Putting bacteria to work
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“In the chemical biology laboratory at TU/e, we use bacteria to produce ice-binding proteins for us. This way, we don’t have to isolate them from ice fish for our research. That’s not only better for the ice fish, but also useful for us, because it allows us to tinker with the protein structure very precisely in order to find out which parts are essential for the function of the proteins.”
Together with colleagues at Wageningen University & Research and Washington University, they used AI to computationally design proteins that did not yet exist, with the desired properties. Using E. coli bacteria, they produce these artificial proteins in the lab. Voets and her TU/e colleagues then study how the proteins interact with ice crystals under different circumstances.
New family of artificially designed proteins
In a recent paper in PNAS , the joint team presents an entirely new family of artificially designed proteins that is more stable, more active, and more versatile than the ice-binding proteins that exist in nature, Voets explains. “Naturally occurring ice-binding proteins are generally only found in cold environments. Some of these proteins already lose their characteristic folding and thus their ability to bind ice at room temperature. The new class of proteins we developed remains stable in a much wider temperature range.”
That is very useful for practical applications, stresses Voets. “Imagine that you would want to add such proteins to human organs to freeze them for storage. The fact that these proteins don’t need to be kept at low temperatures to remain functional makes the handling a lot easier, as you do not need special cooling equipment or expertise.”
Converging developments
According to Voets, this important breakthrough was not only the result of hard work and determination, but also of perfect timing: “Several developments are now converging”, she explains. “There has been huge progress in computational methods for designing these proteins. At the same time, the world’s most powerful super-resolved fluorescence microscopes are available at the ICMS Advanced Microscopy Facility (AMF) , allowing us to track individual proteins on ice for the first time. On top of that, interdisciplinary collaborations with biomedical engineers at the Institute for Complex Molecular Systems , cardiologists at Utrecht University Medical Center, and transplant surgeons at University Medical Center Groningen have been essential.”
Next step toward societal impact
One of the contributing TU/e researchers is postdoc Tim Hogervorst from the Self-Organizing Soft Matter group . He discovered that the essential properties of these proteins can also be transferred to polymer-based materials, enabling scalable, cost-efficient production. In collaboration with The Gate , Voets and Hogervorst are now taking the next step toward societal impact by investigating how this discovery can be transformed into a practical, real-world product, available for others to use.
The €150.000 Proof of Concept grant Voets recently received from the European Research Council will definitely help her achieve that goal. And should open the way for the pragmatic use of her new antifreeze materials, marking a critical step toward the long-term goal of high-quality preservation of tissue and organs.
date:2026-02-09 14:18:00