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Discovery of minimalistic cyclic ice binding peptides

The discovery of small ice binding peptides has been published in Nature Communications. In this work, the team used phage display - a high -throughput technique which enabled billions of short peptides to screened for their ability to bind ice crystals. This lead to the discovery a small, 14 amino acid, cyclic peptide sequence which was a potent ice growth inhibitor. This work was a collaboration with Harm-Anton Klok (EPFL Switzerland) and Dr Corey Stevens, who visited Warwick several times to undertaken much of this research. The Sosso Group at Warwick provided modelling expertise to understand how such a small peptide can bind ice. The peptide was also used as a 'CryoTag' to enable purification of proteins by a simple ice-binding process. The work is important as this peptide is easy to synthesise by solid phage peptide synthesis, allowing access for more experiments and can be easily modified for further study.

Read the paper here

A Minimalistic Cyclic Ice-Binding Peptide from Phage Display