revealing new pathways for ice control using minimal molecular units.

By deciphering nature’s strategies for ice regulation, we open up new possibilities for technological applications in food science, agriculture, cryopreservation, and climate change mitigation.