IceBinders: artificial antifreeze proteins
Some organisms have the capacity to survive at sub-zero temperatures thanks to unique proteins that selectively bind to ice crystals. Wageningen University and Eindhoven University of Technology have collaboratively designed artificial versions of such ice-binding proteins that can prevent the growth of large ice crystals. Together, WUR and TU/e are looking for partners to realize valuable applications for this new technology.
Upon freezing and thawing, ice crystals can cause a lot of cellular damage to biological tissues. It has been proven in proof-of-concept studies that ice-binding proteins can protect cells against some forms of freezing damage. The designed ice-binding proteins are thermostable and can be produced in bioreactors using suitable host microorganisms such as E. coli.
What makes our system unique?
- Computationally designed artificial ice-binding proteins
- High thermal stability and high activity
- Can be produced efficiently through a biotechnological process
- Patented technolog
High-potential applications
- Organ and tissue transport and preservation
- Preservation of live cells (e.g. cell cultures for research, CarT cells, cells for IVF)
- Preventing freeze damage in frozen food
Development stage & collaboration opportunities
The technology is at TRL3/TRL 4 and protected by IP. The proteins have been produced at lab scale. Proof-of-concept cryopreservation studies have been performed using live cells. Wageningen University & Research and TU/e are actively taking steps to work on further product development.
Interested? Get in touch with:
Contact
Questions? Reach out to:
dr. N (Nikita) Sajeev
Publications & Patents
- de Haas, R. J., de Vries, R., Tas, R., Voets, I. (2024). Improved ice-binding proteins based on twist constrained helices. (Patent No. WO2024076237A1).
- de Haas, R. J., Tas, R. P., van den Broek, D., Zheng, C., Nguyen, H., Kang, A., Bera, A. K., King, N. P., Voets, I. K., & de Vries, R. (2023). De novo designed ice-binding proteins from twist-constrained helices. Proceedings of the National Academy of Sciences of the United States of America, 120(27), Article e2220380120.