The researchers created synthetic ice-binding proteins (antifreeze proteins) inspired by the antifreeze proteins in the blood of Arctic icefish (picture from Wikipedia).
Professor Ilja Voets from the Eindhoven University of Technology (TU/e) is making significant strides in the use of antifreeze proteins to prevent freezing damage to biological systems, with the long-term goal of extending donor organ preservation for life-saving transplants.
Freezing biological material pauses metabolism and enables long-term storage, but ice crystals formed during the process rupture cells and destroy tissue upon thawing. Voets draws inspiration from Arctic icefish, whose blood contains small ice-binding proteins that inhibit ice crystal growth. These proteins adhere to ice surfaces, creating a curved ice-water interface that slows further crystallization — keeping ice crystals small enough for blood to keep flowing.
Rather than isolating proteins from fish, Voets' lab uses E. coli bacteria to produce both natural and computationally designed proteins. In a recent PNAS publication, her team — in collaboration with Wageningen University & Research and Washington University — introduced an entirely new family of artificially designed ice-binding proteins that are more stable, more active, and functional across a wider temperature range than their natural counterparts. This thermal stability is particularly valuable for practical use, as it removes the need for specialized cooling during handling.
A key next step came from postdoc Tim Hogervorst, who showed that the essential properties of these proteins can be transferred to polymer-based materials, enabling scalable and cost-efficient production. Supported by an ERC Proof of Concept grant of €150,000, Voets and her team are now working to translate this discovery into a real-world product for tissue and organ preservation.
Bron: TU/e