Antifreeze proteins take two roads to arrive at the same destination
DOI: 10.1063/10.0047489
Antifreeze proteins take two roads to arrive at the same destination lead image
Antifreeze proteins (AFPs), like their name implies, prevent freezing in organisms by inhibiting ice crystal growth. They can function at low concentrations and have already been explored as additives in foods ranging from meat to ice cream.
Interestingly, AFPs from fish and insects have evolved differently, meaning the proteins have the same function but do so via different mechanisms. This results in different structure-function relationships.
Ran Drori and Amish Patel summarized two types of AFP — hyperactive AFPs from insects and moderately active AFPs from fish — to understand the field of AFP research.
AFPs inhibit growth kinetically: They latch on to ice crystals and inhibit further icing. Insects are exposed to lower temperatures and greater fluctuations than fish, so hAFPs still function at lower temperatures than mAFPs.
Beyond the difference in temperature functions, mAFPs and hAFPs interact with ice differently, leading to different failure states when the proteins can no longer suppress ice growth.
Because AFPs operate in lower concentrations than traditional antifreeze techniques that use salt or dimethyl sulfoxide, Drori is already using them in his lab for food preservation.
“The similar behavior we’ve measured in foundational experiments — we see a mirror image of that in applications,” he said. “Now it’s easier to decipher the experiments in inside [of] food using the knowledge that we obtained in the fundamental and basic experiments.”
The authors also outline experiments to further characterize the de-icing mechanisms of AFP proteins in the paper, which Drori and Patel hope will inspire people to join the field.
“I want more people to study these proteins,” Drori said. “That’s my main goal.”
Source: “Different paths, same purpose: How antifreeze proteins stop ice crystals from growing,” by Ran Drori and Amish J. Patel, Journal of Chemical Physics (2026). The article can be accessed at https://doi.org/10.1063/5.0339028 .
