Advanced materials (Deerfield Beach, Fla.)Aug 29, 2025

A Highly Effective and Cost-Efficient Antifreeze Protein

Longevity & Aging Weekly Brief ↗PubMed ↗DOI ↗OA ↗

Updated Jan 2, 2026

Abstract

Antifreeze polypeptides that inhibit ice crystal growth are effective at µg concentrations.

The polypeptides are made from the amino acids alanine (Ala) and glutamic acid (Glu).
They remain stable after thermal events and are biodegradable and nontoxic to human cells.
Mirror-image versions of these polypeptides resist degradation and are suited for long-lasting applications.
The α-helical shape of the polypeptides contributes to their ability to prevent ice crystal growth, while their chirality does not impact this function.
In initial tests, the polypeptides prevented damage to model protein therapeutics during freeze-thaw cycles and showed potential for use in frozen food products.

Simplified

The growth of large ice crystals during freeze and thaw events is a challenge in diverse settings from transportation and agriculture to foods and biomedicine. Design, synthesis, and evaluation of antifreeze polypeptides that inhibit ice crystal growth at µg concentrations are reported herein. The polypeptides, composed of Ala and Glu, are prepared using economical methodology, are stable after thermal events, are biodegradable, and are nontoxic to human cells. Mirror-image polypeptides have resisted degradation and are suitable for applications with a longevity criterion. Their α-helical conformation plays a role in antifreeze activity, but chirality does not. In proof-of-concept experiments, the antifreeze polypeptides could prevent damage to model protein therapeutics during repeated freeze-thaw cycles and could be applied to prevent large ice crystals in a frozen food product. These simple, economical Ala/Glu polypeptides are promising materials for diverse antifreeze applications, particularly in biological settings.