Using phages to discover new antifreeze proteins

Using phage to discover new antifreeze proteins

Using viruses (phage display) to identify the one molecule in a billion (peptide8) that controls the formation of ice.

Controlling, and mitigating the effects of ice growth is crucial to protect infrastructure, help preserve frozen cells and to enhance texture of frozen foods. An international collaboration of Warwick scientists working with researchers from Switzerland have used a phage display platform to discover new, small, peptides which function like larger antifreeze proteins. This presents a route to new, easier to synthesize, cryoprotectants.Caption: Using viruses (phage display) to identify the one molecule in a billion (peptide8) that controls the formation of ice.

Ice binding proteins, which includes antifreeze proteins, are produced by a large range of species from fish, to insects to plants, to prevent the damage caused by ice. The proteins achieve the remarkable function of recognizing and binding to ice, even in the huge excess of water (which ice is the solid form of). New antifreeze proteins have typically been discovered by isolation from the organisms

In this work, the team took a very different approach by screening billions of possible peptides to find those which could bind to ice. This was achieved by Phage Display—a technology whereby a virus is used to generate vast numbers of peptides, and those which ‘bind’ to the ice can be isolated.

This work highlights that even very small changes within the structure of these peptides can make a huge difference in their ability to control the formation of ice. Our computer simulations allowed us to identify and understand the importance of these structural changes—which is a key step toward the rational design of synthetic cryoprotectants. Truly, Warwick is a great place to be if you want to understand how ice forms and what can we do to have a say in this process.

We have been working on developing synthetic tools to understand, and interfere with, ice growth processes with an aim of helping develop new cryoprotectants. This work was really exciting, as we made use of biotechnology tools (phage) to discover small, cyclic, peptides which are remarkably potent.

Corey A. Stevens et al, A minimalistic cyclic ice-binding peptide from phage display,Nature Communications (2021). DOI: 10.1038/s41467-021-22883-w

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